Alpha-B Crystallin Antibody, Clone 1A7.D5: APC

Alpha B Crystallin (CRYAB) is a small heat shock protein (sHSP) originally identified as a structural component of the vertebrate eye lens. While it contributes to lens transparency by preventing protein aggregation, CRYAB is now recognized for its broader role as a molecular chaperone and cytoprotective agent in various tissues, including the central nervous system. CRYAB shares structural and functional similarities with other sHSPs such as HSP25 and HSP27. It binds to misfolded or denatured proteins, stabilizing them in a soluble state and preventing toxic aggregation—a key pathological feature in neurodegenerative diseases like Alzheimer’s, Parkinson’s, and multiple sclerosis. Under cellular stress, CRYAB becomes phosphorylated, enhancing its chaperone activity and contributing to protein quality control. Unlike its Alpha A counterpart, Alpha B Crystallin is widely expressed beyond the lens, including in glial cells, neurons, and muscle tissue. It interacts with diverse cellular components such as membrane proteins, cytoskeletal elements, nuclear proteins, and DNA, supporting its role in maintaining intracellular architecture and stress resilience. Importantly, CRYAB is overexpressed in several neurological disorders and has been shown to inhibit apoptosis by blocking caspase activation. This anti-apoptotic function positions CRYAB as a promising therapeutic target and biomarker in neurodegenerative disease research, with potential applications in neuroprotection, inflammation modulation, and regenerative medicine.

Detects ~20kDa (Predicted mol. weight is ~21kDa). Does not cross-react with αA-crystallin, βL-crystallin, βH-crystallin, γ-crystallin, HSP25, HSP27 or HSP47 proteins.

Alpha B Crystallin, CRYAB, CRYA2, HSPB5, Heat Shock Protein Beta-5, Heat Shock Protein Family B Member 5, Alpha-Crystallin B Chain, Crystallin Alpha B, Alpha (B) -Crystallin, HEL-S-101, CMD1II, CTPP2, CTRCT16, MFM2, Rosenthal Fiber Component, Epididymis Secretory Protein Li 101, Heat-Shock 20 KD Like-Protein, Renal Carcinoma Antigen NY-REN-27

0.5 µg/ml of SMC-159 was sufficient for detection of 50 ng purified alpha B crystalline by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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. 9. Head M.W. et al. (2000) Neuropathol Appl Neurobiol. 26: 304-312. 10. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

Detects ~20kDa (Predicted mol. weight is ~21kDa) . Does not cross-react with αA-crystallin, βL-crystallin, βH-crystallin, γ-crystallin, HSP25, HSP27 or HSP47 proteins.

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. 9. Head M.W. et al. (2000) Neuropathol Appl Neurobiol. 26: 304-312. 10. Banduseela V.C., et al. (2009) Physiol Genomics. 39 (3) : 141-159.