Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1996-2-23
pubmed:abstractText
A 551-bp hIL-11 gene fragment that includes no nucleotide sequences encoding signal polypeptide and the initial 8 amino acids of the mature protein was cloned into a high-level expression vector pEx31B of E. coli. The authors identified the recombinant plasmid, designated pEx31-IL11, by restriction endonucleases digestion and DNA sequencing. The resulting recombinant plasmids were then used to transform E. coli strain HB101, and expression in the PL promoter system, which is temperature-regulated, was achieved. The expressed fusion protein amounts to 50% of total bacterial proteins. The hIL-11 protein expressed in E. coli was fused to the N-terminal 99 amino acids of the MS2 polymerase to form the inclusion body. These recombinant proteins can be purified to about 80% by extracting inclusion body with urea. One IL-6-dependent cell line 7 TD1 was used for bioassay. The recombinant hIL-11 protein was preliminarily purified and renatured to a specific activity of 10(5)U/mg, even in the presence of an excess of a neutralizing anti-IL-6 antibody.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1001-652X
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1202-9
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Expression of human interleukin-11 cDNA in E. coli.
pubmed:affiliation
Institute of Basic Medical Sciences, Beijing, China.
pubmed:publicationType
Journal Article