Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-11-25
pubmed:abstractText
This unit presents a rapid and simple method for the nonchromatographic purification of recombinant proteins expressed in E. coli. This method relies on a thermally responsive elastin-like polypeptide (ELP) tag, where the tagged protein is precipitated using a mild temperature shift. The tag is then induced to self-cleave by a mild pH shift and is subsequently removed by a final thermal precipitation. The result is a purified native protein target, without the requirement for affinity apparatus or protease removal of the tag. This protocol describes the required cloning methods to insert a given target into the expression vector, as well as the general method for purifying the resulting expressed protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1934-3663
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
Chapter 26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
Unit 26.4.1-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Recombinant protein purification by self-cleaving elastin-like polypeptide fusion tag.
pubmed:affiliation
Princeton University, Princeton, New Jersey, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.