Production, purification and characterization of recombinant human R-spondin1 (RSPO1) protein stably expressed in human HEK293 cells
Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, n...
Saved in:
| Published in | BMC biotechnology Vol. 20; no. 1; p. 5 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
BioMed Central
20.01.2020
BioMed Central Ltd BMC |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1472-6750 1472-6750 |
| DOI | 10.1186/s12896-020-0600-0 |
Cover
| Abstract | Background
The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygro
r
and subjected to cell clones isolation.
Results
rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose.
Conclusion
Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. |
|---|---|
| AbstractList | Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic [beta]-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygro.sup.r and subjected to cell clones isolation. Results rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Conclusion Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. Keywords: Tissue engineering, Heterologous mammalian protein expression system, Recombinant human R-spondin1 (RSPO1), Peptide growth factors, HEK293 cells Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygror and subjected to cell clones isolation. Results rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Conclusion Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic [beta]-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygro.sup.r and subjected to cell clones isolation. rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygror and subjected to cell clones isolation.BACKGROUNDThe R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygror and subjected to cell clones isolation.rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose.RESULTSrhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose.Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering.CONCLUSIONTherefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. Abstract Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygror and subjected to cell clones isolation. Results rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Conclusion Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygro and subjected to cell clones isolation. rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. BACKGROUND: The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygroʳ and subjected to cell clones isolation. RESULTS: rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. CONCLUSION: Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing the Wnt pathway. Several studies have demonstrated the importance of RSPOs in regulation of a number of tissue-specific processes, namely: bone formation, skeletal muscle tissue development, proliferation of pancreatic β-cells and intestinal stem cells and even cancer. RSPO1 stands out among RSPOs molecules with respect to its potential therapeutic use, especially in the Regenerative Medicine field, due to its mitogenic activity in stem cells. Here, we generated a recombinant human RSPO1 (rhRSPO1) using the HEK293 cell line, obtaining a purified, characterized and biologically active protein product to be used in Cell Therapy. The hRSPO1 coding sequence was synthesized and subcloned into a mammalian cell expression vector. HEK293 cells were stably co-transfected with the recombinant expression vector containing the hRSPO1 coding sequence and a hygromycin resistance plasmid, selected for hygro r and subjected to cell clones isolation. Results rhRSPO1 was obtained, in the absence of serum, from culture supernatants of transfected HEK293 cells and purified using a novel purification strategy, involving two sequential chromatographic steps, namely: heparin affinity chromatography, followed by a molecular exclusion chromatography, designed to yield a high purity product. The purified protein was characterized by Western blotting, mass spectrometry and in vitro (C2C12 cells) and in vivo (BALB/c mice) biological activity assays, confirming the structural integrity and biological efficacy of this human cell expression system. Furthermore, rhRSPO1 glycosylation analysis allowed us to describe, for the first time, the glycan composition of this oligosaccharide chain, confirming the presence of an N-glycosylation in residue Asn137 of the polypeptide chain, as previously described. In addition, this analysis revealing the presence of glycan structures such as terminal sialic acid, N-acetylglucosamine and/or galactose. Conclusion Therefore, a stable platform for the production and purification of recombinant hRSPO1 from HEK293 cells was generated, leading to the production of a purified, fully characterized and biologically active protein product to be applied in Tissue Engineering. |
| ArticleNumber | 5 |
| Audience | Academic |
| Author | Carreira, Ana Claudia Oliveira Sogayar, Mari Cleide Levin, Gabriel Koga, Bruna Andrade Aguiar Belchior, Gustavo Gross |
