Anti-α A Crystallin [Clone 1H3.B8]
Anti-α A Crystallin [Clone 1H3.B8]
Product No.: 11075
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Clone 1H3.B8 Target α A Crystallin Formats AvailableView All Product Type Monoclonal Alternate Names Heat shock protein β-4, HspB4 [Cleaved into:α-crystallin A(1-172;α-crystallin A(1-168;α-crystallin A(1-162] Isotype Mouse IgG1 Applications ELISA , WB |
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Antibody DetailsProduct DetailsReactive Species Bovine ⋅ Human ⋅ Mouse ⋅ Rat Host Species Mouse Immunogen Native alpha crystallin Product Concentration Lot Specific Formulation This monoclonal antibody is formulated in phosphate buffered saline (PBS) pH 7.2 - 7.4 with no carrier protein or preservatives added. State of Matter Liquid Product Preparation Antibodies are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates. Storage and Handling This antibody is stable for at least one (1) year at -20°C. Avoid multiple freeze-thaw cycles. Country of Origin USA Shipping Next Day 2-8°C Applications and Recommended Usage? Quality Tested by Leinco Immunoblotting: use at 0.5-1ug/ml. A band of ~20 kDa is detected.
Positive control: Purified alpha A crystallin. User should determine optimal concentrations for their application. Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionDescriptionSpecificity This antibody recognizes human, mouse, rat, and bovine alpha A crystallin. Other species have not been tested. It does not cross-react with alpha B crystallin, beta-L crystallin, beta-H crystallin, gamma crystallin, Hsp25, Hsp27, or Hsp47. 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. Function Contributes to the transparency and refractive index of the lens (PubMed:18302245). In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed:22120592, PubMed:31792453, PubMed:18199971, PubMed:19595763). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373). {PubMed:18199971, PubMed:19595763, PubMed:22120592, PubMed:28935373, PubMed:31792453, PubMed:18302245}. NCBI Gene Bank ID UniProt.org Research Area Heat Shock & Stress Proteins References & CitationsTechnical Protocols  Certificate of Analysis |
Formats Available
Products are for research use only. Not for use in diagnostic or therapeutic procedures.
