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.
仕様
Synonyms：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
Host：Rabbit
Reactivity：Human,Mouse,Rat
Applications：WB,IHC,ELISA
Concentration：0.2mg/mL
Immunogen：Recombinant protein of human DNAJA1
Purification Method：Affinity purification
Clonality：Polyclonal
Conjugation：Unconjugated
Buffer：PBS with 0.05％ sodium azide, 50％ glycerol, PH7.3
