Recombinant human alpha A Crystallin/CRYAA protein (ab48778)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE, WB
Description
-
Product name
Recombinant human alpha A Crystallin/CRYAA protein
See all alpha A Crystallin/CRYAA proteins and peptides -
Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS -
Amino acids
1 to 173
-
Specifications
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.
-
Applications
Functional Studies
SDS-PAGE
Western blot
-
Form
Liquid -
Additional notes
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.
pH: 7.50
Constituents: 0.316% Tris HCl, 0.0292% EDTA, 0.29% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
-
Alternative names
- Acry 1
- Alpha crystallin A chain
- Alpha-crystallin A chain
see all -
Function
May contribute to the transparency and refractive index of the lens. -
Involvement in disease
Defects 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 similarities
Belongs to the small heat shock protein (HSP20) family. -
Post-translational
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 localization
Cytoplasm. 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
Protocols
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.
Datasheets and documents
-
Datasheet download
References (2)
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