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β-Crystallin monoclonal antibody (3.H9.2)

 
ADI-SPA-230-F 200 µg 431.00 USD
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Product Specification

Alternative Name:CRYBB
 
Clone:3.H9.2
 
Host:Mouse
 
Isotype:IgG1
 
Immunogen:Native bovine β-crystallin.
 
UniProt ID:P11843 (beta-crystallin A3)
 
Gene/Protein Identifier:I45857 (PIR, beta-crystallin A3)
 
Source:Purified from ascites.
 
Species reactivity:Bovine, Rabbit
 
Applications:WB
 
Recommended Dilutions/Conditions:Western Blot (1µg/ml, 1:1,000, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Detects a band of ~25kDa by Western blot.
 
Purity Detail:Protein G affinity purified.
 
Formulation:Liquid. In PBS containing 0.09% sodium azide and 50% glycerol.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background: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.
 
Regulatory Status:RUO - Research Use Only
 

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;

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