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Cat. Number
070323178412158
Chemical Name
Hsp70 (Hsc70) Monoclonal Antibody (Clone N27)
References
Synonyms
  • Heat Shock Protein 70
Formula Weight 72.0
Formulation Protein G affinity-purified IgG at 1 mg/ml in PBS, pH. 7.2, containing 50% glycerol and 0.09% sodium azide
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Human Hsp70 +
Murine Hsp70 +
Rat Hsp70 +
Bovine Hsp70 +
C. elegans Hsp70 +
Beluga Hsp70 +
Canine Hsp70 +
Chicken Hsp70 +
Drosophila Hsp70 +
Fish (carp, Chinook/chum salmon, rainbow trout) Hsp70 +
Guinea pig Hsp70 +
Hamster Hsp70 +
Monkey Hsp70 +
Porcine Hsp70 +
Plant (cucumber/pea) Hsp70 +
rabbit Hsp70 +
ovine Hsp70 +
Xenopus Hsp70 +
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Background Reading

Welch, W.J., and Suhan, J.P. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J Cell Biol 103 2035-2052 (1986).

Polanowska-Grabowska, R., Simon, C.G., Falchetto, R., et al. Platelet adhesion to collagen under flow causes dissociation of a phosphoprotein complex of heat-shock proteins and protein phosphatase 1. Blood 90(4) 1516-1526 (1997).

Schnell, D.J., Kessler, F., and Blobel, G. Isolation of components of the chloroplast protein import machinery. Science 266(5187) 1007-1012 (1994).

Boorstein, W.R., Ziegelhoffer, T., and Craig, E.A. Molecular evolution of the HSP70 multigene family. J Mol Evol 38(1) 1-17 (1994).

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).

Fink, A.L. Chaperone-mediated protein folding. Physiol Rev 79(2) 425-449 (1999).

Bork, P., Sander, C., and 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).

Rothman, J.E. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell 59 591-601 (1989).

Kabakov, A.E., Budagova, K.R., Latchman, D.S., et al. Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion. Am J Physiol Cell Physiol 283 C521-C534 (2002).

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Size Global Purchasing
50 µg  
200 µg  

Description

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., and 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., and 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).

下一个：Hsp70 (Hsc70) Monoclonal Antibody (Clone BB70)上一个：Hsp70 Monoclonal Antibody (Clone C92F3A-5)
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