| References |
| Synonyms |
|
| Formula Weight |
70.0 |
| Formulation |
Protein G affinity-purified mouse IgG, FITC onjugated, at a concentration of 0.33 mg/ml in PBS, pH 7.2, containing 50% glycerol and 0.01% sodium azide |
| Purity |
>98% |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human Hsp70 |
+ |
| Murine Hsp70 |
+ |
| Rat Hsp70 |
+ |
| Bovine Hsp70 |
+ |
| Canine Hsp70 |
+ |
| Chicken Hsp70 |
+ |
| Drosophila Hsp70 |
+ |
| Fish (carp) Hsp70 |
+ |
| Guinea pig Hsp70 |
+ |
| Hamster Hsp70 |
+ |
| Monkey Hsp70 |
+ |
| Porcine Hsp70 |
+ |
| Rabbit Hsp70 |
+ |
| Ovine 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).
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).
Jeong, L.S., Yoo, S.J., Lee, K.M., et al. Design, synthesis, and biological evaluation of fluoroneplanocin A as the novel mechanism-based inhibitor of S-adenosylhomocysteine hydrolase. J Med Chem 46(2) 201-203 (2003).
Rothman, J.E. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell 59 591-601 (1989).
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| Size |
Global Purchasing |
| 50 µg |
|
| 200 µg |
|
Description
Antigen:
human Hsp70
·
Clone designation:
C92F3A-5
·
Host:
mouse
·
Application(s):
Flow cytometry
·
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 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 nucle 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. The binding of ATP triggers a bound substrate protein.5 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
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).
5
Fink, A.L. Chaperone-mediated protein folding. Physiol Rev 79(2) 425-449 (1999).
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