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crystallin, alpha B

Cat：P07036

Summary:

【Derived From】： E.coli

【Endotoxin】： Not measured

【Amino Acid】： 1-716aa

【Purity】： ≥85% by SDS-PAGE.

【Name】： CRYAB

【Full Name】： crystallin，alpha B

【Uniprot】： P02511

【Gene ID】： 1410

【Mol Mass】： 20.2kDa

【Application】： Immunology research

【Purification】： NI-NTA affinity purification

【Bioactive】： N0

【Tag】： With a 6×His tag at the N/C-terminus.

【Concentration】： 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)

【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks， stored at < -20℃ for 1 year.

【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restrict

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