| Author_xml | – sequence: 1 givenname: Gabriel surname: Levin fullname: Levin, Gabriel organization: Cell and Molecular Therapy Center (NUCEL), Medical School, University of São Paulo – sequence: 2 givenname: Bruna Andrade Aguiar surname: Koga fullname: Koga, Bruna Andrade Aguiar organization: Cell and Molecular Therapy Center (NUCEL), Medical School, University of São Paulo, Department of Surgery, School of Veterinary Medicine and Animal Science, University of Sao Paulo – sequence: 3 givenname: Gustavo Gross surname: Belchior fullname: Belchior, Gustavo Gross organization: Cell and Molecular Therapy Center (NUCEL), Medical School, University of São Paulo – sequence: 4 givenname: Ana Claudia Oliveira surname: Carreira fullname: Carreira, Ana Claudia Oliveira email: ancoc@iq.usp.br, anaclaudiaoli@gmail.com organization: Cell and Molecular Therapy Center (NUCEL), Medical School, University of São Paulo, Department of Surgery, School of Veterinary Medicine and Animal Science, University of Sao Paulo – sequence: 5 givenname: Mari Cleide orcidid: 0000-0003-4805-4609 surname: Sogayar fullname: Sogayar, Mari Cleide email: mcsogayar@gmail.com, mcsoga@iq.usp.br organization: Cell and Molecular Therapy Center (NUCEL), Medical School, University of São Paulo, Biochemistry Department, Chemistry Institute, University of São Paulo |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31959207$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNk0tv1DAUhSNURB_wA9igSGxaiRS_YjsbpKoqdNRKU02BreXYztRVxg52Ai1rfjieZmg7FaBRpMS5-c7JtY-9m20570yWvYbgEEJO30eIeEULgEABKEi3Z9kOJAwVlJVg69F4O9uN8RoAyDigL7JtDKuyQoDtZL8ugteD6q137_JuCLaxSi7fcul0rq5kkKo3wf4ci77Jg1F-UVsnXZ9fDQvp8lkRO--0dTDfn11eTOFB3gXfG-vy2Mu6vc3NTRdMjEbnqTaKTk_OUIVzZdo2vsyeN7KN5tXquZd9-Xjy-fi0OJ9-mhwfnReKYd4XVYkh1bpUCmmgKMKaYIMg5jVNEwVM14AoiBWrJSBMK6orTTgpEShLQGiJ97LJ6Ku9vBZdsAsZboWXVtwVfJgLGXqrWiMMaiivSYUgTx4Y8qqGlEENAaprSFDyQqPX4Dp5-0O27b0hBGIZjxjjESkesYxHgCT6MIq6oV4YrYzrg2zXOln_4uyVmPvvglYMVowlg_2VQfDfBhN7sbBxuYbSGT9EgTDnLPUJyAYowQBXnC_n8vYJeu2H4FIUiSoZIgBW_IGay7RA1jU-taiWpuKIQp4SIGWVqMO_UOnSZmFV2r-NTfU1wcGaIDG9uenncohRnF1MNmYnl7PN2enXdfbN41zuA_lzThIAR0AFH2MwzUZhsycaZfu7Y5RWxLb_Va72Vkx_cXMTHvL4t-g3oBY_eg |
| CitedBy_id | crossref_primary_10_1016_j_bbrep_2020_100874 crossref_primary_10_1016_j_bej_2024_109279 crossref_primary_10_1002_bit_28414 crossref_primary_10_3389_fbioe_2020_00476 crossref_primary_10_3390_biom12010003 |
| Cites_doi | 10.1016/j.cellsig.2009.02.001 10.4161/epi.5.6.12179 10.1086/509789 10.1074/jbc.M508324200 10.1038/sj.jid.5701078 10.1021/bi401090h 10.1016/j.bbaexp.2003.10.009 10.1002/humu.20665 10.1242/dev.01522 10.1021/cr990076h 10.1186/gb-2012-13-3-242 10.1016/j.ydbio.2006.08.018 10.1093/glycob/cwi060 10.1038/leu.2008.130 10.2741/2076 10.1073/pnas.0702305104 10.1074/jbc.M706105200 10.1042/bj3360647 10.1016/j.modgep.2006.08.006 10.1038/embor.2011.175 10.1053/j.gastro.2007.02.001 10.1128/MCB.4.12.2929 10.1074/jbc.M701927200 10.1016/j.drudis.2010.06.009 10.1038/sj.jid.5701088 10.3892/ol.2016.4425 10.1038/nature07935 10.1016/j.devcel.2004.07.019 10.1242/dev.027284 10.1038/nbt1252 10.1038/nature10337 10.1074/jbc.M110.129874 10.1038/nature22313 10.1242/dev.033910 10.1158/0008-5472.CAN-17-0219 10.1007/s00018-007-7471-6 10.1038/nrm3383 10.3109/07388551.2015.1084266 10.1101/gad.219360.113 10.1038/nm.1951 10.1177/2472555216683651 10.3389/fimmu.2018.02807 10.1038/nature11019 10.1371/journal.ppat.1000879 10.1038/nbt.2361 10.1101/cshperspect.a002881 10.1091/mbc.e08-02-0187 10.1016/j.cellsig.2011.09.023 10.1126/science.1177808 10.1038/ng1883 10.1073/pnas.1106083108 10.1007/s12033-016-9939-9 10.6026/97320630003119 10.1242/dev.013359 10.1126/science.1112521 10.1016/S0723-2020(11)80089-5 10.3390/ijms17060937 10.1016/S0021-9258(18)35712-0 10.1016/j.ydbio.2007.08.023 10.1016/j.febslet.2008.01.035 10.1007/s12033-010-9287-0 10.1016/j.devcel.2011.01.006 10.1016/j.febslet.2013.11.035 10.1038/ng1907 10.1074/jbc.M008073200 |
| ContentType | Journal Article |
| Copyright | The Author(s). 2020 COPYRIGHT 2020 BioMed Central Ltd. 2020. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
| Copyright_xml | – notice: The Author(s). 2020 – notice: COPYRIGHT 2020 BioMed Central Ltd. – notice: 2020. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
| DBID | C6C AAYXX CITATION NPM IOV ISR KPI 3V. 7QO 7TB 7U5 7X7 7XB 88E 8AO 8FD 8FE 8FG 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA ARAPS AZQEC BBNVY BENPR BGLVJ BHPHI CCPQU DWQXO FR3 FYUFA GHDGH GNUQQ HCIFZ K9. L7M LK8 M0S M1P M7P P5Z P62 P64 PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS 7X8 7S9 L.6 5PM ADTOC UNPAY DOA |
| DOI | 10.1186/s12896-020-0600-0 |
| DatabaseName | Springer Nature OA Free Journals CrossRef PubMed Gale In Context: Opposing Viewpoints Gale In Context: Science Gale In Context: Global Issues ProQuest Central (Corporate) Biotechnology Research Abstracts Mechanical & Transportation Engineering Abstracts Solid State and Superconductivity Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) ProQuest Pharma Collection Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni Edition) ProQuest One Sustainability ProQuest Central UK/Ireland Advanced Technologies & Aerospace Collection ProQuest Central Essentials Biological Science Collection ProQuest Central Technology Collection Natural Science Collection ProQuest One Community College ProQuest Central Korea Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Advanced Technologies Database with Aerospace ProQuest Biological Science Collection Health & Medical Collection (Alumni Edition) Medical Database Biological Science Database Advanced Technologies & Aerospace Database ProQuest Advanced Technologies & Aerospace Collection Biotechnology and BioEngineering Abstracts ProQuest Central Premium ProQuest One Academic (New) Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) Unpaywall for CDI: Periodical Content Unpaywall DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef PubMed Publicly Available Content Database ProQuest Central Student