βB1-crystallin Antibody (A-8): sc-374496

βB1-crystallin Antibody (A-8) is a mouse monoclonal IgM kappa antibody that detects βB1-crystallin from mouse, rat, and human sources through western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-βB1-crystallin antibody (A-8) is available in non-conjugated form. Crystallins are key structural proteins in vertebrate eye lenses, maintaining lens transparency and refractive index for proper vision. βB1-crystallin (A-8) antibody targets a member of the β-crystallin subfamily, which forms dimers and higher-order aggregates contributing to unique optical properties. βB1-crystallin features seven distinct protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions, crucial for stability and function. βB1-crystallin interacts with other crystallins and lens-specific proteins, forming a complex network supporting lens architecture and function. Understanding βB1-crystallin′s interactions and structural characteristics helps explain lens transparency mechanisms and cataract pathogenesis, making anti-βB1-crystallin antibody (A-8) valuable for ocular biology research.

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βB1-crystallin Antibody (A-8) References:

1. Association behaviour of human betaB1-crystallin and its truncated forms.  |  Bateman, OA., et al. 2001. Exp Eye Res. 73: 321-31. PMID: 11520107
2. Crystal structure of truncated human betaB1-crystallin.  |  Van Montfort, RL., et al. 2003. Protein Sci. 12: 2606-12. PMID: 14573871
3. Initiation codon mutation in betaB1-crystallin (CRYBB1) associated with autosomal recessive nuclear pulverulent cataract.  |  Meyer, E., et al. 2009. Mol Vis. 15: 1014-9. PMID: 19461930
4. Truncated human betaB1-crystallin shows altered structural properties and interaction with human betaA3-crystallin.  |  Srivastava, K., et al. 2009. Biochemistry. 48: 7179-89. PMID: 19548648
5. A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the βB1/βA3-crystallin heteromer but not the βB1-crystallin homomer.  |  Wang, KJ., et al. 2011. Hum Mutat. 32: E2050-60. PMID: 21972112
6. Increasing βB1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R.  |  Wang, S., et al. 2013. Biochim Biophys Acta. 1832: 302-11. PMID: 23159606
7. The N-terminal extension of βB1-crystallin chaperones β-crystallin folding and cooperates with αA-crystallin.  |  Leng, XY., et al. 2014. Biochemistry. 53: 2464-73. PMID: 24669963
8. Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain.  |  Qi, LB., et al. 2016. Protein Cell. 7: 501-15. PMID: 27318838
9. Cataract-Causing S93R Mutant Destabilized Structural Conformation of βB1 Crystallin Linking With Aggregates Formation and Cellular Viability.  |  Ren, L., et al. 2022. Front Mol Biosci. 9: 844719. PMID: 35359596
10. Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates.  |  Zhang, Y., et al. 2023. Int J Biol Macromol. 242: 124722. PMID: 37148932

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-βB1-crystallin Antibody (A-8) has 0 citations in a variety of scientific publications.

Primary antibodies like Anti-βB1-crystallin Antibody (A-8) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

βB1-crystallin Antibody (A-8) Specifications

Alternate Product Name: βB1-crystallin

Product Clone Name: A-8

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgM kappa light chain

Amino Acids: 65-103

Epitope Target: βB1-crystallin

Epitope Species: human

Product Reactivity/Detection: βB1-crystallin

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, ELISA

Vialing Information: Each vial contains 200 µg IgM kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 0 citations in various scientific publications

Available Conjugates/Forms for βB1-crystallin Antibody (A-8): P: Blocking Peptide

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