Hsc70 (human, recombinant)

Hsc70 is a chaperone from the Hsp70 chaperone family encoded by the HspA8 gene that shares 85% sequence identity to Hsp70 (encoded by HspA1A gene), and is one of the constitutively expressed members from this family.¹ Hsc70 acts as the main housekeeping protein but is also involved in many functions such as ubiquitin-proteasome degradation pathway and transporting cytoplasmic proteins into the nucleus.^2,3 Hsc70 also garnered interests as a potential therapeutic target since promoting accumulation of unfolded proteins can serve as a potential strategy to cause tumor death.⁴

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1. Stricher, F., Macri, C., and Muller, S. HSPA8/HSC70 chaperone protein: Structure, function, and chemical targeting. Autophagy 9(12), 1937-1954 (2013).

2. Bercovich, B., Stancovski, I., Mayer, A., et al. Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70. The Journal of Biological Chemisty 272(14), 9002-9010 (1997).

3. Dang, C.V., and Lee, W.M. Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins. The Journal of Biological Chemisty 264(30), 18019-18023 (1989).

4. Leu, J.I., Pimkina, J., Frank, A., et al. A small molecule inhibitor of inducible heat shock protein 70. Mol. Cell 36(1), 15-27 (2009).