Heat Shock Protein 70, Rat Recombinant Protein | Hspa1a recombinant protein

Heat Shock Protein 70, Recombinant, Rat (HSP70)

Cat. Num. AAA636057

• Gene Names: Hspa1a; HSP72; Hspa1; Hspa1b; Hsp70-1
• Applications: Western Blot
• Purity: Purified; 90% as determined by SDS-PAGE analysis.
• Synonyms: Heat Shock Protein 70; Rat; Recombinant; Rat (HSP70); Hspa1a recombinant protein

• Host: E Coli
• Purity/Purification: Purified; 90% as determined by SDS-PAGE analysis.
• Form/Format: Supplied as a liquid in 50mM Tris, pH 7.5, 1mM DTT, 100mM sodium chloride, 0.1mM PMSF.

• Applicable Applications for Hspa1a recombinant protein: Western Blot (WB)
• Application Notes: Suitable for use in Western Blot analysis. If this protein is to be used for Western blot analysis, we recommend that the material be diluted into an appropriate amount of SDS-PAGE sample buffer. On a 15-well minigel system, 100ng of protein per lane should be sufficient when used in a colorimetric Western Blot and an appropriate alkaline phosphatase conjugated secondary antibody for detection. This protein does not contain DnaK or Hsc70 as demonstrated by Western Blot analysis.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.

Related Product Information for Hspa1a recombinant protein

The heat shock protein, Hsp70 is part of the Hsp70 family which contains a number of highly-related protein isoforms ranging in size from 66kD to 78kD. The 70kD heat shock cognate protein, Hsc70 is closely related biochemically and biologically to Hsp70 and is part of the Hsp70 family. These proteins include both cognate members which are found within major intracellular compartments and highly inducible isoforms which appear to be predominantly cytoplasmic or nuclear in distribution (1). Members of the Hsp70 family are molecular chaperones which are involved in many cellular functions such as protein folding, transport, maturation and degradation and they exert their function in an ATPdependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (2). Recent data has demonstrated that BAG-1 which possesses a ubiquitin-like domain at its amino terminus and which has been shown to associate with the 26S proteosome in HeLa cells, modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal a role of BAG-1 as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome (3). There is also experimental data which shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate and form a cochaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp) which is essential for normal neurotransmitter release (4).

Product Categories/Family for Hspa1a recombinant protein

Molecular Biology; MB-Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 260064045
• NCBI GeneID: 24472
• NCBI Accession #: NP_114177.2
• NCBI GenBank Nucleotide #: NM_031971.2
• UniProt Accession #: Q07439; P42853; Q63256
• Molecular Weight: 70,185 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1A/1B
• NCBI Official Synonym Full Names: heat shock 70kD protein 1A
• NCBI Official Symbol: Hspa1a
• NCBI Official Synonym Symbols: HSP72; Hspa1; Hspa1b; Hsp70-1
• NCBI Protein Information: heat shock 70 kDa protein 1A/1B; HSP70.1/2; HSP70-1/HSP70-2; heat shock protein 70-1; heat shock 70 kDa protein 1/2
• UniProt Protein Name: Heat shock 70 kDa protein 1A/1B
• Protein Family: Heat shock 70 kDa protein
• UniProt Gene Name: Hspa1a
• UniProt Synonym Gene Names: Hsp70-1; Hspa1; HSP70-1/HSP70-2
• UniProt Entry Name: HSP71_RAT

NCBI Description

heat inducible gene; induced by global ischemia and kainic acid-induced seizures [RGD, Feb 2006]

Uniprot Description

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70.

Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis

Cellular Component: signalosome; focal adhesion; protein complex; mitochondrion; basolateral plasma membrane; inclusion body; cytosol; ribonucleoprotein complex; centriole; perinuclear region of cytoplasm; apical plasma membrane; cytoplasm; nuclear speck; intracellular; nucleus; ubiquitin ligase complex; vesicle

Molecular Function: protease binding; ATPase activity; unfolded protein binding; protein N-terminus binding; NF-kappaB binding; protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; double-stranded RNA binding; ATPase activity, coupled; ATP binding

Biological Process: binding of sperm to zona pellucida; positive regulation of T cell mediated cytotoxicity; positive regulation of erythrocyte differentiation; defense response; negative regulation of caspase activity; response to unfolded protein; negative regulation of vasoconstriction; negative regulation of cell proliferation; negative regulation of myeloid cell apoptosis; response to heat; mRNA catabolic process; protein refolding; negative regulation of protein ubiquitination; negative regulation of cell growth; negative regulation of apoptosis