βB2-crystallin Antibody (H-1): sc-376007

βB2-crystallin Antibody (H-1) is a mouse monoclonal IgG1 antibody that detects βB2-crystallin in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). βB2-crystallin plays a crucial role in maintaining the structural integrity and transparency of the eye lens, which is essential for proper vision. Anti-βB2-crystallin antibody (H-1) is part of the β-crystallin subfamily, known for its ability to form dimers and higher-order aggregates, contributing to the lens′s refractive properties. The unique structure of βB2-crystallin, characterized by seven distinctive protein regions, including homologous motifs and connecting peptides, allows βB2-crystallin to effectively stabilize lens fibers against aggregation and denaturation. βB2-crystallin interacts with other crystallins and lens-specific proteins, which is vital for lens development and function. βB2-crystallin′s ability to undergo post-translational modifications, such as phosphorylation, further enhances functional diversity and adaptability in response to cellular stress, making βB2-crystallin an important target for studies related to lens transparency and cataract formation. With broad species reactivity and versatility in various applications, anti-βB2-crystallin antibody (H-1) serves as an invaluable tool for researchers investigating molecular mechanisms underlying lens biology and ocular health.

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βB2-crystallin Antibody (H-1) References:

1. Creation of a new eye lens crystallin (Gambeta) through structure-guided mutagenic grafting of the surface of betaB2 crystallin onto the hydrophobic core of gammaB crystallin.  |  Kapoor, D., et al. 2009. FEBS J. 276: 3341-53. PMID: 19438717
2. βB2-Crystallin Promotes Axonal Regeneration in the Injured Optic Nerve in Adult Rats.  |  Böhm, MR., et al. 2015. Cell Transplant. 24: 1829-44. PMID: 25299378
3. BetaB2-crystallin mutations associated with cataract and glaucoma leads to mitochondrial alterations in lens epithelial cells and retinal neurons.  |  Dulle, JE., et al. 2017. Exp Eye Res. 155: 85-90. PMID: 28131617
4. Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.  |  Xi, Z., et al. 2017. Structure. 25: 496-505. PMID: 28238532
5. Effects of cataract-causing mutations W59C and W151C on βB2-crystallin structure, stability and folding.  |  Zhao, WJ., et al. 2017. Int J Biol Macromol. 103: 764-770. PMID: 28528950
6. Identification of Isomeric Aspartate residues in βB2-crystallin from Aged Human Lens.  |  Takata, T., et al. 2018. Biochim Biophys Acta Proteins Proteom. 1866: 767-774. PMID: 29654977
7. A Triple Mutation of BetaB2-Crystallin is Necessary to Develop Cataract and Glaucoma.  |  Rübsam, A., et al. 2017. J Clin Exp Ophthalmol. 8: PMID: 29805843
8. Introduction of an extra tryptophan fluorophore by cataract-associating mutations destabilizes βB2-crystallin and promotes aggregation.  |  Xu, J., et al. 2018. Biochem Biophys Res Commun. 504: 851-856. PMID: 30219234
9. Endoplasmic Reticulum Stress and the Lysosomal Pathway Play Crucial Roles in the Progression of βB2-Crystallin Mutation-Induced Congenital Cataracts in Mice.  |  Xiao, W., et al. 2023. Invest Ophthalmol Vis Sci. 64: 34. PMID: 37103007
10. Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.  |  Sun, J., et al. 2024. Protein Sci. 33: e5092. PMID: 38924206

The preferred βB1-crystallin antibody is βB1-crystallin Antibody (H-3): sc-48335.