File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1111/lam.12280
- Scopus: eid_2-s2.0-84906095288
- PMID: 24814641
- WOS: WOS:000340684400012
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: High-level expression, purification and characterization of active human C1q and tumour necrosis factor-related protein-1 in Escherichia coli
Title | High-level expression, purification and characterization of active human C1q and tumour necrosis factor-related protein-1 in Escherichia coli |
---|---|
Authors | |
Keywords | PET32 Escherichia coli Expression and purification Fusion protein Human C1q and tumour necrosis factor-related protein-1 Thioredoxin |
Issue Date | 2014 |
Citation | Letters in Applied Microbiology, 2014, v. 59, n. 3, p. 334-341 How to Cite? |
Abstract | C1q and tumour necrosis factor-related proteins (CTRPs) are a family of adiponectin paralogues. CTRP1 plays important biological functions in diabetes, obesity and hypertension. To further explore the physiological roles of human CTRP1 and its mechanisms of action, hCTRP1 gene was expressed in Escherichia coli. In the E. coli expression system, a large amount of soluble thioredoxin (Trx)-hCTRP1 fusion protein could be produced using the expression plasmid pET32a (+) and induction with IPTG at 18°C, which accounts about 20% of the total soluble bacterial proteins. The recombinant Trx-hCTRP1 fusion protein was purified to an approx. 95% purity using Ni-NTA affinity chromatography and Superdex G-75 column with a yield of about 28-mg protein from 1-l bacterial cultures. The purified recombinant Trx-hCTRP1 was shown to be active under in vivo and in vitro assay conditions. © 2014 The Society for Applied Microbiology. |
Persistent Identifier | http://hdl.handle.net/10722/238896 |
ISSN | 2023 Impact Factor: 2.0 2023 SCImago Journal Rankings: 0.525 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, H. | - |
dc.contributor.author | Hui, X. | - |
dc.contributor.author | Li, K. | - |
dc.contributor.author | Tang, X. | - |
dc.contributor.author | Hu, X. | - |
dc.contributor.author | Xu, A. | - |
dc.contributor.author | Wu, D. | - |
dc.date.accessioned | 2017-02-20T03:17:49Z | - |
dc.date.available | 2017-02-20T03:17:49Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Letters in Applied Microbiology, 2014, v. 59, n. 3, p. 334-341 | - |
dc.identifier.issn | 0266-8254 | - |
dc.identifier.uri | http://hdl.handle.net/10722/238896 | - |
dc.description.abstract | C1q and tumour necrosis factor-related proteins (CTRPs) are a family of adiponectin paralogues. CTRP1 plays important biological functions in diabetes, obesity and hypertension. To further explore the physiological roles of human CTRP1 and its mechanisms of action, hCTRP1 gene was expressed in Escherichia coli. In the E. coli expression system, a large amount of soluble thioredoxin (Trx)-hCTRP1 fusion protein could be produced using the expression plasmid pET32a (+) and induction with IPTG at 18°C, which accounts about 20% of the total soluble bacterial proteins. The recombinant Trx-hCTRP1 fusion protein was purified to an approx. 95% purity using Ni-NTA affinity chromatography and Superdex G-75 column with a yield of about 28-mg protein from 1-l bacterial cultures. The purified recombinant Trx-hCTRP1 was shown to be active under in vivo and in vitro assay conditions. © 2014 The Society for Applied Microbiology. | - |
dc.language | eng | - |
dc.relation.ispartof | Letters in Applied Microbiology | - |
dc.subject | PET32 | - |
dc.subject | Escherichia coli | - |
dc.subject | Expression and purification | - |
dc.subject | Fusion protein | - |
dc.subject | Human C1q and tumour necrosis factor-related protein-1 | - |
dc.subject | Thioredoxin | - |
dc.title | High-level expression, purification and characterization of active human C1q and tumour necrosis factor-related protein-1 in Escherichia coli | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1111/lam.12280 | - |
dc.identifier.pmid | 24814641 | - |
dc.identifier.scopus | eid_2-s2.0-84906095288 | - |
dc.identifier.hkuros | 246738 | - |
dc.identifier.volume | 59 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 334 | - |
dc.identifier.epage | 341 | - |
dc.identifier.eissn | 1472-765X | - |
dc.identifier.isi | WOS:000340684400012 | - |
dc.identifier.issnl | 0266-8254 | - |