Anti-Hsp70 antibody [SPM254], prediluted (ab17850)
- Product nameAnti-Hsp70 antibody [SPM254], predilutedSee all Hsp70 primary antibodies ...
- DescriptionMouse monoclonal [SPM254] to Hsp70, prediluted
- SpecificityThis antibody recognizes both the constitutive (HSP73), and inducible (HSP72) forms of HSP70.
- Tested applicationsIHC-P more details
- Species reactivityReacts with: Human, Monkey
Predicted to work with: Cow
Full length protein from HeLa cells (Human).
- Positive control
- BT474 or Hela cells. Breast carcinoma.
- Storage instructionsStore at +4°C.
- Concentration information loading...
- PurityProtein A purified
- Clonality Monoclonal
- Clone numberSPM254
- Light chain typekappa
- Research Areas
Our Abpromise guarantee covers the use of ab17850 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||IHC-P: 1/1. Perform heat mediated antigen retrieval before commencing with IHC staining protocol.|
- FunctionIn cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
- Tissue specificityHSPA1B is testis-specific.
- Sequence similaritiesBelongs to the heat shock protein 70 family.
- Cellular localizationCytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
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References for Anti-Hsp70 antibody [SPM254], prediluted (ab17850)
This product has been referenced in:
- Slotta-Huspenina J et al. A specific expression profile of heat-shock proteins and glucose-regulated proteins is associated with response to neoadjuvant chemotherapy in oesophageal adenocarcinomas. Br J Cancer 109:370-8 (2013). Read more (PubMed: 23839491) »
- Wolff C et al. Successful protein extraction from over-fixed and long-term stored formalin-fixed tissues. PLoS One 6:e16353 (2011). WB ; Human, Mouse . Read more (PubMed: 21305021) »