ProQuest Advanced Technologies & Aerospace Collection ProQuest Central Essentials SciTech Premium Collection ProQuest Central China ProQuest One Applied & Life Sciences ProQuest One Sustainability Health Research Premium Collection Natural Science Collection Health & Medical Research Collection Biological Science Collection ProQuest Central (New) ProQuest Medical Library (Alumni) Advanced Technologies & Aerospace Collection ProQuest Biological Science Collection ProQuest One Academic Eastern Edition ProQuest Hospital Collection ProQuest Technology Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Solid State and Superconductivity Abstracts Engineering Research Database ProQuest One Academic ProQuest One Academic (New) Technology Collection Technology Research Database ProQuest One Academic Middle East (New) Mechanical & Transportation Engineering Abstracts ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Central ProQuest Health & Medical Research Collection Biotechnology Research Abstracts Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Advanced Technologies Database with Aerospace ProQuest SciTech Collection Advanced Technologies & Aerospace Database ProQuest Medical Library ProQuest Central (Alumni) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | Publicly Available Content Database MEDLINE - Academic PubMed AGRICOLA |
| Database_xml | – sequence: 1 dbid: C6C name: Springer Nature OA Free Journals (Selected full-text) url: http://www.springeropen.com/ sourceTypes: Publisher – sequence: 2 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 3 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 4 dbid: UNPAY name: Unpaywall url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/ sourceTypes: Open Access Repository – sequence: 5 dbid: 8FG name: ProQuest Technology Collection url: https://search.proquest.com/technologycollection1 sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Engineering Chemistry Medicine |
| EISSN | 1472-6750 |
| EndPage | 5 |
| ExternalDocumentID | oai_doaj_org_article_e2f68b49218d483189b1671d102bb142 10.1186/s12896-020-0600-0 PMC6971977 A618720459 31959207 10_1186_s12896_020_0600_0 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GeographicLocations | Brazil |
| GeographicLocations_xml | – name: Brazil |
| GrantInformation_xml | – fundername: Conselho Nacional de Desenvolvimento Científico e Tecnológico grantid: 3118/2015-6 funderid: http://dx.doi.org/10.13039/501100003593 – fundername: Fundação de Amparo à Pesquisa do Estado de São Paulo grantid: grant number 2015/11128-3; 2017/01072-6; 2016/05311-2 (Thematic Project) funderid: http://dx.doi.org/10.13039/501100001807 – fundername: CAPES grantid: 88882.315613/2019-01; 88882.327814/2019-01 – fundername: BNDES grantid: 09.2.1066.1 – fundername: Financiadora de Estudos e Projetos grantid: 01.08.0622.05 funderid: http://dx.doi.org/10.13039/501100004809 – fundername: Ministério da Ciência, Tecnologia, Inovações e Comunicações funderid: http://dx.doi.org/10.13039/501100011875 – fundername: MS-DECIT – fundername: ; grantid: grant number 2015/11128-3; 2017/01072-6; 2016/05311-2 (Thematic Project) – fundername: ; – fundername: ; grantid: 88882.315613/2019-01; 88882.327814/2019-01 – fundername: ; grantid: 01.08.0622.05 – fundername: ; grantid: 09.2.1066.1 – fundername: ; grantid: 3118/2015-6 |
| GroupedDBID | --- 0R~ 23N 2WC 53G 5GY 5VS 6J9 7X7 88E 8AO 8FE 8FG 8FH 8FI 8FJ A8Z AAFWJ AAHBH AAJSJ AASML ABDBF ABUWG ACGFO ACGFS ACIHN ACIWK ACPRK ACUHS ADBBV ADMLS ADRAZ ADUKV AEAQA AENEX AEUYN AFKRA AFPKN AFRAH AHBYD AHMBA AHYZX ALMA_UNASSIGNED_HOLDINGS AMKLP AMTXH AOIJS ARAPS BAPOH BAWUL BBNVY BCNDV BENPR BFQNJ BGLVJ BHPHI BMC BPHCQ BVXVI C6C CCPQU CS3 DIK DU5 E3Z EAD EAP EAS EBD EBLON EBS EMB EMK EMOBN ESTFP ESX F5P FYUFA GROUPED_DOAJ GX1 HCIFZ HH5 HMCUK HYE I-F IAG IAO IHR INH INR IOV ISR ITC ITG ITH KPI KQ8 LK8 M1P M48 M7P ML0 M~E O5R O5S OK1 OVT P2P P62 PGMZT PHGZM PHGZT PIMPY PJZUB PPXIY PQGLB PQQKQ PROAC PSQYO PUEGO RBZ RNS ROL RPM RSV RVI SCM SOJ SV3 TR2 TUS UKHRP W2D WOQ WOW XSB AAYXX CITATION -A0 3V. ACRMQ ADINQ ALIPV C24 NPM PMFND 7QO 7TB 7U5 7XB 8FD 8FK AZQEC DWQXO FR3 GNUQQ K9. L7M P64 PKEHL PQEST PQUKI PRINS 7X8 7S9 L.6 5PM 2VQ 4.4 ADTOC AHSBF C1A EJD H13 IPNFZ RIG UNPAY |
| ID | FETCH-LOGICAL-c738t-95316dd5cc2d0c623d43e2138b647207db04c13c7ba047dc6d9d4845205504653 |
| IEDL.DBID | DOA |
| ISSN | 1472-6750 |
| IngestDate | Wed Aug 27 01:29:55 EDT 2025 Wed Aug 20 00:03:33 EDT 2025 Tue Sep 30 16:36:54 EDT 2025 Wed Oct 01 13:25:19 EDT 2025 Wed Oct 01 14:20:41 EDT 2025 Fri Jul 25 19:24:12 EDT 2025 Tue Jun 17 21:48:20 EDT 2025 Tue Jun 10 20:32:56 EDT 2025 Fri Jun 27 04:17:46 EDT 2025 Fri Jun 27 03:45:23 EDT 2025 Fri Jun 27 04:01:43 EDT 2025 Wed Feb 19 02:31:33 EST 2025 Thu Apr 24 22:59:02 EDT 2025 Wed Oct 01 01:52:04 EDT 2025 Sat Sep 06 07:29:56 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | Heterologous mammalian protein expression system HEK293 cells Tissue engineering Peptide growth factors Recombinant human R-spondin1 (RSPO1) |
| Language | English |
| License | Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. cc-by |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c738t-95316dd5cc2d0c623d43e2138b647207db04c13c7ba047dc6d9d4845205504653 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| ORCID | 0000-0003-4805-4609 |
| OpenAccessLink | https://doaj.org/article/e2f68b49218d483189b1671d102bb142 |
| PMID | 31959207 |
| PQID | 2357240198 |
| PQPubID | 44068 |
