中文名稱： DNAJA1 抗原（重組蛋白）

英文名稱：DNAJA1 Antigen (Recombinant Protein)

別名：DnaJ (Hsp40) homolog, subfamily A, member 1; DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; NEDD7; hDJ-2

儲(chǔ) 存：冷凍（-20℃）

相關(guān)類別：抗原

概述

Fusion protein corresponding to a region derived from 206-397 amino acids of human DNAJA1

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Full name:

DnaJ (Hsp40) homolog, subfamily A, member 1

Synonyms:

DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; NEDD7; hDJ-2

Swissprot:

P31689

Gene Accession:

BC008182

Purity:

>85%, as determined by Coomassie blue stained SDS-PAGE

Expression system:

Escherichia coli

Tags:

His tag C-Terminus, GST tag N-Terminus

Background:

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

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DNAJA1 抗原（重組蛋白）

Full name:	DnaJ (Hsp40) homolog, subfamily A, member 1
Synonyms:	DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; NEDD7; hDJ-2
Swissprot:	P31689
Gene Accession:	BC008182
Purity:	>85%, as determined by Coomassie blue stained SDS-PAGE
Expression system:	Escherichia coli
Tags:	His tag C-Terminus, GST tag N-Terminus
Background:	DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.