Alpha-A Crystallin Antibody, Clone 1H3.B8: PerCP

Alpha A Crystallin (CRYAA) is a member of the small heat shock protein (sHSP) family and a major structural component of the vertebrate eye lens. Traditionally recognized for its role in maintaining lens transparency and refractive properties, CRYAA is now gaining attention in neuroscience for its molecular chaperone activity and neuroprotective potential. CRYAA prevents protein aggregation by binding to partially unfolded or denatured proteins, a function critical in the context of neurodegenerative diseases characterized by protein misfolding, such as Alzheimer’s, Parkinson’s, and Huntington’s disease. Under cellular stress, CRYAA undergoes phosphorylation, enhancing its chaperone function and contributing to protein homeostasis. Beyond the lens, CRYAA is expressed in various tissues and interacts with a wide range of cellular components, including membrane proteins, nuclear proteins, Golgi matrix proteins, and even DNA. These interactions suggest broader roles in intracellular architecture, signal transduction, and genomic stability. Importantly, both Alpha A and Alpha B Crystallins exhibit anti-apoptotic properties by inhibiting caspase activation, positioning them as potential modulators of neuronal survival. CRYAA’s autokinase activity and involvement in cytoskeletal dynamics further support its relevance in maintaining neuronal integrity under stress. As interest grows in targeting molecular chaperones for neurodegenerative therapy, CRYAA stands out as a promising candidate for biomarker development, therapeutic delivery, and cellular resilience enhancement in the aging and diseased brain.

0.5 µg/ml was sufficient for detection of 100 ng purified alphaA crystalline by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

1. Merck K.B. et al. (1993) J Biol Chem. 268: 1046-1052. 2. Horwitz J. (1992) Proc Natl Acad Sci USA 89(21): 10449-10453. 3. Cobb B.A. and Petrash J.M. (2002) Biochemistry. 41: 483-490 4. Horwitz J. (2003) Exp Eye Res. 76: 145-153. 5. Bullard B. et al. (2004) J Biol Chem. 279: 7917-7924. 6. Gangalum R.K., Schibler M.J. and Bhat S.P. (2004) J Biol Chem. 279: 43374.43377. 7. Maddala R. and Rao V.P. (2005) Exp Cell Res. 306: 203-215. 8. Yaung J., et al. (2007) Molecular Vision 13: 566-577.

1. Merck K.B. et al. (1993) J Biol Chem. 268: 1046-1052. 2. Horwitz J. (1992) Proc Natl Acad Sci USA 89 (21) : 10449-10453. 3. Cobb B.A. and Petrash J.M. (2002) Biochemistry. 41: 483-490 4. Horwitz J. (2003) Exp Eye Res. 76: 145-153. 5. Bullard B. et al. (2004) J Biol Chem. 279: 7917-7924. 6. Gangalum R.K., Schibler M.J. and Bhat S.P. (2004) J Biol Chem. 279: 43374.43377. 7. Maddala R. and Rao V.P. (2005) Exp Cell Res. 306: 203-215. 8. Yaung J., et al. (2007) Molecular Vision 13: 566-577.