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AB5598

Anti-Alpha B Crystallin (phospho S45) 抗体

Anti-Alpha B Crystallin (phospho S45) antibody

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(4 Publications)

Rabbit Polyclonal Alpha B Crystallin phospho S45 antibody. Suitable for WB and reacts with Recombinant fragment - Cow samples. Cited in 4 publications. Immunogen corresponding to Synthetic Peptide within Human CRYAB phospho S45 aa 1-100.

別名を表示する

CRYA2, HSPB5, CRYAB, Alpha-crystallin B chain, Alpha(B)-crystallin, Heat shock protein beta-5, Heat shock protein family B member 5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component, HspB5

1 Images
Western blot - Anti-Alpha B Crystallin (phospho S45) antibody (AB5598)
  • WB

Unknown

Western blot - Anti-Alpha B Crystallin (phospho S45) antibody (AB5598)

Western blot of recombinant bovine phospho-alpha-B crystallin (Ser45) using ab5598. Lane 1 is phospho-alpha-B crystallin (Ser45) and lane 2 is unphosphorylated alpha-B crystallin.

All lanes:

Western blot - Anti-Alpha B Crystallin (phospho S45) antibody (ab5598)

Predicted band size: 20 kDa

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

アプリケーション

WB

applications

免疫原

Synthetic Peptide within Human CRYAB phospho S45 aa 1-100. The exact immunogen used to generate this antibody is proprietary information.

P02511

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Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Immunogen
バッファー組成
Preservative: 0.05% Sodium azide Constituents: PBS, 3% BSA
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
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補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Alpha B Crystallin also known as CRYAB or alpha B crystallin protein is a small heat shock protein with a molecular mass of approximately 20 kDa. It is expressed in various tissues including the eye lens heart skeletal muscles and the brain. Alpha B Crystallin functions mechanically as a chaperone helping to prevent the aggregation of unfolded proteins by stabilizing them. This protein plays an important role in maintaining proper cellular function especially under stress conditions.
Biological function summary

Alpha B crystallin performs as part of the larger small heat shock protein family which contributes to the cellular defense system. It acts primarily as a chaperone binding to denatured proteins to protect the cells from damage during environmental stresses such as heat and oxidative stress. Alpha B crystallin often forms oligomeric complexes which increases its protective properties. This protein exhibits significant anti-apoptotic functions by interacting with various apoptosis-regulating factors contributing to cellular survival.

Pathways

Alpha B crystallin integrates into the cellular stress response and apoptosis pathways. It involves the PI3K/Akt signaling pathway known for regulating cell survival and preventing programmed cell death. Alpha B crystallin also interacts with other proteins such as Bcl-2 further enhancing its role in anti-apoptotic activities. Its contribution to these pathways highlights its protective function during cellular stress situations.

Alpha B crystallin is associated with cataracts and dilated cardiomyopathy. It plays a significant role in maintaining lens transparency and mutations or dysfunctions in alpha B crystallin can lead to cataract development. Similarly in cardiac tissue abnormal alpha B crystallin expression links to dilated cardiomyopathy. The protein is also known to associate with other structural proteins like desmin where disruptions may contribute to muscle-related diseases.
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製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:
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ターゲットの情報

May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity).
See full target information CRYAB phospho S45
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文献 (4)

Recent publications for all applications. Explore the full list and refine your search

The Journal of clinical investigation 135: PubMed39932799

2025

Phosphorylation of CRYAB induces a condensatopathy to worsen post-myocardial infarction left ventricular remodeling.

Applications

Unspecified application

Species

Unspecified reactive species

Moydul Islam,David R Rawnsley,Xiucui Ma,Walter Navid,Chen Zhao,Xumin Guan,Layla Foroughi,John T Murphy,Honora Navid,Carla J Weinheimer,Attila Kovacs,Jessica Nigro,Aaradhya Diwan,Ryan P Chang,Minu Kumari,Martin E Young,Babak Razani,Kenneth B Margulies,Mahmoud Abdellatif,Simon Sedej,Ali Javaheri,Douglas F Covey,Kartik Mani,Abhinav Diwan

Antioxidants (Basel, Switzerland) 10: PubMed34208998

2021

MEK1/2-ERK Pathway Alterations as a Therapeutic Target in Sporadic Alzheimer's Disease: A Study in Senescence-Accelerated OXYS Rats.

Applications

Unspecified application

Species

Unspecified reactive species

Natalia A Muraleva,Nataliya G Kolosova,Natalia A Stefanova

Proceedings of the National Academy of Sciences of 114:E1745-E1754 PubMed28196893

2017

Phosphorylation of αB-crystallin supports reactive astrogliosis in demyelination.

Applications

Unspecified application

Species

Unspecified reactive species

Hedwich F Kuipers,Jane Yoon,Jack van Horssen,May H Han,Paul L Bollyky,Theo D Palmer,Lawrence Steinman

Japanese journal of ophthalmology 53:436-9 PubMed19763765

2009

Diagnostic Western blot for lens-specific proteins in aqueous fluid after traumatic lens-induced uveitis.

Applications

Unspecified application

Species

Unspecified reactive species

Masaki Tanito,Sachiko Kaidzu,Tohru Katsube,Shin Nonoyama,Yasuyuki Takai,Akihiro Ohira
View all publications
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