βB2-crystallin Antibody (D-1): sc-376856

βB2-crystallin Antibody (D-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 (D-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 its seven distinctive protein regions, including homologous motifs and connecting peptides, allows it to effectively stabilize the lens′s refractive index while preventing light scattering. βB2-crystallin interacts with other crystallins and lens-specific proteins, which is vital for lens development and function. The ability of βB2-crystallin to undergo post-translational modifications, such as phosphorylation, enhances its functional diversity and adaptability in response to cellular conditions, making it a significant focus of research in ocular health and disease.

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βB2-crystallin Antibody (D-1) References:

1. Mutation of interfaces in domain-swapped human betaB2-crystallin.  |  Smith, MA., et al. 2007. Protein Sci. 16: 615-25. PMID: 17327390
2. Subfertility in mice harboring a mutation in betaB2-crystallin.  |  Duprey, KM., et al. 2007. Mol Vis. 13: 366-73. PMID: 17392687
3. Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface.  |  Takata, T., et al. 2010. Exp Eye Res. 91: 336-46. PMID: 20639133
4. Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.  |  Lampi, KJ., et al. 2012. Exp Eye Res. 104: 48-58. PMID: 22982024
5. The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallin.  |  Xu, J., et al. 2012. PLoS One. 7: e51200. PMID: 23236454
6. Crybb2 coding for βB2-crystallin affects sensorimotor gating and hippocampal function.  |  Sun, M., et al. 2013. Mamm Genome. 24: 333-48. PMID: 24096375
7. The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly.  |  Zhang, K., et al. 2014. Biochim Biophys Acta. 1842: 44-55. PMID: 24120835
8. Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation.  |  Xi, YB., et al. 2014. Biochem Biophys Res Commun. 447: 244-9. PMID: 24704203
9. MiR-326 antagomir delays the progression of age-related cataract by upregulating FGF1-mediated expression of betaB2-crystallin.  |  Ren, H., et al. 2018. Biochem Biophys Res Commun. 505: 505-510. PMID: 30268497
10. Polymorphisms in CRYBB2 encoding βB2-crystallin are associated with antisaccade performance and memory function.  |  Giegling, I., et al. 2020. Transl Psychiatry. 10: 113. PMID: 32317624

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