Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE, WB
Product nameRecombinant human alpha A Crystallin/CRYAA protein
See all alpha A Crystallin/CRYAA proteins and peptides
Purity> 95 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS
Amino acids1 to 173
Our Abpromise guarantee covers the use of ab48778 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This product was previously labelled as alpha A Crystallin
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: 0.316% Tris HCl, 0.0292% EDTA, 0.29% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Acry 1
- Alpha crystallin A chain
- Alpha-crystallin A chain
FunctionMay contribute to the transparency and refractive index of the lens.
Involvement in diseaseDefects in CRYAA are a cause of cataract autosomal dominant (ADC) [MIM:604219]. Cataract is an opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Cataract is the most common treatable cause of visual disability in childhood.
Sequence similaritiesBelongs to the small heat shock protein (HSP20) family.
modificationsO-glycosylated; contains N-acetylglucosamine side chains.
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.
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.
Cellular localizationCytoplasm. Nucleus. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab48778 has been referenced in 2 publications.
- Fan Q et al. Identification of proteins that interact with alpha A-crystallin using a human proteome microarray. Mol Vis 20:117-24 (2014). PubMed: 24453475
- Rao NA et al. Small Heat Shock Protein aA-Crystallin Prevents Photoreceptor Degeneration in Experimental Autoimmune Uveitis. PLoS One 7:e33582 (2012). PubMed: 22479415