Anti-α B Crystallin Antibody (11073)
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Antibody DetailsProduct DetailsReactive Species Bovine ⋅ Chicken ⋅ Human ⋅ Mouse ⋅ Rat Host Species Rabbit Immunogen Synthetic peptide corresponding to human alpha B crystallin. Product Concentration Lot Specific Formulation Whole antiserum State of Matter Liquid Product Preparation Whole antiserum Storage and Handling This antibody is stable for at least one (1) year at -20°C. Country of Origin USA Shipping Next Day 2-8°C Applications and Recommended Usage? Quality Tested by Leinco Immunoblotting: use at 1:5,000-1:10,000 dilution. A band of ~22 kDa is detected.
These are recommended concentrations. User should determine optimal concentrations for their application. Positive control: 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. DescriptionDescriptionSpecificity Rabbit Polyclonal Antibody specific to α B Crystallin Background Alpha crystallins are water-soluble lens proteins of the vertebrate eye that are related to the small heat shock protein family. Lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are further divided into acidic (Alpha A) and basic (Alpha B) groups. In the lens, alpha crystallin maintains proper refractive index, however it can also function as a molecular chaperone that binds to denatured proteins, keeping them in solution and maintaining the translucency of the lens. In response to cellular stress, alpha crystallin is phosphorlyated and may serve a structural control function and play a role in protein maintenance. Both alpha A and alpha B crystallin prevent apoptosis by inhibiting caspases. Alpha B crystallin is found in many cells and organs outside the lens and is over-expressed in cells subjected to stress conditions and in several neurological disorders. Function May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {UniProtKB:P23927}. NCBI Gene Bank ID UniProt.org Research Area Heat Shock & Stress Proteins References & CitationsTechnical ProtocolsCertificate of Analysis |
