HSP40-4 Polyclonal Antibody

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.

DJ 2; DJ2; DjA1; DnaJ (Hsp40) homolog; subfamily A; member 1; DnaJ homolog subfamily A member 1; DnaJ protein homolog 2; DNAJ2; Dnaja1; DNJA1; hDJ 2; HDJ-2; HDJ2; Heat shock 40 kDa protein 4; heat shock protein DNAJ like 2; Heat shock protein J2; HSDJ; HSJ-2; HSJ2; HSPF4; Human DnaJ protein 2; NEDD7; Neural precursor cell expressed developmentally down regulated 7; OTTHUMP00000021193