| Overview |
| bs-11277R-PE |
| HSP 40-4/HDJ2/DNAJA1 Polyclonal Antibody, PE Conjugated |
| WB |
| Mouse |
| Human, Rat, Cow, Sheep, Pig, Rabbit |
| Specifications |
| PE |
| Rabbit |
| KLH conjugated synthetic peptide derived from human HSP 40-4 |
| 21-110/397 |
| Polyclonal |
| IgG |
| 1ug/ul |
| Purified by Protein A. |
| Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. |
| Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles. |
| Target |
| Cytoplasm, Nucleus, Cell membrane |
| DJ 2; DJ2; DjA1; DnaJ Hsp40 homolog, subfamily A, member 1; DnaJ homolog subfamily A member 1; DnaJ protein homolog 2; DNAJ2; Dnaja1; DNJA1_HUMAN; 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. |
| 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. |
| Application Dilution |
| WB |
1:300-5000 |
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