antibody

HSP70 Antibody

SMC-230D

100 µg

286.00 USD

monoclonal

rat

nonconjugated

7FB

western blot, ELISA, immunocytochemistry

HSP70 Antibody

Rat Anti-Drosophila HSP70 Monoclonal IgG2B

HSP70

Unconjugated

286.00 USD

USD

Cell Signaling Protein Trafficking Chaperone Proteins Cancer Tumor Biomarkers Cancer Heat Shock

HSP70Bb Antibody, Heat Shock Protein 70Bb Antibody, dHSP70 Antibody, HSP70b Antibody, HSP70B Antibody, Dm-HSP70 Antibody

100 µg

Antibodies

Monoclonal

7FB

Prepared from Drosophila tissue culture cells heat shocked at 36.5◦C for 3 hours, and isolated using SDS PAGE.

Drosophila

NP_524927.2

Q9BIS2

WB ICC/IF ELISA

Rat

IgG2B

Dr

Fruit Fly (Drosophila melanogaster)

WB (1:2000); optimal dilutions for assays should be determined by the user.

Protein G Purified

PBS pH7.4, 50% glycerol, 0.1% sodium azide

1 mg/ml

Detects ~70kDa (heat-inducible form).

-20ºC

Blue Ice or 4ºC

StressMarq Biosciences Cat# SMC-230D, RRID: AB_2699430

1 µg/ml of SMC-230 was sufficient for detection of Drosophila HSP70 using an indirect assay with rabbit anti-rat IgG and goat anti-rabbit IgG:HRP.

HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). 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 (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 critical conformational change leading to the release of the 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 and oligomerization and protein transport. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell 59: 591-601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Galan A., et al. (2000) J. Biol. Chem. 275: 11418-11424. 8. Kondo T., et al. (2000) J. Biol. Chem. 275: 8872-8879. 9. Misaki T., et al. (1994) Clin. Exp. Immun. 98: 234-239. 10. Pockley A.G., et al. (1998) Immunol. Invest. 27: 367-377. 11. Moon I.S., et al. (2001) Cereb Cortex 11(3): 238-248. 12. Dressel et al. (2000) J. Immunol. 164: 2362-2371. 13. Verma A.K., et al. (2007) Fish and Shellfish Immunology. 22(5): 547-555. 14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.