This Antibody was verified by Knockout to ensure that the antibody binds to the antigen stated.
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. DnaJB4 (DnaJ homolog subfamily B member 4), also known as HLJ1, is expressed in skeletal muscle, heart and pancreas, and lower expression in brain, placenta and liver.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: DnaJ (Hsp40) homolog, subfamily B, member 4; DnaJ homolog subfamily B member 4; DnaJ-like heat shock protein 40; DNAJB 4; Heat shock 40 kDa protein 1 homolog; heat shock protein 40 homolog; HLJ 1; HSP40 homolog; Human liver DnaJ-like protein
Gene Aliases: DjB4; DNAJB4; DNAJW; HLJ1
UniProt ID: (Human) Q9UDY4
Entrez Gene ID: (Human) 11080
Molecular Function: chaperone