Anti-alpha A Crystallin/CRYAA antibody [EPR14125(B)]

Supplementary info

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

Activity summary

Alpha A Crystallin also known as CRYAA or crystallin protein is a small heat shock protein with a molecular mass of approximately 20 kDa. It is the major structural protein in the eye lens and is also expressed in other tissues like the heart kidney and brain. The protein forms large complexes with other alpha crystallin proteins to provide structural stability and help maintain the transparency and refractive index of the lens. This specific role of alpha A Crystallin makes it essential for proper eye function.

Biological function summary

Alpha A Crystallin acts like a molecular chaperone. It helps prevent the aggregation of misfolded proteins which is important in maintaining cellular protein homeostasis. Alpha A Crystallin can combine with alpha B Crystallin in lens fiber cells to form a hetero-oligomeric complex. This ability to bind unfolded proteins and assist in refolding processes highlights its importance in cell stress responses especially in situations where proteins could potentially denature and lose function.

Pathways

Alpha A Crystallin participates significantly in the oxidative stress response and apoptotic pathways. It interacts with proteins involved in these processes such as caspases to inhibit cell death and curb the deleterious effects of reactive oxygen species. In the apoptotic pathway alpha A Crystallin's role in regulating cell survival highlights its association with proteins like Hsp70 another heat shock protein that serves as a stabilizing agent during cellular stress.

Associated diseases and disorders

Certain mutations in alpha A Crystallin link it to cataracts and age-related macular degeneration. These ocular conditions arise when the protein's chaperone function declines leading to the aggregation of lens proteins and subsequent loss of lens transparency. Alpha B Crystallin the sister protein shows a similar role in these disorders indicating how disturbances in the intricate network of crystallin interactions affect ocular health.