HSPA8 / HSC70 recombinant protein

Recombinant Human HSPA8 / HSC70 Protein (His tag)

Cat. Num. AAA2545806

• Gene Names: HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• Purity: > 90 % as determined by SDS-PAGE
• Synonyms: HSPA8 / HSC70; Recombinant Human HSPA8 / HSC70 Protein (His tag); HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10; LAP1; MGC131511; MGC29929; NIP71; HSPA8 / HSC70 recombinant protein

• Host: E Coli
• Purity/Purification: > 90 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, 10% glycerol, pH 7.5
• Sequence Length: 646

• Application Notes: The recombinant human HSPA8 consisting of 657 amino acids and has a calculated molecular mass of 72.4 kDa. The apparent molecular mass of the protein is approximately 65 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Met
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for HSPA8 / HSC70 recombinant protein

Background: HSPA8, also known as HSC70, is a member of the heat shock protein family due to homology with other heat shock proteins. The heat shock protein 70 family is comprised by both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. HSPA8 belongs to the heat-shock cognate subgroup. Members of the human heat-shock protein multigene family have several highly conserved proteins with structural and functional properties in common, but vary in the extent of their inducibility in response to metabolic stress. HSPA8 is constitutively expressed and performs functions related to normal cellular processes. This protein binds to nascent polypeptides to facilitate correct protein folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Two alternatively spliced variants have been characterized to date. HSPA8 acts as a repressor of transcriptional activation. It inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones. It also is a ATPase that works with auxilin to remove clathrin coated vesicles. In neurons, synaptojanin is also an important protein involved in vesicle uncoating.

Description: A DNA sequence encoding the human HSPA8 (P11142-1) (Met 1-Asp 646) was expressed, with a polyhistide tag at the N-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 5729877
• NCBI GeneID: 3312
• NCBI Accession #: NP_006588.1
• NCBI GenBank Nucleotide #: NM_006597.5
• UniProt Accession #: P11142; Q9H3R6
• Molecular Weight: 53,518 Da
• NCBI Official Full Name: heat shock cognate 71 kDa protein isoform 1
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 8
• NCBI Official Symbol: HSPA8
• NCBI Official Synonym Symbols: LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• NCBI Protein Information: heat shock cognate 71 kDa protein
• UniProt Protein Name: Heat shock cognate 71 kDa protein
• UniProt Gene Name: HSPA8
• UniProt Synonym Gene Names: HSC70; HSP73; HSPA10; LAP-1; LPS-associated protein 1

NCBI Description

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]

Uniprot Description

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: cell-cell adherens junction; cytosol; extracellular matrix; extracellular space; focal adhesion; intracellular; lysosomal lumen; lysosomal membrane; membrane; nucleoplasm; nucleus; plasma membrane; ribonucleoprotein complex; ubiquitin ligase complex

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

Biological Process: ATP metabolic process; cellular response to starvation; negative regulation of transcription, DNA-dependent; neurotransmitter secretion; nuclear mRNA splicing, via spliceosome; protein refolding; regulation of mRNA stability; regulation of protein complex assembly; regulation of protein stability