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Cat. Number

070312649540358

Chemical Name

Hsp70 Polyclonal Antibody

References

Synonyms

Heat Shock Protein 70

Formulation

Whole rabbit serum (check label for amount)

Stability

1 year

Storage

-20°C

Shipping

Wet ice in continental US; may vary elsewhere

Specificity

Human Hsp70	+
Murine Hsp70	+
Rat Hsp70	+
Beluga Hsp70	+
Cow Hsp70	+
Canine Hsp70	+
Fish (carp) Hsp70	+
Guinea pig Hsp70	+
Hamster Hsp70	+
Monkey Hsp70	+
Procin Hsp70	+
Ovine Hsp70	+
Coral Hsp70	+

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Background Reading

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).

Ianaro, A., Ialenti, A., Maffia, P., et al. Role of cyclopentenone prostaglandins in rat carrageenin pleurisy. FEBS Lett 508 61-66 (2001).

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).

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).

Trentin, G.A., Yin, X., Tahir, S., et al. A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel ras GTPase-activating protein (RasGAP)-binding protein. J Biol Chem 276(6) 13087-13095 (2001).

Locke, M. Heat shock transcription factor activation and Hsp72 accumulation in aged skeletal muscle. Cell Stress Chaperones 5(1) 45-51 (2000).

Hung, T., Skepper, J.N., and Burton, G.J. In vitro ischemia-reperfusion injury in term human placenta as a model for oxidative stress in pathological pregnancies. Am J Pathol 159(3) 1031-1043 (2001).

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

Show all 10 Hide all but first 3

Size	Global Purchasing
25 µg
100 µg

Description

Antigen: full length Hsp70 · Host: rabbit · Application(s): WB, IP, ELISA, IHC, and ICC · Hsp70 genes encode abundant heat-inducible 70 kDa Hsps (Hsp70). In most eukaryotes Hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes 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.^1,2 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.³ 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.⁴ The structure of this ATP binding domain displays multiple features of nucleotide binding proteins.⁵ 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. The binding of ATP triggers a bound substrate protein.⁶ The universal ability of Hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding, oligomerization, and protein transport.

1 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).

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

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

4 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).

5 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).

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

下一个：Hsp70 Monoclonal FITC Antibody (Clone C92)上一个：Hsp70 (salmonid) Polyclonal Antibody

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