HSC70 Antibody / HSPA8 (R31940)

Description

HSC70 (also known as HSPA8) is a constitutively expressed member of the HSP70 family that functions as an ATP-dependent chaperone. It binds nascent and stress-denatured polypeptides to promote folding, prevents aggregation, and coordinates protein quality control with co-chaperones such as HSP40/DNAJ and nucleotide exchange factors. HSC70 participates in clathrin uncoating, chaperone-mediated autophagy, and trafficking at membranes, with activity documented in cytosol, nucleus, and organelle-associated compartments.

Through cycles of ATP binding and hydrolysis, HSC70 regulates client stability and turnover, supporting proteostasis during basal growth and under environmental challenges. Its roles in endocytosis, antigen processing, and selective autophagy make it a versatile readout for cell biology, protein homeostasis research, and pathway modulation studies across multiple model systems.

The HSC70 antibody enables specific detection of endogenous HSC70 in applications such as western blot, immunofluorescence, and immunohistochemistry. Researchers use the HSC70 antibody to quantify protein abundance, assess subcellular localization (including clathrin-coated structures), and monitor chaperone engagement following genetic or pharmacologic perturbation. With high specificity and consistent performance, the HSC70 antibody supports rigorous analysis of molecular chaperone function and proteostasis mechanisms.

Application Notes

Optimal dilution of the HSC70 antibody should be determined by the researcher.

Immunogen

Amino acids 520-614 of human HSPA8/HSC70 were used as the immunogen for the HSC70 antibody.

Storage

After reconstitution, the HSC70 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.