Anti-mtHsp70 Antibody, clone JG1 clone JG1, from mouse

Heat shock 70 kDa protein 1A (UniProt: Q61696; also known as Heat shock 70 kDa protein 3, HSP70.3, Hsp68, PBP74, Grp75) is encoded by the Hspa1a (also known as Hsp70-3, Hsp70A1) gene (Gene ID: 193740) in murine species. The 70-kDa heat shock protein (HSP70) is highly conserved, ubiquitous protein that functions as a molecular chaperone and helps in folding of newly synthesized or denatured proteins and in activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Heat shock 70 kDa protein 1A is localized in cytoplasmic mRNP granules containing untranslated mRNAs. It is acetylated at Lysine 77 by NA110 in response to cellular stress and then it is gradually deacetylated by HDAC4 at later stages. Its acetylation enhances its chaperone activity and determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form are shown to bind to HOPX and STUB1, respectively. It contains four ATP-binding regions and its N-terminal nucleotide binding domain (NBD; ATPase domain) is responsible for binding and hydrolyzing ATP. Its substrate binding domain (SBD) is localized to the C-terminal region. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. (Ref.: Green, JM et al. (1995). Hybridoma 14(4); 347-354).