| PageCount | 1 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_e2f68b49218d483189b1671d102bb142 unpaywall_primary_10_1186_s12896_020_0600_0 pubmedcentral_primary_oai_pubmedcentral_nih_gov_6971977 proquest_miscellaneous_2388767104 proquest_miscellaneous_2343039882 proquest_journals_2357240198 gale_infotracmisc_A618720459 gale_infotracacademiconefile_A618720459 gale_incontextgauss_KPI_A618720459 gale_incontextgauss_ISR_A618720459 gale_incontextgauss_IOV_A618720459 pubmed_primary_31959207 crossref_primary_10_1186_s12896_020_0600_0 crossref_citationtrail_10_1186_s12896_020_0600_0 springer_journals_10_1186_s12896_020_0600_0 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2020-01-20 |
| PublicationDateYYYYMMDD | 2020-01-20 |
| PublicationDate_xml | – month: 01 year: 2020 text: 2020-01-20 day: 20 |
| PublicationDecade | 2020 |
| PublicationPlace | London |
| PublicationPlace_xml | – name: London – name: England |
| PublicationTitle | BMC biotechnology |
| PublicationTitleAbbrev | BMC Biotechnol |
| PublicationTitleAlternate | BMC Biotechnol |
| PublicationYear | 2020 |
| Publisher | BioMed Central BioMed Central Ltd BMC |
| Publisher_xml | – name: BioMed Central – name: BioMed Central Ltd – name: BMC |
| References | K Blochlinger (600_CR62) 1984; 4 S Tomaselli (600_CR8) 2008; 29 Y Ishii (600_CR18) 2008; 128 J Lubbers (600_CR56) 2018; 9 O Kazanskaya (600_CR4) 2004; 7 JK Yoon (600_CR5) 2012; 24 KW Moremen (600_CR54) 2012; 13 JC Bustos-Valenzuela (600_CR65) 2010; 46 W de Lau (600_CR48) 2007; 12 M Tsuchiya (600_CR51) 2016; 11 M Tsuchiya (600_CR40) 2016; 11 A Fico (600_CR46) 2011; 68 C Bergmann (600_CR15) 2006; 79 T Sato (600_CR49) 2009; 459 M Aoki (600_CR13) 2007; 301 DC Blaydon (600_CR16) 2006; 38 E Cadieu (600_CR12) 2009; 326 A Glinka (600_CR27) 2011; 12 X Zhou (600_CR60) 2017; 77 MA Demasi (600_CR61) 2016; 58 KS Carmon (600_CR26) 2011; 108 T Chitlaru (600_CR43) 1998; 336 O Kazanskaya (600_CR14) 2008; 135 B Ohkawara (600_CR24) 2011; 20 JS Nam (600_CR19) 2006; 281 Z Liu (600_CR36) 2008; 283 L Ayadi (600_CR23) 2008; 3 W Lu (600_CR47) 2008; 582 SM Bell (600_CR10) 2008; 135 HX Hao (600_CR30) 2012; 485 HE Moad (600_CR52) 2013; 52 S Legardinier (600_CR66) 2005; 15 KA Kim (600_CR31) 2005; 309 R van Amerongen (600_CR2) 2009; 136 ME Binnerts (600_CR29) 2007; 104 X Lin (600_CR45) 2004; 131 S Ley (600_CR34) 2017; 22 KA Kim (600_CR20) 2008; 19 J Zhao (600_CR35) 2007; 132 Q Wei (600_CR28) 2007; 282 SQ Kuang (600_CR38) 2008; 22 NO Brüchle (600_CR17) 2008; 128 P Parma (600_CR7) 2006; 38 J Hofsteenge (600_CR58) 2001; 276 KM Cadigan (600_CR1) 2009; 1 JS Nam (600_CR9) 2007; 7 WG Tong (600_CR39) 2010; 5 D Wang (600_CR53) 2013; 27 Chiung-Fang Chang (600_CR41) 2016; 17 T Uemori (600_CR64) 1992; 15 AD Bandaranayake (600_CR57) 2014; 588 JS Nam (600_CR11) 2007; 311 G Walsh (600_CR55) 2010; 15 A Ootani (600_CR50) 2009; 15 MJ van Vliet (600_CR33) 2010; 6 SJ Li (600_CR21) 2009; 21 KA Houck (600_CR22) 1992; 267 Kelley S. Yan (600_CR32) 2017; 545 WB de Lau (600_CR6) 2012; 13 VS Wong (600_CR37) 2010; 285 T Kamata (600_CR3) 2004; 1676 R Aebersold (600_CR67) 2001; 101 J Dumont (600_CR44) 2016; 36 W de Lau (600_CR25) 2011; 476 G Walsh (600_CR42) 2006; 24 A Abo (600_CR59) 2012; 30 E Costanzi (600_CR63) 1990; 23 |
| References_xml | – volume: 21 start-page: 916 issue: 6 year: 2009 ident: 600_CR21 publication-title: Cell Signal doi: 10.1016/j.cellsig.2009.02.001 – volume: 5 start-page: 499 issue: 6 year: 2010 ident: 600_CR39 publication-title: Epigenetics doi: 10.4161/epi.5.6.12179 – volume: 79 start-page: 1105 issue: 6 year: 2006 ident: 600_CR15 publication-title: Am J Hum Genet doi: 10.1086/509789 – volume: 281 start-page: 13247 issue: 19 year: 2006 ident: 600_CR19 publication-title: J Biol Chem doi: 10.1074/jbc.M508324200 – volume: 128 start-page: 867 issue: 4 year: 2008 ident: 600_CR18 publication-title: J Invest Dermatol doi: 10.1038/sj.jid.5701078 – volume: 52 start-page: 7295 issue: 41 year: 2013 ident: 600_CR52 publication-title: Biochemistry doi: 10.1021/bi401090h – volume: 1676 start-page: 51 issue: 1 year: 2004 ident: 600_CR3 publication-title: Biochim Biophys Acta doi: 10.1016/j.bbaexp.2003.10.009 – volume: 29 start-page: 220 issue: 2 year: 2008 ident: 600_CR8 publication-title: Hum Mutat doi: 10.1002/humu.20665 – volume: 131 start-page: 6009 issue: 24 year: 2004 ident: 600_CR45 publication-title: Development doi: 10.1242/dev.01522 – volume: 101 start-page: 269 issue: 2 year: 2001 ident: 600_CR67 publication-title: Chem Rev doi: 10.1021/cr990076h – volume: 13 start-page: 242 issue: 3 year: 2012 ident: 600_CR6 publication-title: Genome Biol doi: 10.1186/gb-2012-13-3-242 – volume: 301 start-page: 218 issue: 1 year: 2007 ident: 600_CR13 publication-title: Dev Biol doi: 10.1016/j.ydbio.2006.08.018 – volume: 15 start-page: 776 issue: 8 year: 2005 ident: 600_CR66 publication-title: Glycobiology doi: 10.1093/glycob/cwi060 – volume: 22 start-page: 1529 issue: 8 year: 2008 ident: 600_CR38 publication-title: Leukemia doi: 10.1038/leu.2008.130 – volume: 12 start-page: 471 year: 2007 ident: 600_CR48 publication-title: Front Biosci doi: 10.2741/2076 – volume: 104 start-page: 14700 issue: 37 year: 2007 ident: 600_CR29 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0702305104 – volume: 283 start-page: 8723 issue: 13 year: 2008 ident: 600_CR36 publication-title: J Biol Chem doi: 10.1074/jbc.M706105200 – volume: 336 start-page: 647 issue: Pt 3 year: 1998 ident: 600_CR43 publication-title: Biochem J doi: 10.1042/bj3360647 – volume: 7 start-page: 306 issue: 3 