DNAJC5G Polyklonale Antilichaam, PerCP-Cy5.5 Vervoeging

The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. Members of the DnaJ family are characterized by the presence of the J domain. 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. Proteins of the DnaJ family contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis.

CSP-gamma; DNJ5G_HUMAN; Cysteine string protein gamma; DnaJ (Hsp40) homolog subfamily C member 5 gamma; DnaJ homolog subfamily C member 5G; Gamma CSP; Gamma cysteine string protein.

285126

Q8N7S2

Cell membrane

Mouse, Rat

101-189/189

DNAJC5G

PerCP-Cy5.5

KLH conjugated synthetic peptide derived from human DNAJC5G

IF (IHC-P), IF (IHC-F), IF (ICC)

Purified by Protein A.

482nm/694nm

1µg/µl

IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

285126

Human, Rabbit