ITN0190
ITN0190
- Catalog: ITN0190
- Gene/Protein: CRYAA CRYA1 HSPB4
- Product Description: Immunotag™ CRYAA Polyclonal Antibody
385.0000
Price in reward points: 385
| Antibody Specification | |
| Datasheet | 
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| Target Protein | CRYAA |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | WB,ELISA |
| Recommended Dilution | WB 1:500-2000 ELISA 1:5000-20000 |
| Concentration | 1 mg/ml |
| Reactive Species | Human,Mouse,Rat |
| Host Species | Rabbit |
| Immunogen | Synthesized peptide derived from human protein, at AA range: 1-80 |
| Specificity | CRYAA Polyclonal Antibody detects endogenous levels of protein. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, and 0.02% sodium azide. |
| Gene Name | CRYAA CRYA1 HSPB4 |
| Accession No. | P02489 P24622 P24623 |
| Description | crystallin alpha A(CRYAA) Homo sapiens 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 distin |
| Protein Expression | Colon,Lens,Spleen, |
| Subcellular Localization | nucleus,cytoplasm,extracellular exosome, |
| Protein Function | disease:Crystallins do not turn over as the lens ages, providing ample opportunity for post-translational modifications or oxidations. These modifications may change crystallin solubility properties and favor senile cataract.,disease:Defects in CRYAA are the cause of zonular central nuclear cataract [MIM:123580, 604219]; one of a considerable number of phenotypically and genotypically distinct forms of autosomal dominant cataract. This congenital cataract is a common major abnormality of the eye that frequently cause blindness in infants.,function:May contribute to the transparency and refractive index of the lens.,mass spectrometry: PubMed:10930324,mass spectrometry: PubMed:8175657,mass spectrometry: PubMed:9655350,mass spectrometry:With 1 phosphate group PubMed:8175657,PTM:Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.,PTM:O-glycosylated; contains N-acetylglucosamine side chains.,PTM:Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual.,similarity:Belongs to the small heat shock protein (HSP20) family., |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |
| Material Safety Data Sheet | |
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