year: 2007 ident: 600_CR9 publication-title: Gene Expr Patterns doi: 10.1016/j.modgep.2006.08.006 – volume: 12 start-page: 1055 issue: 10 year: 2011 ident: 600_CR27 publication-title: EMBO Rep doi: 10.1038/embor.2011.175 – volume: 132 start-page: 1331 issue: 4 year: 2007 ident: 600_CR35 publication-title: Gastroenterology doi: 10.1053/j.gastro.2007.02.001 – volume: 4 start-page: 2929 issue: 12 year: 1984 ident: 600_CR62 publication-title: Mol Cell Biol doi: 10.1128/MCB.4.12.2929 – volume: 282 start-page: 15903 issue: 21 year: 2007 ident: 600_CR28 publication-title: J Biol Chem doi: 10.1074/jbc.M701927200 – volume: 15 start-page: 773 issue: 17–18 year: 2010 ident: 600_CR55 publication-title: Drug Discov Today doi: 10.1016/j.drudis.2010.06.009 – volume: 128 start-page: 791 issue: 4 year: 2008 ident: 600_CR17 publication-title: J Invest Dermatol doi: 10.1038/sj.jid.5701088 – volume: 11 start-page: 3279 issue: 5 year: 2016 ident: 600_CR51 publication-title: Oncol Lett doi: 10.3892/ol.2016.4425 – volume: 459 start-page: 262 issue: 7244 year: 2009 ident: 600_CR49 publication-title: Nature doi: 10.1038/nature07935 – volume: 7 start-page: 525 issue: 4 year: 2004 ident: 600_CR4 publication-title: Dev Cell doi: 10.1016/j.devcel.2004.07.019 – volume: 135 start-page: 3655 issue: 22 year: 2008 ident: 600_CR14 publication-title: Development doi: 10.1242/dev.027284 – volume: 24 start-page: 1241 issue: 10 year: 2006 ident: 600_CR42 publication-title: Nat Biotechnol doi: 10.1038/nbt1252 – volume: 11 start-page: 3279 issue: 5 year: 2016 ident: 600_CR40 publication-title: Oncol Lett doi: 10.3892/ol.2016.4425 – volume: 476 start-page: 293 issue: 7360 year: 2011 ident: 600_CR25 publication-title: Nature doi: 10.1038/nature10337 – volume: 285 start-page: 21292 issue: 28 year: 2010 ident: 600_CR37 publication-title: J Biol Chem doi: 10.1074/jbc.M110.129874 – volume: 23 start-page: 795 issue: 9 year: 1990 ident: 600_CR63 publication-title: Braz J Med Biol Res – volume: 545 start-page: 238 issue: 7653 year: 2017 ident: 600_CR32 publication-title: Nature doi: 10.1038/nature22313 – volume: 136 start-page: 3205 issue: 19 year: 2009 ident: 600_CR2 publication-title: Development doi: 10.1242/dev.033910 – volume: 77 start-page: 6589 issue: 23 year: 2017 ident: 600_CR60 publication-title: Cancer Res doi: 10.1158/0008-5472.CAN-17-0219 – volume: 68 start-page: 923 issue: 6 year: 2011 ident: 600_CR46 publication-title: Cell Mol Life Sci doi: 10.1007/s00018-007-7471-6 – volume: 13 start-page: 448 issue: 7 year: 2012 ident: 600_CR54 publication-title: Nat Rev Mol Cell Biol doi: 10.1038/nrm3383 – volume: 36 start-page: 1110 issue: 6 year: 2016 ident: 600_CR44 publication-title: Crit Rev Biotechnol doi: 10.3109/07388551.2015.1084266 – volume: 27 start-page: 1339 issue: 12 year: 2013 ident: 600_CR53 publication-title: Genes Dev doi: 10.1101/gad.219360.113 – volume: 15 start-page: 701 issue: 6 year: 2009 ident: 600_CR50 publication-title: Nat Med doi: 10.1038/nm.1951 – volume: 22 start-page: 571 issue: 5 year: 2017 ident: 600_CR34 publication-title: SLAS Discov doi: 10.1177/2472555216683651 – volume: 9 start-page: 2807 year: 2018 ident: 600_CR56 publication-title: Front Immunol doi: 10.3389/fimmu.2018.02807 – volume: 485 start-page: 195 issue: 7397 year: 2012 ident: 600_CR30 publication-title: Nature doi: 10.1038/nature11019 – volume: 6 issue: 5 year: 2010 ident: 600_CR33 publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000879 – volume: 30 start-page: 835 issue: 9 year: 2012 ident: 600_CR59 publication-title: Nat Biotechnol doi: 10.1038/nbt.2361 – volume: 1 start-page: a002881 issue: 2 year: 2009 ident: 600_CR1 publication-title: Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a002881 – volume: 19 start-page: 2588 issue: 6 year: 2008 ident: 600_CR20 publication-title: Mol Biol Cell doi: 10.1091/mbc.e08-02-0187 – volume: 24 start-page: 369 issue: 2 year: 2012 ident: 600_CR5 publication-title: Cell Signal doi: 10.1016/j.cellsig.2011.09.023 – volume: 326 start-page: 150 issue: 5949 year: 2009 ident: 600_CR12 publication-title: Science doi: 10.1126/science.1177808 – volume: 38 start-page: 1245 issue: 11 year: 2006 ident: 600_CR16 publication-title: Nat Genet doi: 10.1038/ng1883 – volume: 108 start-page: 11452 issue: 28 year: 2011 ident: 600_CR26 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1106083108 – volume: 58 start-page: 404 issue: 6 year: 2016 ident: 600_CR61 publication-title: Mol Biotechnol doi: 10.1007/s12033-016-9939-9 – volume: 3 start-page: 119 issue: 3 year: 2008 ident: 600_CR23 publication-title: Bioinformation doi: 10.6026/97320630003119 – volume: 135 start-page: 1049 issue: 6 year: 2008 ident: 600_CR10 publication-title: Development doi: 10.1242/dev.013359 – volume: 309 start-page: 1256 issue: 5738 year: 2005 ident: 600_CR31 publication-title: Science doi: 10.1126/science.1112521 – volume: 15 start-page: 181 issue: 2 year: 1992 ident: 600_CR64 publication-title: Syst Appl Microbiol doi: 10.1016/S0723-2020(11)80089-5 – volume: 17 start-page: 937 issue: 6 year: 2016 ident: 600_CR41 publication-title: International Journal of Molecular Sciences doi: 10.3390/ijms17060937 – volume: 267 start-page: 26031 issue: 36 year: 1992 ident: 600_CR22 publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)35712-0 – volume: 311 start-page: 124 issue: 1 year: 2007 ident: 600_CR11 publication-title: Dev Biol doi: 10.1016/j.ydbio.2007.08.023 – volume: 582 start-page: 643 issue: 5 year: 2008 ident: 600_CR47 publication-title: FEBS Lett doi: 10.1016/j.febslet.2008.01.035 – volume: 46 start-page: 118 issue: 2 year: 2010 ident: 600_CR65 publication-title: Mol Biotechnol doi: 10.1007/s12033-010-9287-0 – volume: 20 start-page: 303 issue: 3 year: 2011 ident: 600_CR24 publication-title: Dev Cell doi: 10.1016/j.devcel.2011.01.006 – volume: 588 start-page: 253 issue: 2 year: 2014 ident: 600_CR57 publication-title: FEBS Lett doi: 10.1016/j.febslet.2013.11.035 – volume: 38 start-page: 1304 issue: 11 year: 2006 ident: 600_CR7 publication-title: Nat Genet doi: 10.1038/ng1907 – volume: 276 start-page: 6485 issue: 9 year: 2001 ident: 600_CR58 publication-title: J Biol Chem doi: 10.1074/jbc.M008073200 |
