Anti-Alpha B Crystallin antibody [1B6.1-3G4]

Supplementary info

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

Activity summary

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.

Associated diseases and disorders

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.