βB1-crystallin Antibody (H-3): sc-48335

βB1-crystallin Antibody (H-3) is a mouse monoclonal IgG1 kappa light chain antibody that detects βB1-crystallin of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-βB1-crystallin antibody (H-3) is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. βB1-crystallin plays a crucial role in maintaining the structural integrity and transparency of the vertebrate eye lens, which is essential for proper vision. Located primarily in the lens fibers, βB1-crystallin contributes to the refractive properties of the lens by forming a highly organized structure that minimizes light scattering. This organization is vital for optimal visual acuity, as any disruption in the crystallin structure can lead to cataract formation and impaired vision. βB1-crystallin′s ability to form dimers and higher-order aggregates is essential for lens transparency, and interactions with other crystallins help stabilize the lens architecture. Understanding βB1-crystallin function and importance is critical for research into lens-related diseases and potential therapeutic interventions.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

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βB1-crystallin Antibody (H-3) References:

1. The short 5' untranslated region of the betaA3/A1-crystallin mRNA is responsible for leaky ribosomal scanning.  |  Werten, PJ., et al. 1999. Mol Biol Rep. 26: 201-5. PMID: 10532316
2. Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization.  |  Gangalum, RK., et al. 2004. J Biol Chem. 279: 43374-7. PMID: 15339919
3. The P23T cataract mutation causes loss of solubility of folded gammaD-crystallin.  |  Evans, P., et al. 2004. J Mol Biol. 343: 435-44. PMID: 15451671
4. Transcriptional regulation of mouse alphaB- and gammaF-crystallin genes in lens: opposite promoter-specific interactions between Pax6 and large Maf transcription factors.  |  Yang, Y., et al. 2004. J Mol Biol. 344: 351-68. PMID: 15522290
5. The small heat shock protein alpha B-crystallin is a novel inhibitor of TRAIL-induced apoptosis that suppresses the activation of caspase-3.  |  Kamradt, MC., et al. 2005. J Biol Chem. 280: 11059-66. PMID: 15653686
6. The benefits of being β-crystallin heteromers: βB1-crystallin protects βA3-crystallin against aggregation during co-refolding.  |  Wang, S., et al. 2011. Biochemistry. 50: 10451-61. PMID: 22032798
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. Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation.  |  Leng, XY., et al. 2016. Biochem J. 473: 2087-96. PMID: 27208166
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
11. Beta A3/A1-crystallin association: role of the N-terminal arm.  |  Hope, JN., et al. 1994. Protein Eng. 7: 445-51. PMID: 8177894
12. Association properties of betaB2- and betaA3-crystallin: ability to form dimers.  |  Hejtmancik, JF., et al. 1997. Protein Eng. 10: 1347-52. PMID: 9514125

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 (H-3) has 3 citations in a variety of scientific publications.

Primary antibodies like Anti-βB1-crystallin Antibody (H-3) 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 (H-3) Specifications

Alternate Product Name: βB1-crystallin

Product Clone Name: H-3

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG₁ kappa light chain

Amino Acids: 1-252

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 IgG₁ kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 3 citations in various scientific publications

Available Conjugates/Forms for βB1-crystallin Antibody (H-3): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin