Background:

Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into α, β and γ families, and the β- and γ-crystallins also compose a superfamily. Crystallins usually contain seven distinct protein regions, inclu-ding four homologous motifs, a connecting peptide, and N- and C-terminal extensions. α-crystallins consist of three gene products, αA-, αB- and αC-crystallin, which are members of the small heat shock protein family (HSP 20). α-crystallins act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, α-crystallins do not renature these proteins. Expression of αA-crystallin is restricted to the lens and defects of this gene cause the development of autosomal dominant congenital cataracts (ADCC). The human αB-crystallin gene product is expressed in many tissues, including lens, heart and skeletal muscle. Elevated expression of αB-crystallin is associated with many neurological diseases, and a missense mutation in this gene has co-segregated in a family with a Desmin-related myopathy.

Alternative names:

CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component

Clonality:

Polyclonal

Reactivity:

Human,Mouse,Rat

Source:

Rabbit

Isotype:

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Immunogen:

Synthesized peptide derived from human Crystallin-αB around the non-phosphorylation site of S19.

Concentration:

1mg/ml

Applications:

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Recommende dilutions:

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Storage:

PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.

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