Heat Shock 70kDa Protein 8 (HSPA8) Antibody – Rabbit Polyclonal

This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

HSC70: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co- chaperones. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG and TSC2. Interacts with BAG1. Interacts with SV40 VP1. Interacts with DNAJC7. Interacts with HERC5. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Constitutively synthesized. Ubiquitous. Belongs to the heat shock protein 70 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Chaperone; Heat shock protein; Nucleolus; RNA-binding

Chromosomal Location of Human Ortholog: 11q24.1

Cellular Component: blood microparticle; cytosol; extracellular exosome; extracellular matrix; extracellular region; extracellular space; ficolin-1-rich granule lumen; focal adhesion; intracellular; intracellular ribonucleoprotein complex; late endosome; lysosomal lumen; lysosomal membrane; melanosome; membrane; myelin sheath; nucleolus; nucleoplasm; nucleus; plasma membrane; presynapse; secretory granule lumen; spliceosomal complex; ubiquitin ligase complex

Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; cadherin binding; enzyme binding; G-protein coupled receptor binding; heat shock protein binding; phosphatidylserine binding; protein binding; RNA binding; ubiquitin protein ligase binding; unfolded protein binding

Biological Process: ATP metabolic process; cellular response to starvation; chaperone cofactor-dependent protein folding; chaperone-mediated autophagy translocation complex disassembly; chaperone-mediated protein transport involved in chaperone-mediated autophagy; clathrin coat disassembly; late endosomal microautophagy; mRNA splicing, via spliceosome; negative regulation of transcription, DNA-dependent; neurotransmitter secretion; neutrophil degranulation; positive regulation of mRNA splicing, via spliceosome; protein amino acid methylation; protein folding; protein refolding; protein targeting to lysosome involved in chaperone-mediated autophagy; regulation of cell cycle; regulation of cellular response to heat; regulation of mRNA stability; regulation of protein complex assembly; regulation of protein import; regulation of protein stability; response to unfolded protein; transcription, DNA-dependent; viral process