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Article

Expression, purification and characterization of soluble human interleukin-6 receptor alpha-chain and its mutant protein in Escherichia coli.

Biotechnology letters - 1 Sept 2007

Wang Jing, Yang Zhenhui, Shi Ming, Li Yan, Guo Ning, Shen Beifen, Feng Jiannan

Abstract excerpt

To investigate the function of the N-terminal immunoglobulin (Ig)-like domain of the human interleukin-6 receptor alpha-chain (hIL-6R), we constructed a soluble human interleukin-6 receptor (shIL-6R) (named EC05, amino acids 20-354) and soluble variants of the shIL-6R lacking the Ig-like domain (named EC70, amino acids 105-354). The two extracellular portions of hIL-6R were expressed as soluble fusion proteins...

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Identifiers

PMID: 17534582
DOI: 10.1007/s10529-007-9402-x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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