| SSID | ssj0017806 |
| Score | 2.277821 |
| Snippet | Background
The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by... The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by inducing... Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by... BACKGROUND: The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and death, by... Abstract Background The R-Spondin proteins comprise a family of secreted proteins, known for their important roles in cell proliferation, differentiation and... |
| SourceID | doaj unpaywall pubmedcentral proquest gale pubmed crossref springer |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 5 |
| SubjectTerms | Affinity chromatography Analysis Anticoagulants Applied Microbiology Beta cells bioactive properties Biochemical Engineering Biological activity Biomedical Engineering/Biotechnology Biotechnology blood serum bone formation Bone growth Cell culture Cell death Cell differentiation Cell proliferation Cell therapy Chains Chemistry Chemistry and Materials Science Chromatography clones Cloning Coding Galactose gel chromatography Genetic Engineering Genetic engineering in animals and animal cell systems genetic vectors Glycan Glycosylation HEK293 cells Heparin Heterologous mammalian protein expression system Human cell culture human cell lines humans Hygromycin Identification and classification Intestine intestines islets of Langerhans Mass spectrometry Mass spectroscopy medicine Methods mice Muscles N-Acetylglucosamine neoplasms Oligosaccharides Osteogenesis Pancreas Peptide growth factors Plant Breeding/Biotechnology plasmids Polypeptides Production processes Protein purification protein secretion Proteins Purification Recombinant human R-spondin1 (RSPO1) Recombinant proteins Regenerative medicine Research Article sialic acid Signal transduction Skeletal muscle Stem cell transplantation Stem cells Structural integrity therapeutics Tissue engineering Western blotting |
| SummonAdditionalLinks | – databaseName: ProQuest Technology Collection dbid: 8FG link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwhV1Lb9QwELagHKAHxJtAQQYh8ShR7cRxkhMqqEtLBV1tadWbFT-2VFqSZR-C3vnhzDjZdANie43H0q7n7Rl_Q8iLJM0dk4ULmeAmFI7nYSEKG2rJhkUeJZnWeKH_-YvcPRKfTpKT5sJt2rRVLmyiN9S2MnhHvoWwLOB9IEd-N_4R4tQorK42IzSukms8AknCl-K9j20VIc2YbCqZPJNbU7DFvuUWR63gg-qOL_KQ_f8a5iXP9HfXZFs6XSfX5-W4OP9ZjEZL3ql3i9xswkq6XcvBbXLFlXfI-hLY4F3yu1-DuwIj3tLxfII9Qp4ttCgtNS1wc_0uk1ZDisnyd-1bZaif5UcHIXbUgrvj9NXgsH_AX1MP9HBWUogy9eicul--s9ZZCt_qTbs7--DtKZYIpvfIUW_n64fdsJnBEJo0zmZY3eXS2sSYyDIDsZIVsYt4nGnEnWep1UwYHptUF0yk1kibW5GJJGKQ-iB2232yVlale0iozm1mwZ5JJ42wQ1akzoK9tTJKpYu5DghbcEOZBqAc52SMlE9UMqlqBipgoEIGKhaQN-2WcY3OsYr4PbK4JURgbf-hmpyqRk-Vi4Yy0yKHyAf-Bxi8XHOZcgtxmMb7soA8RwFRCJ1RYm_OaTGfTtXewbHaljzDkT9J_j-iw8HlRPv9vQ7Ry4ZoWMFZmKJ5NAEnirhdHcqNDiVYCdNdXki0aqzUVF3oVECetcu4EzvvSlfNkUZAlJNDIraKBlwVnBITAXlQK0l7yjGiF4GgBCTtqE-HDd2V8uybxzmXecohPQnI5kLRLn76Ci5vtrp4uUw8Wn0sj8mNyJsLDt5kg6zNJnP3BILQmX7qLc0f88x_1w priority: 102 providerName: ProQuest – databaseName: Scholars Portal Journals: Open Access dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZKOUAPiDeBggxC4lECduJ1kgNCBbXaUpWu2i7qzYofWyot2WUfonvnhzPjZNMNlO2FazyWEs87M_6GkOetJHNM5i5kgptQOJ6FuchtqCXr5VnUSrXGH_p7X2S7Kz4ft45XyHy8VXWA4wtTO5wn1R313579mH0AhX_vFT6V78ZgY30rLY5QwYvSV8hVcEwRCvmeOC8qJCmTVWHzwm0N1-QR_P-20wuO6s8myrqSukauTYthPvuZ9_sLzmr7JrlRRZl0sxSLW2TFFbfJ2gL24B3yq1NivQJf3tDhdIQtQ55LNC8sNTWOc3lNkw56FHPn79p3zlA_2o8ehNhgC96P05cHh519_op63IfTgkLQqfsz6s58o62zFJ6Vm9pbu-D8KVYMxndJd3vr6FM7rEYyhCaJ0wkWe7m0tmVMZJmB0MmK2EU8TjXC0LPEaiYMj02icyYSa6TNrEhFK2KQCSGU2z2yWgwK94BQndnUgnmTThpheyxPnAXza2WUSBdzHRA254YyFV45js3oK5-3pFKVDFTAQIUMVCwgr-stwxKsYxnxR2RxTYg42_7BYHSiKrVVLurJVIsMAiH4DrB_meYy4RbCMo2_zwLyDAVEIZJGga06J_l0PFY7-1_VpuQpTgBqZf8iOjy4nGi3s9MgelER9QZwFiav7lDAiSKMV4NyvUEJRsM0l-cSreY6pxD5CAI8nqUBeVov405sxCvcYIo0AoKeDPKyZTTgueCUmAjI_VJJ6lOOEcwIBCUgSUN9GmxorhSn3zzsucwSDtlKQDbminb-6ku4vFHr4uUy8fB_yMQjcj3yRoWDC1onq5PR1D2GyHWin3h79BvvxY8W priority: 102 providerName: Scholars Portal – databaseName: Springer Nature OA Free Journals dbid: C6C link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1bb9MwFLZgPIw9IBi3wEAGIXEZEXbi2MnjqDZ1TLCqY2hvVnwpTCpptbaCvfPDOcdJQ8NlE6_xcdSeu3OOv0PIs0wVnsnSx0xwGwvPi7gUpYuNZKOySLLcGPyg__6D7B-LdyfZSQMWjXdhVuv3PJdvZuA_Q5ssjkfBS9BXybUM_C527_Vkry0YqJzJpmj5122dsBPQ-f_0wStB6PcGybZKukHWF9W0PP9WjscrgWjvJrnRZJB0pxb5LXLFV5tkvbcc3LZJNlYwBm-TH4Ma0xX4_5pOF2fYGhSkQcvKUdviNdfXMelkRPGM_NWEDhkaRvjRYYyNtBDlOH0xPBoc8pc04DucVhSSSzM-p_57aKj1jsKzelN_9wCCPMXKwOwOOd7b_djrx83ohdiqNJ9jUZdL5zJrE8cspEhOpD7haW4Qbp4pZ5iwPLXKlEwoZ6UrnMhFljA48SBk212yVk0qf59QU7jcgRuTXlrhRqxU3oGbdTJR0qfcRIQtJaNtg0uO4zHGOpxPcqlrYWoQpkZhahaRV-2WaQ3KcRHxWxR3S4h42uEBqJluzFP7ZCRzIwpIeOB_gJ8rDJeKO0i_DH4mi8hTVBaNiBkVtuR8Lhezmd4__KR3JM9x0k9W_IvoaHg50cFgv0P0vCEaTYAXtmzuSgBHEa6rQ7nVoQRVs93lpXbrxjnNNCIcQSLHizwiT9pl3IkNd5WfLJBGQHJTwPnrIhqIUMAlJiJyrzaYlsspghaBokREdUypI4buSnX6JcCby0JxOJVEZHtpdL9--gVS3m7t8nKdePBf735IrifBk3CIKVtkbX628I8gFZ2bx8EJ_QRynXwN