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.
Immunogen
Synthetic peptide directed towards the C terminal region of human CRYAB
Application
Rabbit Anti-CRYAB antibody is suitable for western blot applications at a concentration of 5 μg/ml.
Biochem/physiol Actions
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.
Sequence
Synthetic peptide located within the following region: KYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVT
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Suppression of activation of pathogenic CD4(+) T cells is a potential therapeutic intervention in multiple sclerosis (MS). We previously showed that a small heat shock protein, CRYAB, reduced T cell proliferation, pro-inflammatory cytokine production and clinical signs of experimental allergic
Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly associated with the progression of NPC. However, little is known about the functional impact of CRYAB on NPC progression. In this study
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