Crystallin, α B (CRYAB) is a molecular chaperone that holds protein in soluble aggregates. It functions as a tumor suppressor by interacting with adherens junction to inhibit the progression of nasopharyngeal carcinoma. It is also known to inhibit stimulation of CD4+ T cells in relapsing-remitting multiple sclerosis patients.
Rabbit Anti-CRYAB antibody recognizes canine, rabbit, pig, human, mouse, rat, and bovine CRYAB.

Synthetic peptide directed towards the C terminal region of human CRYAB

Rabbit Anti-CRYAB antibody is suitable for western blot applications at a concentration of 5 μg/ml.

Alpha crystallins are composed of: alpha-A and alpha-B, for acidic and basic, respectively. 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. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Synthetic peptide located within the following region: KYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVT

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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