priority: 102 providerName: Springer Nature – databaseName: Unpaywall dbid: UNPAY link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Zb9NAEF5B-gB94D4MBS0IiaM49Tqbtf0YUKuUijZKSVWeVt4jJWrqRDkE5ZkfzszaMXGBVEi8Wd5ZyZ6da3dnviHkRTNKbCBS6wecaZ9blvgpT42vRNBPk7AZK4UH-h_3RbvHPxw3j4t2QFgLo860Goxm-bFyfbkEfejsNjzo062x6efqHoutKVhYl0iLDVSwTPoqWRN421Qja739Tuuzqy-KQh9C48W95h_nVTyTA_D_3Uwv-amLOZTlReo6uTbPxun513Q4XPJVOzfJcPGXeYrKaX0-U3X9_QIA5H9iwy1yo4hpaSsXwtvkis3ukPUlpMO75EcnR5YFKXhLx_MJJig5maBpZqguUaPzolA66lPcqZ8pl6dDXSNB2vUxnRd8LaOvuoedA_aaOpSJQUYhxFXDc2q_ubReayi8yye1t_cg1KB4PzG9R3o725_et_2iAYSvo0Y8w6tlJoxpah2aQEOgZnjDhqwRKwS9DyKjAq5ZQ0cqDXhktDCJ4TFvhgHsuxA47j6pZaPMPiRUJSY2YEyFFZqbfpBG1oCxNyKMhG0w5ZFgsfhSF-jo2KRjKN0uKRYyZ7AEBktksAw88qacMs6hQVYRv0OJKgkR1du9GE1OZGEkpA37IlY8gbAL_gOsbaKYiJiBIFDhYZ1HnqM8SsTtyDAx6CSdT6dy9-BItgSLsd9QM_kb0WH3cqK9zm6F6GVB1B-hwKVFxQZwFEHDKpQbFUowUbo6vFAgWZjIqUScJQgnWRJ75Fk5jDMx7S-zoznScAixEtgFrqIBPwlcCrhHHuQ6WXK5gdBJICgeiSraWlmG6kg2-OJA1kUSMdgbeWRzode_Pn3FKm-Wqn-5TDz6J-rH5HrotJuBZ9sgtdlkbp9AQDxTTwtD9xN_Fas0 priority: 102 providerName: Unpaywall |
| Title | Production, purification and characterization of recombinant human R-spondin1 (RSPO1) protein stably expressed in human HEK293 cells |
| URI | https://link.springer.com/article/10.1186/s12896-020-0600-0 https://www.ncbi.nlm.nih.gov/pubmed/31959207 https://www.proquest.com/docview/2357240198 https://www.proquest.com/docview/2343039882 https://www.proquest.com/docview/2388767104 https://pubmed.ncbi.nlm.nih.gov/PMC6971977 https://bmcbiotechnol.biomedcentral.com/track/pdf/10.1186/s12896-020-0600-0 https://doaj.org/article/e2f68b49218d483189b1671d102bb142 |
| UnpaywallVersion | publishedVersion |
| Volume | 20 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVFSB databaseName: Free Full-Text Journals in Chemistry customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: HH5 dateStart: 20010101 isFulltext: true titleUrlDefault: http://abc-chemistry.org/ providerName: ABC ChemistRy – providerCode: PRVADU databaseName: BioMedCentral customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: RBZ dateStart: 20010101 isFulltext: true titleUrlDefault: https://www.biomedcentral.com/search/ providerName: BioMedCentral – providerCode: PRVAFT databaseName: Open Access Digital Library customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: KQ8 dateStart: 20010401 isFulltext: true titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html providerName: Colorado Alliance of Research Libraries – providerCode: PRVAFT databaseName: Open Access Digital Library customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: KQ8 dateStart: 20010101 isFulltext: true titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html providerName: Colorado Alliance of Research Libraries – providerCode: PRVAFT databaseName: Open Access Digital Library customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: KQ8 dateStart: 20000101 isFulltext: true titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html providerName: Colorado Alliance of Research Libraries – providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: DOA dateStart: 20000101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVEBS databaseName: EBSCOhost Academic Search Ultimate customDbUrl: https://search.ebscohost.com/login.aspx?authtype=ip,shib&custid=s3936755&profile=ehost&defaultdb=asn eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: ABDBF dateStart: 20010101 isFulltext: true titleUrlDefault: https://search.ebscohost.com/direct.asp?db=asn providerName: EBSCOhost – providerCode: PRVEBS databaseName: Inspec with Full Text customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: ADMLS dateStart: 20010101 isFulltext: true titleUrlDefault: https://www.ebsco.com/products/research-databases/inspec-full-text providerName: EBSCOhost – providerCode: PRVBFR databaseName: Free Medical Journals customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: DIK dateStart: 20010101 isFulltext: true titleUrlDefault: http://www.freemedicaljournals.com providerName: Flying Publisher – providerCode: PRVFQY databaseName: GFMER Free Medical Journals customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: GX1 dateStart: 0 isFulltext: true titleUrlDefault: http://www.gfmer.ch/Medical_journals/Free_medical.php providerName: Geneva Foundation for Medical Education and Research – providerCode: PRVHPJ databaseName: ROAD: Directory of Open Access Scholarly Resources customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: M~E dateStart: 20010101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVAQN databaseName: PubMed Central customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: RPM dateStart: 20010101 isFulltext: true titleUrlDefault: https://www.ncbi.nlm.nih.gov/pmc/ providerName: National Library of Medicine – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: 7X7 dateStart: 20090101 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: http://www.proquest.com/pqcentral?accountid=15518 eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: BENPR dateStart: 20090101 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Technology Collection customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: 8FG dateStart: 20090101 isFulltext: true titleUrlDefault: https://search.proquest.com/technologycollection1 providerName: ProQuest – providerCode: PRVFZP databaseName: