MaxLight™650 is a new Far-IR stable dye conjugate comparable to Alexa Fluor™647, DyLight™649, Cy5™ and offers better labeling efficiency, brighter imaging and increased immunodetection. Absorbance (655nm); Emission (676nm); Extinction Coefficient 250,000.alpha B crystallin is a 20kD water-soluble major structural protein and member of the heat shock protein family, designated HSPB5, which acts as a molecular chaperone and is believed to play a role in the maintenance of ocular lens transparency/refractive index. Besides the involvement of both alpha A and alpha B crystallin in the prevention of protein precipitation and cataract formation in the eye, alpha crystallins have also been demonstrated in other tissues including the heart, brain, kidney, spleen and thymus. Studies have shown that a mutation in alpha B crystallin is responsible for desmin-related myopathy (DRM) and cataract(1), and that alpha B crystallin is a major component of the astrocytic inclusions known as Rosenthal fibers (RFs), found in Alexander's disease.ApplicationsSuitable for use in FLISA and Western Blot. Other applications not tested.Recommended DilutionWestern Blot: 1:1000-1:2000. Detects a band at ~20kD in mouse eye cell lysates.Optimal dilutions to be determined by the researcher.Hybridoma: |Sp2/0 myeloma cells with spleen cells from Balb/c mice.Storage and StabilityMay be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Note: Applications are based on unconjugated antibody.ImmunogenRecombinant protein corresponding to aa1-175 of human alpha B crystallin purified from E.coli.FormSupplied as a liquid in PBS, pH 7.2. Labeled with MaxLight™650.PurityPurified by Protein G affinity chromatography from tissue culture supernatant.SpecificityRecognizes human alpha B crystallin at ~20kD. Species crossreactivity: mouse.References1. Perng, M.D. et al. (1999) The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274: 33235-33243.

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