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Rabbit Anti-DNAJA2 antibody
The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJA2 (DnaJ homolog subfamily A member 2), also known as HIRA-interacting protein 4 or cell cycle progression restoration gene 3 protein, contains one CR-type zinc finger and is a co-chaperone of HSC 70.
Function:
Co-chaperone of Hsc70.
Subcellular Location:
Membrane.
Similarity:
Contains 1 CR-type zinc finger.
Contains 1 J domain.
SWISS:
O60884
Gene ID:
10294
Database links:
Entrez Gene: 10294 Human
Entrez Gene: 56445 Mouse
Entrez Gene: 16826 Rat
Omim: 611322 Human
SwissProt: O60884 Human
SwissProt: Q9QYJ0 Mouse
SwissProt: O35824 Rat
Unigene: 73678 Human
Unigene: 475573 Mouse
Unigene: 3904 Rat
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