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Cat. Number

070327452603150

Chemical Name

Hsp70 (Hsc70) Monoclonal Antibody (Clone BB70)

References

Synonyms

Heat Shock Protein 70

Formula Weight

72.0

Formulation

Protein G affinity-purified mouse IgG at a concentration of 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	+
Ovine Hsp70	+
Canine Hsp70	+
Beluga Hsp70	+
Bovine Hsp70	+
Fish (carp, rainbow trout, chinook/chum salmon) Hsp70	+
Gunina pig Hsp70	+
Scallop pig Hsp70	+
Hamster Hsp70	+
Rabbit Hsp70	+
Chicken Hsp70	+
Xenopus Hsp70	+
Drosophila Hsp70	+
Yeast Hsp70	+

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Background Reading

Zou, J., Guo, Y., Guettouche, T., et al. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94(4) 471-480 (1998).

Fernandez-Funez, P., Nino-Rosales, M.L., de Gouyon, B., et al. Identification of genes that modify ataxin-1-induced neurodegeneration. Nature 408 101-106 (2000).

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

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).

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).

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

Prapapanich, V., Chen, S., Toran, E.J., et al. Mutational analysis of the hsp70-interacting protein hip. Mol Cell Biol 16(11) 6200-6207 (1996).

Smith, D.F., Sullivan, W.P., Marion, T.N., et al. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol 13(2) 869-876 (1993).

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Size	Global Purchasing
50 µg
200 µg

Description

Antigen: chicken Hsp70/Hsp90 complex · Clone designation: BB70 · Host: mouse · Isotype: IgG2a · Application(s): WB, IP, and IHC · Hsp70 genes encode abundant heat-inducible 70 kDa Hsps (Hsp70s). In most eucaryotes 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 Global Polyclonal Antibody上一个：Hsp70 (Hsc70) Monoclonal Antibody (Clone N27)

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