αA-crystallin Antibody (H-4): sc-398304

αA-crystallin Antibody (H-4) is a mouse monoclonal IgG1 antibody that detects αA-crystallin in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). αA-crystallin is a member of the small heat shock protein family and plays a crucial role in maintaining lens transparency and refractive index, which is vital for proper vision. αA-crystallin (H-4) antibody targets a protein that functions as a molecular chaperone, preventing the aggregation of denatured proteins, although not facilitating their renaturation. The unique structure of αA-crystallin, which includes seven distinct protein regions and four homologous motifs, allows formation of large soluble aggregates that stabilize other proteins under stress conditions. Expression of αA-crystallin is restricted to the lens, and mutations in the αA-crystallin gene can lead to autosomal dominant congenital cataracts, highlighting importance in ocular health. Anti-αA-crystallin antibody (H-4) serves as an essential tool for researchers studying this protein in both normal physiology and disease states, particularly in lens development and related disorders.

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αA-crystallin Antibody (H-4) References:

1. Identification and characterization of a copper-binding site in αA-crystallin.  |  Raju, M., et al. 2011. Free Radic Biol Med. 50: 1429-36. PMID: 21300147
2. Increased expression of αA-crystallin in human diabetic eye.  |  Kase, S., et al. 2011. Int J Mol Med. 28: 505-11. PMID: 21617844
3. Specific phosphorylation of αA-crystallin is required for the αA-crystallin-induced protection of astrocytes against staurosporine and C2-ceramide toxicity.  |  Li, R., et al. 2012. Neurochem Int. 60: 652-8. PMID: 22414529
4. αA-crystallin gene CpG islands hypermethylation in nuclear cataract after pars plana vitrectomy.  |  Zhu, XJ., et al. 2015. Graefes Arch Clin Exp Ophthalmol. 253: 1043-51. PMID: 25663476
5. Isomerization of Asp residues plays an important role in αA-crystallin dissociation.  |  Takata, T. and Fujii, N. 2016. FEBS J. 283: 850-9. PMID: 26700637
6. Regulation of c-Maf and αA-Crystallin in Ocular Lens by Fibroblast Growth Factor Signaling.  |  Xie, Q., et al. 2016. J Biol Chem. 291: 3947-58. PMID: 26719333
7. Structural and functional consequences of chaperone site deletion in αA-crystallin.  |  Santhoshkumar, P., et al. 2016. Biochim Biophys Acta. 1864: 1529-38. PMID: 27524665
8. Hydrophobic residues of melittin mediate its binding to αA-crystallin.  |  Ramirez, LM., et al. 2020. Protein Sci. 29: 572-588. PMID: 31762096
9. Site-specific rapid deamidation and isomerization in human lens αA-crystallin in vitro.  |  Takata, T., et al. 2020. Protein Sci. 29: 955-965. PMID: 31930615
10. Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization.  |  Sun, J., et al. 2024. PLoS One. 19: e0306856. PMID: 38991013

The preferred αA-crystallin antibody is αA-crystallin Antibody (B-2): sc-28306.