Hsp70/Hsc70 Antibody from MYBIOSOURCE INC.
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|---|---|
| Antigenic Specificity | Hsp70/Hsc70 |
| Clone | [BB70] |
| Host Species | Mouse |
| Reactive Species | human, mouse, rat, sheep, dog, beluga, bovine, fish, guinea pig, Scallop porcine, hamster, rabbit, chicken, Xenopus, Drosophila, yeast |
| Isotype | IgG2a |
| Format | PE-ATTO 594 conjugate |
| Size | 0.2 mg |
| Concentration | 1mg/mL |
| Applications | Westen Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Protein-binding Assay |
| Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
| Description | Background Info: Detects ~72 and ~73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots. Scientific Background: 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 5O% 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 protei |
| Immunogen | n/a |
| Other Names | [HSC54; Hsc70; HSC71; Hsp70 1; Hsp701/Hsp70 2; Hsp70.1; Hsp71; Hsp72; Hsp73; HSPA1; HSPA10; HSPA1A; HSPA1B; LAP1; NIP71], [HSPA2; HSP70; HSP70; HSP70] |
| Gene, Accession # | Gene ID: 423504, NCBI: NP_001006686.1, UniProt: P08106 |
| Catalog # | MBS800274 |
| Price | $505 |
| Order / More Info | Hsp70/Hsc70 Antibody from MYBIOSOURCE INC. |
| Product Specific References | 1. Zho J. (1998) Cell 94 : 471-480. 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. Smith D.F., et al, (1993) Mol. Cell. Biol. 13(2): 869- 876. 8. Prapapanich V., et al. (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature 408(6808): 101- 106.1. Rodina, A. et al. (2013). Identification of an Allosteric Pocket on Human Hsp70 Reveals a Mode of Inhibition of This Therapeutically Important Protein. Cell Chemistry & Biology. doi: 10.1016/j.chembiol.2013.10.0082. Kang, Y. et al. (2014). Heat Shock Protein 70 Inhibitors. 1. 2,5'-Thiodipyrimidine and 5-(Phenylthio)pyrimidine Acrylamides as Irreversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401551n3. Taldone, T. et al. (2014). Heat Shock Protein 70 Inhibitors. 2. 2,5'-Thiodipyrimidines, 5-(Phenylthio)pyrimidines, 2-(Pyridin-3-ylthio)pyrimidines, and 3-(Phenylthio)pyridines as Reversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401552y4. Rodina, A. et al. (2014). Affinity Purification Probes of Potential Use To Investigate theEndogenous Hsp70 Interactome in Cancer. ACS Chem Biol. doi.org/10.1021/cb500256u |
MYBIOSOURCE INC.
MYBIOSOURCE INC.
P.O. Box 153308
San Diego CA 92195-3308
P: 1.858.633.0165
P: 1.888.MBS.0165 (1.888.627.0165) (US & Canada)
F: 1.858.633.0166
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http://www.MyBioSource.com
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