β-Crystallin, mAb (3.H9.2)

[CRYBB]



ADI-SPA-230-D	50 µg	165.00 USD

ADI-SPA-230-F	200 µg	345.00 USD

Product Specification

Purity Detail:	Protein G affinity purified.

Formulation:	Liquid. In PBS, pH 7.2, containing 0.1mM PMSF and 50% glycerol.

Clone:	3.H9.2

Isotype:	Mouse IgG1

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

Miscellaneous/General:	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:	Please click here for the comprehensive product datasheet.

Product Literature References

lambda-crystallin related to dehydroascorbate reductase in the rabbit lens: M. Takehana, et al. ; Jpn. J. Ophthalmol. 47, 437 (2003), Application(s): WB using rabbit samples, Abstract;