Anti-Zebrafish Hsc70 / Hspa8

0.5mg/ml if reconstituted with 0.2ml sterile DI water. HSPA8 (heat shock 70kDa protein 8) also known as HSC70, HSC71, HSP73, HSPA10, FORMERLY, LAP1 or LPS-ASSOCIATED PROTEIN 1, is a heat shock protein that in humans is encoded by the HSPA8 gene. The HSPA8 gene contains 9 exons and spans 5 kb. The deduced HSPA8 protein has 646 amino acids and a predicted molecular mass of 70,899 Da. And the HSPA8 gene is mapped on 11q24.1. HSPA8 plays an important role in cells by transiently associating with nascent polypeptides to facilitate correct folding. HSP73 also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat-shock proteins HSC70 and HSP70, translation initiation factor EIF4G, and poly (A)-binding protein. In the absence of Il3, Hsc70 formed a complex with Hsp40 and Hip, and this complex, in association with Eif4g and Pabp, formed a high-stability complex with Bim mRNA that protected it from ribonucleases. Protein function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Substrate recognition component in chaperone- mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. May play a role in uncoating of clathrin- coated vesicles. [The UniProt Consortium]