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Technical Data |
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C7944-75J |
Crystallin, alpha B, phosphorylated (Ser45) |
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Description: Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products--alpha-A and alpha-B. There are at least 5 dImmunofluorescenceferent proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identImmunofluorescenceied in bovine and rat lens. Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander’s disease where it accumulates in brain cells of those afflicted. Application(s): Suitable for use in Immunofluorescence, Immunohistochemistry (parafin embedded) and Western Blot. Other applications not tested. Recommended Dilution: Immunofluorescence: 5ug/ml; Immunofluorescence staining of phospho-alpha-B crystallin (Ser45) in U373 MG cells results in cytoplasmic staining. Immunohistochemistry (parafin embedded): 8ug/ml Western Blot: 0.5ug/ml; Detects a band of ~20kD representing recombinant bovine phospho-alpha-B crystallin (Ser45). Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. |
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