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Rabbit Anti-DNAJA4 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. DnaJA4 (DnaJ homolog subfamily A member 4) is a SREBP-regulated chaperone that is thought to regulate the cholesterol biosynthesis pathway.
Subcellular Location:
Membrane.
Similarity:
Contains 1 CR-type zinc finger.
Contains 1 J domain.
SWISS:
Q96JB1
Gene ID:
55466
Database links:
Entrez Gene: 55466 Human
Entrez Gene: 528615 Cow
Entrez Gene: 58233 Mouse
Entrez Gene: 397613 Pig
Entrez Gene: 300721 Rat
SwissProt: Q8WW22 Human
SwissProt: Q9JMC3 Mouse
Unigene: 513053 Human
Unigene: 489676 Mouse
Unigene: 228618 Rat
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