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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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Applications: |
ELISA, WB, IHC |
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Name of antibody: |
DNAJA1 |
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Immunogen: |
Fusion protein of human DNAJA1 |
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Full name: |
DnaJ (Hsp40) homolog, subfamily A, member 1 |
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Synonyms： |
DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; NEDD7; hDJ-2 |
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SwissProt: |
P31689 |
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ELISA Recommended dilution: |
2000-5000 |
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IHC positive control: |
Human colon cancer and human thyroid cancer |
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IHC Recommend dilution: |
100-300 |
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WB Predicted band size: |
45 kDa |
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WB Positive control: |
HepG2, Raji, A431 and 231 cells |
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WB Recommended dilution: |
500-2000 |