Scholars Portal Journals: Open Access customDbUrl: eissn: 1472-6750 dateEnd: 20250131 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: M48 dateStart: 20011101 isFulltext: true titleUrlDefault: http://journals.scholarsportal.info providerName: Scholars Portal – providerCode: PRVAVX databaseName: HAS SpringerNature Open Access 2022 customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: AAJSJ dateStart: 20011201 isFulltext: true titleUrlDefault: https://www.springernature.com providerName: Springer Nature – providerCode: PRVAVX databaseName: Springer Nature OA Free Journals (Selected full-text) customDbUrl: eissn: 1472-6750 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0017806 issn: 1472-6750 databaseCode: C6C dateStart: 20011201 isFulltext: true titleUrlDefault: http://www.springeropen.com/ providerName: Springer Nature |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwELdgPMAeEN8ExmQQEh8jmp26tvO4TRsb07qqY1PhxYo_CpNKWq2tYO_84dwlaWhAdC-8WGp8lpq7833E598R8rKt0sBkFmImuItF4GmciczHVrJBliZtbS1-0D_qyP1T8aHf7i-0-sKasBIeuGTcZkgGUluRgivyQoMGppZLxT04RosfMND6ghubJ1PV-YHSTFZnmFzLzQlY4aLYFpus4FXqhhcqwPr_NskLPunPesn60HSV3Jzl4-zyezYcLvilvTvkdhVQ0q3yRe6SayG_R1YXYAbvk5_dEtYVRPCOjmcXWB1UCIRmuaeuhmwub2TS0YBimvzNFkUytOjiR3sx1tKCo-P0de-ke8zf0ALi4TynEF_a4SUNP4qa2uApPCsX7e8egp-neDgweUBO93Y_7uzHVfeF2KmWnuK5Lpfet51LPHMQJXnRCglvaYuI80x5y4TjLadsxoTyTvoUBCTaCYOkB1HbHpKVfJSHx4Ta1GsPlkwG6YQfsEwFD5bWy0TJ0OI2ImwuDeMqaHLskDE0RYqipSkFaECABgVoWETe1kvGJS7HMuJtFHFNiJDaxQNQNFMpmrlK0SLyAhXEIGhGjlU5X7LZZGIOjs_MluQam_20038RnfSuJjrsHjSIXlVEgxHwwmXVdQngKCJ2NSjXGpRgH1xzeq7RprJPE4MgRxDL8VRH5Hk9jSux5i4PoxnSCIhvUkjBltGAkwIuMRGRR-UmqbncQtwiUJSIqMb2aYihOZOffy0QzmWqOCQmEdmYb7Tff32JlDfqvXi1Tjz5HzrxlNxKCqPCwduskZXpxSw8gyB1atfJddVXMOq99-vkxvZup9uDXztyZ72wVDAeCQ1jb_szzJ92uluffgFK7Y7H |
| linkProvider | Directory of Open Access Journals |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwELZKOZQeEG8CBQwC8ShR7cTrJAeECrTaZftSH6g3Ez-2VFqyS7er0ju_h9_IjJNNGxDbU6_JONr1jL-ZscffEPK8lWSOydyFTHATCsezMBe5DbVkvTyLWqnWuKG_viHbe-Lzfmt_hvye3IXBssoJJnqgtgODe-RLSMsC3gdy5PfDHyF2jcLT1UkLjdIsuu70BFK20bvOJ9DviyhaXdn92A6rrgKhSeL0GM8rubS2ZUxkmQHvb0XsIh6nGpnUWWI1E4bHJtE5E4k10mZWpKIVMQjmkY0MvnuFXBUxE8jVn-zXCR5PUiark1OeyqURYL8v8cXWLniBu-H7fIuAfx3BOU_4d5VmfVQ7T-bGxTA_Pcn7_XPecPUGuV6FsXS5tLubZMYVt8j8OXLD2-TXVkkmC4p_S4fjI6xJ8mZA88JSUxNFl_dA6aBHMTn_rn1pDvW9A-l2iBW84F45fbW9s7XJX1NPLHFYUIhqdf-Uup--ktdZCs_KQe2VLkQXFI8kRnfI3qVo5y6ZLQaFu0-ozmxqAT-lk0bYHssTZwHfrYwS6WKuA8Im2lCmIkTHvhx95ROjVKpSgQoUqFCBigXkTT1kWLKBTBP-gCquBZHI2z8YHB2oCheUi3oy1SKDSAv-BwBsprlMuIW4T-P-XECeoYEopOoosBboIB-PRqqz-UUtS55ii6FW9j-hne2LhbpbnYbQy0qoN4C5MHl1SQNmFHnCGpILDUlAJdN8PbFoVaHiSJ2t4YA8rV_jSKz0K9xgjDKwsuIMEr9pMuAaYZaYCMi9cpHUsxwjWxIYSkCSxvJpqKH5pjj85nnVZZZwSIcCsjhZaGc_fYqWF-u1eLFNPJg-LU_IXHt3fU2tdTa6D8m1yEMHB0-2QGaPj8buEQTAx_qxRx1Kvl42zP0BA4a6fw |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Zb9NAEF5BK1H6gKBchgILQuIoVnft9dp-DKVRk0AbNS3q28p7pFQKTpRD0Hd-ODO2Y2qOVrx6Z61k5_bMfkPIyyhOHZOZ85ngxheOp34mMutryYZZGkSJ1vhB_9O-3DsW3ZPopJpzOlt2uy9LkuWdBkRpyufbEzssVTyR2zOwqkXzLA5NwavR18lqEqUSsq_VVqs76NaFhDhhsipm_nVjwx0VqP1_2uYLzun3xsm6erpO1hb5JDv_lo1GFxxU-za5VUWWtFWKwh1yzeUbZG1nOdBtg6xfwB68S370S6xX4Ms7OllMsWWo4BLNcktNjeNcXtOk4yHF3PmrLjpnaDHajx762GAL3o_T14eD_gF_Qwvch7OcQtCpR-fUfS8abZ2l8KzctLfbA-dPsWIwu0eO27tHO3t-NZLBN3GYzLHYy6W1kTGBZQZCJytCF_Aw0QhDz2KrmTA8NLHOmIitkTa1IhFRwCATQii3-2QlH-fuIaE6tYkF8yadNMIOWRY7C-bXyiCWLuTaI2zJGWUqvHIcmzFSRd6SSFUyUwEzFTJTMY-8rbdMSrCOy4jfI7trQsTZLh6Mp6eqUlvlgqFMtEghEIL_AfYv1VzG3EJYpvHzmUdeoLAoRNLIsVXnNFvMZqpz8Fm1JE9wAlCU_otocHg1Ua_faRC9qoiGYzgLk1V3KOBEEcarQbnZoARRM83lpXSrymjNFCIfQYDH08Qjz-tl3ImNeLkbL5BGQNCTQl52GQ14LjglJjzyoFSY-pRDBDMCQfFI3FClBhuaK_nZlwL2XKYxh2zFI1tLpfv10y_h8latl1fLxKP_evczcqP_oa0-dvZ7j8nNoDAqHNzOJlmZTxfuCUSrc_20skg_AZW5iLg |
| linkToUnpaywall | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Zb9NAEF5B-gB94D4MBS0IiaM49Tqbtf0YUKuUijZKSVWeVt4jJWrqRDkE5ZkfzszaMXGBVEi8Wd5ZyZ6da3dnviHkRTNKbCBS6wecaZ9blvgpT42vRNBPk7AZK4UH-h_3RbvHPxw3j4t2QFgLo860Goxm-bFyfbkEfejsNjzo062x6efqHoutKVhYl0iLDVSwTPoqWRN421Qja739Tuuzqy-KQh9C48W95h_nVTyTA_D_3Uwv-amLOZTlReo6uTbPxun513Q4XPJVOzfJcPGXeYrKaX0-U3X9_QIA5H9iwy1yo4hpaSsXwtvkis3ukPUlpMO75EcnR5YFKXhLx_MJJig5maBpZqguUaPzolA66lPcqZ8pl6dDXSNB2vUxnRd8LaOvuoedA_aaOpSJQUYhxFXDc2q_ubReayi8yye1t_cg1KB4PzG9R3o725_et_2iAYSvo0Y8w6tlJoxpah2aQEOgZnjDhqwRKwS9DyKjAq5ZQ0cqDXhktDCJ4TFvhgHsuxA47j6pZaPMPiRUJSY2YEyFFZqbfpBG1oCxNyKMhG0w5ZFgsfhSF-jo2KRjKN0uKRYyZ7AEBktksAw88qacMs6hQVYRv0OJKgkR1du9GE1OZGEkpA37IlY8gbAL_gOsbaKYiJiBIFDhYZ1HnqM8SsTtyDAx6CSdT6dy9-BItgSLsd9QM_kb0WH3cqK9zm6F6GVB1B-hwKVFxQZwFEHDKpQbFUowUbo6vFAgWZjIqUScJQgnWRJ75Fk5jDMx7S-zoznScAixEtgFrqIBPwlcCrhHHuQ6WXK5gdBJICgeiSraWlmG6kg2-OJA1kUSMdgbeWRzode_Pn3FKm-Wqn-5TDz6J-rH5HrotJuBZ9sgtdlkbp9AQDxTTwtD9xN_Fas0 |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Production%2C+purification+and+characterization+of+recombinant+human+R-spondin1+%28RSPO1%29+protein+stably+expressed+in+human+HEK293+cells&rft.jtitle=BMC+biotechnology&rft.au=Gabriel+Levin&rft.au=Bruna+Andrade+Aguiar+Koga&rft.au=Gustavo+Gross+Belchior&rft.au=Ana+Claudia+Oliveira+Carreira&rft.date=2020-01-20&rft.pub=BMC&rft.eissn=1472-6750&rft.volume=20&rft.issue=1&rft.spage=1&rft.epage=14&rft_id=info:doi/10.1186%2Fs12896-020-0600-0&rft.externalDBID=DOA&rft.externalDocID=oai_doaj_org_article_e2f68b49218d483189b1671d102bb142 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1472-6750&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1472-6750&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1472-6750&client=summon |