Anti-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: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP. [The UniProt Consortium]