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Antigenic Specificity | Hsp70 |
Clone | [C92F3A-5] |
Host Species | Mouse |
Reactive Species | human, mouse, rat, bovine, C.elegans, dog, chicken, Drosophilia, carp, guinea pig, hamster, monkey, porcine, rabbit, sheep |
Isotype | IgG1 |
Format | ATTO 565 conjugate |
Size | 0.2 mg |
Concentration | 1mg/mL |
Applications | Western Blot (WB), Immunoprecipitation (IP), ELISA (EIA), Immunocytochemistry (ICC), Immunohistochemistry (IHC), Flow Cytometry (FC/FACS), IEM |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Background Info: Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. The mapped epitope is in the region of amino acid residues 436-503. Does not cross-react with Hsc70 (Hsp73). 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 aff |
Immunogen | n/a |
Other Names | [Hsp70 1; Hsp70 2; Hsp70.1; Hsp72; HSPA1; HSPA1A; HSPA1B; Hsp 70], [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 # | MBS800498 |
Price | $505 |
Order / More Info | Hsp70 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. 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): 141-159.1. Xu, Y. et al. (2009). 2,3-Dihydrowithaferin A-3β-O-sulfate, a new potential prodrug of withaferin A from aeroponically grown Withania somnifera. Bioorganic & Medicinal Chemistry. 17 (6), 2210-2214. doi:10.1016/j.bmc.2008.10.091 2. Fernndez-Llama, P. et al. (2010). Tamm-Horsfall protein and urinary exosome isolation. Kidney International. 77, 736-742. doi:10.1038/ki.2009.5503. Marubayashi, S. et al. (2010). HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans. J Clin Invest. 120 (10), 3578-3593. doi:10.1172/JCI424424. Olkku, A., Leskinen, J.J., Lammi, M.J., Hynynen, K., and Mahonen, A. (2010). Ultrasound-induced activation of Wnt signaling in human MG-63 osteoblastic cells. Bone. 47 (2), 320-330.5. Aare, S. et al. (2011). Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model. Physiol Genomics. 43 (24), 1334-1350. doi: 10.1152/physiolgenomics.00116.2011. |