Hsp70/Hsc70 Antibody from MYBIOSOURCE INC.

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Antigenic SpecificityHsp70/Hsc70
Clone[N27F3-4]
Host SpeciesMouse
Reactive Specieshuman, mouse, rat, bovine, C.elegans, beluga, dog, chicken, Drosophila, fish, guinea pig, hamster, monkey, porcine, plant (Cucumber, Pea), rabbit, sheep, Xenopus
IsotypeIgG1
Formatunconjugated
Size0.05 mg, 0.2 mg
Concentration1mg/mL
ApplicationsWestern Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FC/FACS), IEM, Immunofluorescence (IF)
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DescriptionBackground 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 proteins
Immunogenn/a
Other Names[Hsp70 1; Hsp70 2; Hsp70.1; Hsp72; HSPA1; HSPA1A; HSPA1B], [HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HEL-S-103; HSPA1; HSX70HSPA1B; HSP70-1/HSP70-2; HSP70.1/HSP70.2]
Gene, Accession #Gene ID: 3303, NCBI: NP_005336.3, UniProt: P08107
Catalog #MBS803929
Price$250, $415
Order / More InfoHsp70/Hsc70 Antibody from MYBIOSOURCE INC.
Product Specific References1. 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. Polanonka-Grabowska R. et. al. (1997) Blood 90: 1516-1526. 8. Schnell D.J. et. al. (1994) Science 266: 1007-1012. 9. Kabakov A.E., et. al. (2002) Am. J.Physiol. 283(2): C521-C534. 10. Ricart J. et. al. (1997) Biochem. J. 324: 635-643. 11. Hang H. and Fox M.H. (1995) Cytometry 19(2): 119-125.1. Chen, Q. et al. (2011). A Novel Neurotrophic Drug for Cognitive Enhancement and Alzheimer's Disease. PLoS One. 6 (12): e27865. doi:10.1371/journal.pone.00278652. Mutsvunguma, L.Z. et al. (2011). Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin. Cell Stress and Chaperones. 16 (5), 505-515. doi:10.1007/s12192-011-0262-x3. Modrow, J. et al. (2012). Highly reliable quantification of proteins such as members of the HSP70 superfamily based on the grey scale index via immune detection stained bands on a Western blot. Forensic Science International. 222 (1), 256-258. doi: 10.1016/j.forsciint.2012.07.0014. Sun, L., Prince, T., Manjarrez, J.R., Scroggins, B.T., and Matts, R.L. (2012). Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins. BBA-Molecular Cell Research. 1823 (6), 1092-1101. doi: 10.1016/j.bbamcr.2012.03.0145. Ghemrawi, R. et al. (2013). Decreased vitamin B12 availability induces ER stress through impaired SIRT1-deacetylation of HSF1. Cell Death and Disease. 4, e553; doi:10.1038/cddis.2013.69
MYBIOSOURCE INC.
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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