兔抗DNAJC17多克隆抗体

Background:

The DnaJ family is one of the largest of all 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, forming peptide binding domains responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DNAJC17 (DnaJ (Hsp40) homolog, subfamily C, member 17) is a 304 amino acid protein containing a J domain and a RRM (RNA recognition motif) domain.

Applications:

WB

Name of antibody:

DNAJC17

Immunogen:

Synthesized peptide derived from N-terminal of human DNAJC17.

Full name:

DnaJ (Hsp40) homolog, subfamily C, member 17

SwissProt:

Q9NVM6

WB Predicted band size:

35 kDa

WB Positive control:

Jurkat cells, HepG2 cells and K562 cells lysates

WB Recommended dilution:

500-3000