重组人alpha A Crystallin/CRYAA蛋白(ab48778)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE, WB
描述
-
产品名称
重组人alpha A Crystallin/CRYAA蛋白
参阅全部 alpha A Crystallin/CRYAA 蛋白酶 -
纯度
> 90 % SDS-PAGE. -
表达系统
Escherichia coli -
蛋白长度
Full length protein -
无动物成分
No -
性质
Recombinant -
-
种属
Human -
序列
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS -
氨基酸
1 to 173
-
技术指标
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.
-
应用
Functional Studies
SDS-PAGE
Western blot
-
形式
Liquid -
补充说明
This product was previously labelled as alpha A Crystallin
-
Concentration information loading...
制备和贮存
-
稳定性和存储
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.
常规信息
-
别名
- Acry 1
- Alpha crystallin A chain
- Alpha-crystallin A chain
see all -
功能
May contribute to the transparency and refractive index of the lens. -
疾病相关
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. -
序列相似性
Belongs to the small heat shock protein (HSP20) family. -
翻译后修饰
O-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. -
细胞定位
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
实验方案
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.
数据表及文件
-
Datasheet download
文献 (3)
ab48778 被引用在 3 文献中.
- Eschbach J et al. Drug upgrade: A complete methodology from old drug to new chemical entities using Nematic Protein Organization Technique. Drug Dev Res 85:e22151 (2024). PubMed: 38349254
- 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