Heat Shock Protein 70, active Recombinant Protein | HSPA8 recombinant protein

Heat Shock Protein 70, active, Recombinant, Human (HSP70)

Cat. Num. AAA635674

• Gene Names: HSPA8; Hsc70; HSPA10
• Applications: ELISA, Western Blot
• Purity: Highly Purified; ~95% (SDS-PAGE).
• Synonyms: Heat Shock Protein 70; active; Recombinant; Human (HSP70); HSPA8 recombinant protein

• Purity/Purification: Highly Purified; ~95% (SDS-PAGE).
• Form/Format: Supplied as a liquid in 20mM Tris, 50mM KCl, 5mM MgCl2, 1mM DTT, pH7.5.

• Applicable Applications for HSPA8 recombinant protein: ELISA (EL/EIA), Western Blot (WB)
• Application Notes: Suitable for use in ELISA and Western Blot.
• Preparation and Storage: May be stored at 4 degree C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for HSPA8 recombinant protein

Hsp70 genes encode abundant heat-inducible 70kD hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (2). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of

Product Categories/Family for HSPA8 recombinant protein

Molecular Biology; MB-Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 76253709
• NCBI GeneID: 281831
• NCBI Accession #: NP_776770.2
• NCBI GenBank Nucleotide #: NM_174345.4
• UniProt Accession #: P19120; Q3MHM4; A5D968
• Molecular Weight: 70kD
• NCBI Official Full Name: heat shock cognate 71 kDa protein
• NCBI Official Synonym Full Names: heat shock 70kDa protein 8
• NCBI Official Symbol: HSPA8
• NCBI Official Synonym Symbols: Hsc70; HSPA10
• NCBI Protein Information: heat shock cognate 71 kDa protein; Hsc70 ATPase; heat shock 70 kDa protein 8; heat shock cognate 71 kD protein; heat shock 70kd protein 10 (HSC71)
• UniProt Protein Name: Heat shock cognate 71 kDa protein
• UniProt Gene Name: HSPA8
• UniProt Synonym Gene Names: HSC70
• UniProt Entry Name: HSP7C_BOVIN

Uniprot Description

GRP78: a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

Protein type: Chaperone; Heat shock protein

Cellular Component: signalosome; endoplasmic reticulum membrane; smooth endoplasmic reticulum; cell surface; focal adhesion; mitochondrion; endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; membrane; melanosome; plasma membrane; integral to endoplasmic reticulum membrane; midbody; nucleus; myelin sheath

Molecular Function: protein domain specific binding; protein binding; enzyme binding; ubiquitin protein ligase binding; unfolded protein binding; ribosome binding; misfolded protein binding; glycoprotein binding; ATP binding

Biological Process: cellular response to glucose starvation; unfolded protein response, activation of signaling protein activity; cerebellum structural organization; substantia nigra development; proteolysis involved in cellular protein catabolic process; positive regulation of protein ubiquitination; cerebellar Purkinje cell layer development; negative regulation of transforming growth factor beta receptor signaling pathway; ER overload response; negative regulation of apoptosis; positive regulation of cell migration