Heat Shock Protein 70 (HSP70, HSP72)

The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.\n\nApplications:\nSuitable for use in Western Blot, Immunoprecipitation, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Flow Cytometry, ELISA and Electron Microscopy. Other applications have not been tested.\n\nRecommended Dilutions:\nWestern Blot (Colorimetric): 1:1000\nImmunohistochemistry: 1:50\nOptimal dilutions to be determined by researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

H1834-35

Size

50ug

Applications

ELISA, FC, ICC, IF, IHC, IP, WB

Hosts

Mouse

Reactivities

Hum, Mouse, Rat, Bov, Can, Ch/Bird, Dro/Arth, GP, NHP, Prc, Rabbit, Sheep, Xen/Amph

Form

Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.

P Type

Mab

Purity

Purified by Protein G affinity chromatography

Isotype

IgG1

References

1. S. Tsutsumi, et al. Nat. Struct. Mol. Biol. 16:1141 (2009). 2. H. Kasamatsu, et al. J. Virol. 83:37 (2008). 3. P.P. Li, et al. J. Virol. 83:37 (2008). 4. X. Wang, et al. Cell Biol. Int. 32:860 (2008). 5. M.I. Hirsh, et al. Crit. Care Med. 36:3220 (2008). 6. C. Preston, et al. J. Virol. 82:11775 (2008). 7. G. Kalesnykas, et al. Neuroscience 155:937 (2008). 8. P. Jaakkola, et al. Mol. Biol. Cell 19:2231 (2008). 9. K. Jones, et al. J. Neuroendocrinol. 19:383 (2007). 10. E. Chang, et al. Am. J. Physiol. Gastrointest. Liver Physiol. 292:G1070 (2007). 11. I. Brown, et al. Cell Stress Chaperones 12:51 (2007). 12. A. Pal, et al. Fish Shellfish Immunol. 22:547 (2007). 13. P. Garnier, et al. Brain Res. Bull. 58: 33 (2002). 14. R. Abdulle, et al. Cell Stress Chaperones 7:6 (2002). 15. I.S. Moon, et al. Cereb. Cortex 11:238 (2001). 16. T. Kondo, et al. J. Biol. Chem. 275:8872 (2000). 17. J. Luders, et al. J. Biol. Chem. 275:4613 (2000). 18. A.L. Fink; Physiol. Rev. 79:425 (1999). 19. B. Stahl, et al. Eur. J. Cell Biol. 78:375 (1999). 20. C.J. Cummings, et al. Nat. Genet. 19:148 (1998). 21. A.G. Pockley, et al. Immunol. Invest. 27:367 (1998). 22. B. Tedeschi & R.P. Ciavarra. Brain Res. Mol. Brain Res. 45:199 (1997). 23. M. Tavaria, et al. Cell Stress Chaperones 1:23 (1996). 24. DnaK: X. Zhu, et al. Science 272:1606 (1996). 25. J.L. Kilgore, et al.; J. Appl. Physiol. 76:598 (1994). 26. W.J. Welch & J.P. Suhan. J. Cell Biol. 103:2035 (1986).

Additional Info

Recognizes human Hsp70 protein at ~70kD. Species Crossreactivity: mouse, rat, beluga, bovine, C. elegans, canine, chicken, Drosophila, fish, gerbil guinea pig, hamster, monkey, porcine, rabbit, sheep, teal, Xenopus