Heat Shock Protein 70-A2, Recombinant, Mouse (HSP70-A2) (Low Endotoxin)

The mouse heat shock protein, Hsp70-A2 is one of the three Hsp70 genes located in the central region of the mouse MHC. Similar clusters of MHC-linked Hsp70 genes occur in rat and human. The human Hsp70-A2 has 98.2% identity in the amino acid sequence to murine Hsp70-A2 (1). A comparison of the nucleotide sequences of the three human Hsp70 genes from various haplotypes has revealed only very limited sequence variation which is not associated with any amino acid polymorphism (2). Murine Hsp70-A2 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 also 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 (3). 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 ATP-dependent 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 (4). 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 (5). 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 (6).\n\nFunctional Assay: \nThis protein has tested positive for ATPase activity.\n\nApplications:\nSuitable for use in Western Blot. This protein does not contain DnaK as demonstrated by Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: (Colorimetric) 10ng of protein.\nOptimal dilutions to be determined by the researcher.\n\nEndotoxin: \n(same/less than) 50 EU/mg as determined by Limulus Amebocyte Lysate (LAL) gel clot assay.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degrees 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.

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