Anti-phospho-Crystallin, alpha B, (Ser59)

Alpha-crystallins composed of alpha-A (~19kD) and alpha-B (~19.2kD) subunits, are major water-soluble proteins accounting for almost 50% of the total protein of the mammalian transparent eye lens and they are also found in a variety of other tissues. The alpha-crystallins have sequence homology as well as structural and functional similarities with the small heat shock proteins such as Hsp25. The alpha-crystallins and Hsp25 have been shown to act as molecular chaperones by suppression of heat-induced aggregation of other proteins and are efficient inhibitors of elastase. The alpha-B subunit like Hsp25 was also found to be a substrate for protein cross-linking by tissue-type transglutaminase. The alpha-crystallins may be involved in metabolic pathways important for the development, maintenance, or pathology of the lens. They prevent destabilized proteins from precipitating out of solution by forming a soluble high-molecular-weight (HMW) complex. The bovine HMW protein form of the lens is composed mostly of alpha-crystallin in a highly aggregated state which has markedly reduced chaperone ability compared to alpha-crystallin. NMR spectroscopy of the naturally occurring HMW complex shows that the short C-terminal extension of alpha-B subunit in HMW has lost its flexibility whereas the alpha-A subunit extension is still flexible. These results suggest that depletion of alpha- crystallin with age as it is converted to HMW, could be one of the contributing factors to cataract formation in the lens. Applications: Suitable for use in Western Blot and Immunoprecipitation. Other applications not tested. Recommended Dilutions: Western Blot (ECL): 1:1000, Optimal dilutions to be determined by researcher., , Positive Control:, alpha Crystallin Protein, Storage and Stability: May 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. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.