Hsp70/Hsc70 Antibody from MYBIOSOURCE INC.
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| Antigenic Specificity | Hsp70/Hsc70 |
| Clone | [N27F3-4] |
| Host Species | Mouse |
| Reactive Species | human, mouse, rat, bovine, C.elegans, beluga, dog, chicken, Drosophila, fish, guinea pig, hamster, monkey, porcine, plant, rabbit, sheep, Xenopus |
| Isotype | IgG1 |
| Format | ATTO 390 conjugate |
| Size | 0.2 mg |
| Concentration | 1mg/mL |
| Applications | Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FC/FACS), IEM, Immunofluorescence (IF) |
| 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 proteins |
| Immunogen | n/a |
| Other Names | [Hsp70 1; Hsp70 2; Hsp70.1; Hsp72; HSPA1; HSPA1A; HSPA1B; hsc70], [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 # | MBS800088 |
| Price | $510 |
| Order / More Info | Hsp70/Hsc70 Antibody from MYBIOSOURCE INC. |
| Product Specific References | 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. 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.
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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