Technical Data
Crystallin, beta
The beta-crystallins comprise a complex group of heteropolymers which are assembled from 6 primary gene products, the acidic (betaA1, betaA2, betaA3) and the basic (betaB1, betaB2, betaB3) polypeptides. betaA1 and betaA3 are identical, except for their N-termini, and appear to be generated by alternative translation of the same gene. betaB1 occurs in two forms, the primary gene product, betaB1a, and betaB1b which is generated through proteolysis. Further heterogeneity stems from post-translational modifications such as phosphorylation and/or other modifications that accumulate with aging. The subunits range in size from 2325 kD for the betaA and 2632kD for the betaB polypeptides. The beta-crystallins can be isolated in several aggregation states, spanning a molecular weight range from about 46kD to > 200kD. These include the octameric betaH, the tetrameric betaL1, and the dimeric betaL2 forms. beta-crystallins generally represent the second most abundant group of proteins in the lens but their proportions and properties vary with development. In the prenatal bovine lens, beta-crystallins account for 30% of the total proteins and betaH is predominant. In the adult, the total has increased to 40% due to an increased production of the betaL species. With the exception of betaB1a and betaB1b which are found only in betaH and appear to be responsible for its aggregation, all polypeptides are found in all forms of the protein. The betaB2 polypeptide (previously called betaBp) predominates, accounting for about 50% of the total. The lack of stoichiometry in the subunit contents suggests that each of the different molecular weight populations is a mixture of aggregates with most of the major polypeptides represented. These various species appear to be in equilibrium and their proportions vary with protein concentration. It is likely that even more highly aggregated forms, are the major species in the lens (213).

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

Recommneded Dilution:
Western Blot (Colorimetric): 1ug/ml
Optimal dilutions to be determined by researcher.

Positive Control:
Bovine beta-Crystallin Protein

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.
MabIgG14E56Affinity Purified
50ug-20CBlue IceBovineMouse
Bovine betaH-crystallin
Purified by Protein G affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.1mM PMSF in 50% glycerol.
Detects a ~25kD protein, corresponding to the apparent molecular mass of beta-crystallin on SDS-PAGE immunoblots, in samples from bovine. There may be weak reactivity with alphaA crystallin detected on immunoblot analysis.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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