BackgroundThis chaperone has numerous roles: safeguarding proteins from stress, aiding folding, activating degradation of misfolded proteins, and assisting in protein complex assembly. It ensures proper folding, guided by co-chaperones. ATP cycles regulate its binding to substrates. Co-chaperones include HSP40s (ATPase stimulation), NEFs (promote substrate release), and TPR domain chaperones. It inhibits transcriptional activation, aids in splicing, interacts with bacterial lipopolysaccharide, and participates in ER-associated protein degradation (ERAD) with STUB1.
DescriptionHSPA8 Recombinant Monoclonal Antibody [3G10]. Unconjugated. Raised in: HEK293F Cell.
FormulationBuffer: Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
SpecificityHuman
IsotypeRabbit IgG
Uniprot IDP11142
PurificationAffinity Chromatography
ImmunogenA synthesized peptide derived from human HSPA8
StorageUpon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Alternative NamesHeat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8, Lipopolysaccharide-associated protein 1, LAP-1, LPS-associated protein 1, HSPA8, HSC70, HSP73, HSPA10
ApplicationELISA, WB; Recommended dilution: WB:1:500-1:5000