Rabbit Polyclonal Alpha B Crystallin phospho S59 antibody. Suitable for WB and reacts with Human samples. Cited in 11 publications. Immunogen corresponding to Synthetic Peptide within Human CRYAB phospho S59 aa 50-100.
Preservative: 0.05% Sodium azide
Constituents: PBS, 3% BSA
WB | |
---|---|
Human | Tested |
Cynomolgus monkey | Predicted |
Hamster | Predicted |
Pig | Predicted |
Rabbit | Predicted |
Sheep | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 0.5 µg/mL | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Sheep, Rabbit, Hamster, Pig, Cynomolgus monkey | Dilution info - | Notes - |
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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).
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
Rabbit Polyclonal Alpha B Crystallin phospho S59 antibody. Suitable for WB and reacts with Human samples. Cited in 11 publications. Immunogen corresponding to Synthetic Peptide within Human CRYAB phospho S59 aa 50-100.
Preservative: 0.05% Sodium azide
Constituents: PBS, 3% BSA
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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.
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.
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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ab5577 at 0.5μg/ml concentration staining approximately 20 KDa Crystallin Alpha B in lane 1) phospho-alpha-B crystallin (Ser59) and lane 2) non phosphorylated alpha-B crystallin in U-251 MG (formally U-373 MG) (Human brain glioma cell line) whole cell lysate.
All lanes: Western blot - Anti-Alpha B Crystallin (phospho S59) antibody (ab5577)
Predicted band size: 20 kDa
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