Anti-Hsp60 Antibody (11100)
Anti-Hsp60 Antibody (11100)
Product No.: 11100
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Clone LK-1 Target Hsp60 Formats AvailableView All Product Type Monoclonal Alternate Names EC 5.6.1.7, 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, Hsp60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein Isotype Mouse IgG1 Applications ELISA , IHC , IP , WB , FCM |
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Antibody DetailsProduct DetailsReactivity Species Human, Mouse, Rat, Rabbit, Bovine, Canine, Porcine, Ovine, Guinea Pig, Hamster, Chicken, Monkey, Xenopus, Drosophila Host Species Mouse Immunogen Recombinant human Hsp60 expressed in E. coli. Product Concentration Lot Specific Formulation PBS, pH 7.4. State of Matter Liquid Product Preparation Purified by Protein G affinity chromatography Storage and Handling This antibody is stable for at least one (1) year at -20°C. Regulatory Status For in vitro investigational use only. Not for
use in therapeutic or diagnostic procedures. Country of Origin USA Shipping Next Day 2-8°C Applications and Recommended Usage? Quality Tested by Leinco Immunoblotting: use at 0.1-1ug/mL. A band of ~60 kDa is detected.
Immunoprecipitation: use at 12.5ug/mLFlow cytometry: use at 10ug/mL These are recommended concentrations. User should determine optimal concentrations for their application. Positive control: Heat-shocked HeLa cell lysate. Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionSpecificity This antibody recognizes human, mouse, rat, rabbit, bovine, canine, porcine, ovine, guinea pig, hamster, chicken, monkey, Xenopus, and Drosophila Hsp60 (60 kDa). It does not cross-react with bacterial or yeast Hsp60. The epitope recognized is within aa 383-447 of human Hsp60. Background Hsp60 is an abundant protein synthesized constitutively in various cell types that is induced to higher concentrations after cell shock. It is present in mitochondria of many mammalian species and has highly similar counterparts in bacteria and plants (where it is localized to chloroplasts). In general, Hsp60 proteins are present in high concentrations, are induced in response to environmental stresses (such as heat shock) are homo-oligomeric structures of 7 or 14 subunits that dissociate reversibly in the presence of Mg2+ and ATP, have ATPase activity, and play a role in folding and assembly of oligomeric protein structures. Hsp60 has been linked to Alzheimer's disease, coronary artery disease, multiple sclerosis, diabetes, and other autoimmune diseases. Antigen DetailsFunction Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). {PubMed:11422376, PubMed:1346131, PubMed:25918392}. NCBI Gene Bank ID UniProt.org Research Area Heat Shock & Stress Proteins References & CitationsTechnical Protocols |
Formats Available
Products are for research use only. Not for use in diagnostic or therapeutic procedures.