Heat shock cognate 71 kDa protein (Hsc70), also known as HSPA8, is a member of the heat shock protein 70 family (Hsp70). Unlike Hsp70, it is a constitutively expressed chaperone protein and is involved in diverse cellular processes including protein folding and protein degradation. Hsc70 consists of two domains: the nucleotide binding domain (NBD) and the substrate binding domain (SBD). Hsc70, with the help of accessory proteins, exerts its chaperone activity by binding to short hydrophobic stretches of nascent or unfolded polypeptides through the SBD in an ATP-dependent manner.
