10011423  Hsp70 (Hsc70) Monoclonal Antibody (Clone N27)

Heat Shock Protein 70

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• See more Flow Cytometry; Immunohistochemistry; Immunoprecipitation; Western Blot; Antibodies

For active pharmaceutical ingredients (APIs) related to Hsp70 (Hsc70) Monoclonal Antibody (Clone N27), see Cayman Pharma

Antigen: murine recombinant Hsp70 · Host: mouse · Application(s): WB, IP, IHC, and flow cytometry · Hsp70 genes encode abundant heat-inducible 70 kDa Hsps (Hsp70s). In most eukatyotes Hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukatyotes 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 50% identity.1 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.2 When Hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half.3 The structure of this ATP binding domain displays multiple features of nucleotide binding proteins.4 All Hsp70s, regardless of location, bind proteins, particularly unfolded ones. 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.
1  Boorstein, W.R., Ziegelhoffer, T., Craig, E.A. Molecular evolution of the HSP70 multigene family. J Mol Evol 38(1) 1-17 (1994).
2  Rothman, J.E. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell 59 591-601 (1989).
3  DeLuca-Flaherty, C., McKay, D.B., Parham, P., et al. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 62 875-887 (1990).
4  Bork, P., Sander, C., Valencia, A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89 7290-7294 (1992).

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Pricing Information

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Size Price Quantity
50 µg €167.00
200 µg €359.00
Pricing updated 2010-08-01.
Prices are subject to change without notice.