β-Crystallin, mAb (3.H9.2) - Enzo Life Sciences

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ADI-SPA-230

Revised 10-Feb-10

β-Crystallin, mAb (3.H9.2)
SYNONYMS	CRYBB
PRODUCT LINE	Stress & Heat Shock Proteins
PRODUCT CATEGORY	Small Heat Shock Proteins / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ADI-SPA-230-D		50 µg	165.00 USD
ADI-SPA-230-F		200 µg	345.00 USD

Product Specification

SPECIES CROSSREACTIVITY:	Others
CLONE:	3.H9.2
ISOTYPE:	Mouse IgG1
PURITY DETAIL:	Protein G affinity purified.
IMMUNOGEN:	Native bovine β Crystallin protein.
SPECIFICITY:	Recognizes bovine and rabbit β crystallin.
APPLICATION:	Western Blot
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C

General Information

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. 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.
BACKGROUND/TECHNICAL INFORMATION
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