Crystallin-αB (phospho Ser19) Rabbit Polyclonal Antibody

Crystallin-αB (phospho Ser19) Rabbit Polyclonal Antibody

Cat: APRab04505
Boyut:20μL Fiyat:$99_x000D_
Boyut:50μL Fiyat:$118_x000D_
Boyut:100μL Fiyat:$220_x000D_
Boyut:200μL Fiyat:$380_x000D_
Uygulama:WB,IHC,ICC/IF,ELISA
Reaktivite:Human,Mouse,Rat
Konjuge:Unconjugated
İsteğe bağlı konjugeler: Biotin, FITC (ücretsiz). Diğer 26 konjugatı görün.

Gen Adı:CRYAB
Category: ポリクローナル抗体 Tags: , , , , , , , , , ,
Crystallin-αB (phospho Ser19) Rabbit Polyclonal Antibody
Konjugasyon: Unconjugated
Rabbit polyclonal Antibody
Uygulama
IHC  ICC/IF  ELISA WB,IHC,ICC/IF,ELISA
Reaktivite
Human,Mouse,Rat
Gen Adı
CRYAB
Saklama
Aliquot and store at -20°C (valid for 12 months). Avoid freeze/thaw cycles.
Özet
Ürün Adı Crystallin-αB (phospho Ser19) Rabbit Polyclonal Antibody
Açıklama Rabbit polyclonal Antibody
Konak Rabbit
Reaktivite Human,Mouse,Rat
Konjugasyon Unconjugated
Modifikasyon Phosphorylated
İzotip IgG
Klonalite Polyclonal
Form Liquid
Konsantrasyon Unconjugated
Saklama Aliquot and store at -20°C (valid for 12 months). Avoid freeze/thaw cycles.
Nakliye Ice bags.
Tampon Liquid in PBS containing 50% glycerol, 0.5% protective protein and 0.02% New type preservative N.
Saflaştırma Affinity purification
Antijen Bilgisi
Gen Adı CRYAB
Alternatif İsimler CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component
Gen Kimliği 1410
SwissProt Kimliği P02511
İmmünojen The antiserum was produced against synthesized peptide derived from human CRYAB around the phosphorylation site of Ser19. AA range:10-59
Uygulama
Uygulama WB,IHC,ICC/IF,ELISA
Seyreltme Oranı WB 1:500-1:2000,IHC 1:100-1:300,ICC/IF 1:50-1:200,ELISA 1:5000-1:20000
Moleküler Ağırlık 24kDa
Araştırma Alanı
Signal Transduction
Arka Plan
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 distindisease: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 CRYAB are the cause of alpha-B crystallinopathy [MIM:608810]. Alpha-B crystallinopathy is a an autosomal dominant form of desmin-related myopathy (DRM) that results in weakness of the proximal and distal limb muscle (including neck, velopharynx, and trunk muscles), signs of cardiomyopathy and cataract. Patients with progressive myopathy characterized by myofibrillar degeneration that commences at the Z-disk, have been described. Mutations truncate the essential C-terminal domain of the protein required for the chaperone function.,disease:Seen as Rosenthal fiber protein in the brain tissue of patients with Alexander disease.,function:May contribute to the transparency and refractive index of the lens.,mass spectrometry: PubMed:10930324,mass spectrometry: PubMed:8175657,mass spectrometry:With 1 phosphate group PubMed:10930324,mass spectrometry:With 1 phosphate group PubMed:8175657,mass spectrometry:With 2 phosphate groups PubMed:8175657,similarity:Belongs to the small heat shock protein (HSP20) family.,subunit:Aggregates with homologous proteins, including CRYAA and the small heat shock protein HSPB1, to form large heteromeric complexes. Interacts with HSPBAP1 and TTN/titin.,tissue specificity:Lens as well as other tissues.,
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