Product Pathways - Protein Folding
HSPA8 (D12F2) Rabbit mAb #8444
|8444S||100 µl (10 western blots)||---||In Stock||---|
|8444||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey, Bovine, Pig||Endogenous||70-72||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Hamster, Chicken, D. melanogaster, Xenopus, Zebrafish, Dog, Horse.
Specificity / Sensitivity
HSPA8 (D12F2) Rabbit mAb recognizes endogenous levels of total HSPA8 protein. This antibody cross-reacts with HSPA2, HSPA1A, and HSPC70.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys25 of human HSPA8 protein.
HSPA8, alternately known as HSC70 or HSP73, is a constitutively expressed member of the HSP70 superfamily (1). Although its primary role in cells appears to be that of a general chaperone for unfolded proteins, HSPA8 has also been identified as the uncoating ATPase responsible for removing clathrin from coated vesicles and may also play a role in stabilizing untranslated mRNAs (1-5). In addition to these "housekeeping" functions, HSPA8 may also have an important role in inducible cellular stress responses. For example, oxidative or thermal stress promotes the nuclear/nucleolar accumulation of HSPA8, where it forms a complex with the topoisomerase I complex and likely protects it from heat inactivation (6,7). HSPA8 is reportedly phosphorylated in response to DNA damage, but it remains unclear what effect, if any, this has on HSPA8 function (8-10). Numerous high throughput studies support this observation. For more information, please see the HSPA8 page in PhosphoSitePlus® at www.phosphosite.org.
- Takayama, S. et al. (1999) J Biol Chem 274, 781-6.
- Goldfarb, S.B. et al. (2006) Proc Natl Acad Sci USA 103, 5817-22.
- Cheetham, M.E. et al. (1996) Biochem J 319 ( Pt 1), 103-8.
- Ma, Y. et al. (2002) J Biol Chem 277, 49267-74.
- Jønson, L. et al. (2007) Mol Cell Proteomics 6, 798-811.
- Shiota, M. et al. (2010) Hybridoma (Larchmt) 29, 453-6.
- Ciavarra, R.P. et al. (1994) Proc Natl Acad Sci USA 91, 1751-5.
- Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
- Matsuoka, S. et al. (2007) Science 316, 1160-6.
- Beausoleil, S.A. et al. (2004) Proc Natl Acad Sci USA 101, 12130-5.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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