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Production of functional human insulin-like growth factor binding proteins (IGFBPs) using recombinant expression in HEK293 cells.

Abstract：

:Insulin-like growth factor binding proteins (IGFBPs) display many functions in humans including regulation of the insulin-like growth factor (IGF) signaling pathway. The various roles of human IGFBPs make them attractive protein candidates in drug discovery. Structural and functional knowledge on human proteins with therapeutic relevance is needed to design and process the next generation of protein therapeutics. In order to conduct structural and functional investigations large quantities of recombinant proteins are needed. However, finding a suitable recombinant production system for proteins such as full-length human IGFBPs, still remains a challenge. Here we present a mammalian HEK293 expression method suitable for over-expression of secretory full-length human IGFBP-1 to -7. Protein purification of full-length human IGFBP-1, -2, -3 and -5 was conducted using a two-step chromatography procedure and the final protein yields were between 1 and 12mg protein per liter culture media. The recombinant IGFBPs contained PTMs and exhibited high-affinity interactions with their natural ligands IGF-1 and IGF-2.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Wanscher ASM,Williamson M,Ebersole TW,Streicher W,Wikström M,Cazzamali G

doi

10.1016/j.pep.2014.10.017

subject

Has Abstract

pub_date

2015-04-01 00:00:00

pages

97-105

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(14)00251-4

journal_volume

108

pub_type

杂志文章

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