FGF-2 Polyclonal Antibody
¥680.00
- 产品信息
商品描述
靶点-Target
CRYAA
反应性
Human,Mouse,Rat
应用
WB,IHC,IF,ELISA
宿主物种-Host Species
Rabbit
同种型-Isotype
IgG,Kappa
MW(Calculated)
20kD
MW(Observed)
20kD
推荐稀释比
IHC 1:200-1:1000;WB 1:2000-1:10000;IF 1:200-1:1000;ELISA 1:5000-1:20000;
组成
PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
纯化工艺
Protein A
储存
-15°C to -25°C/1 year(Do not lower than -25°C)
克隆性
Monoclonal
克隆号
PT1172R
特异性
Endogenous
基因名称
CRYAA CRYA1 HSPB4
蛋白名称
Alpha-crystallin A chain (Heat shock protein beta-4) (HspB4)
Organism-1
Human
基因ID-1
1409
SwissProt-1
P02489
Organism-2
Mouse
SwissProt-2
P24622
Organism-3
Rat
SwissProt-3
P24623
背景
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
细胞定位
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.,
