Technical Data
Crystallin, alpha B (alpha B Crystallin Protein, Alpha(B) Crystallin, Alpha Crystallin B Chain, CRYAB, Crystallin alpha 2, CRYA2, CTPP2, Heat Shock 20 kD Like Protein, Heat Shock Protein beta 5, HSPB5, NY-REN 27 Antigen, Renal Carcinoma Antigen NY-REN-27,
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.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000-1:2000. Detects a band at ~20kD in mouse eye cell lysates.
Optimal dilutions to be determined by the researcher.

Sp2/0 myeloma cells with spleen cells from Balb/c mice.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. 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.
MabIgG2b10B2611Affinity Purified
100ug-20CBlue IceHumanMouse
Recombinant protein corresponding to aa1-175 of human alpha B crystallin purified from E.coli.
Purified by Protein G affinity chromatography.
Supplied as a liquid in PBS, pH 7.4, 0.09% sodium azide.
Recognizes human alpha B crystallin at ~20kD. Species crossreactivity: mouse.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. 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.