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| Cat.No | ACP05271 | Target Name | CRYAB |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 1-175aa | Mol Weight | 20.2 kDa |
| Protein Length | Full length | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P02511 |
|---|
Uniprot Id
P02511
Target Species
Human
Target Name
CRYAB
Target Full Name
Alpha-crystallin B chain
Target Function
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Target Involvement
Myopathy, myofibrillar, 2 (MFM2); Cataract 16, multiple types (CTRCT16); Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB); Cardiomyopathy, dilated 1II (CMD1II)
Target Subcellular Location
Cytoplasm. Nucleus. Secreted.
Target Protein Families
Small heat shock protein (HSP20) family
Target Tissue Specificity
Lens as well as other tissues. Expressed in myocardial tissue.
Target Research Area
Cancer
Target Synonyms
AACRYA; Alpha B crystallin; Alpha crystallin B chain; Alpha(B)-crystallin; Alpha-crystallin B chain; CRYA2; Cryab; CRYAB_HUMAN; Crystallin alpha B; Crystallin alpha polypeptide 2; CTPP2; Heat shock 20 kD like protein; Heat shock protein beta 5; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY REN 27; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component
Target 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. 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 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. Alternative splicing results in multiple transcript variants.
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