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BRAND / VENDOR: Abcam

Abcam, ab249040, Anti-beta Crystallin A3 antibody [EPR9586] - BSA and Azide free

CATALOG NUMBER: ab249040
Regular price$0.99
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Product Description

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal beta Crystallin A3 antibody. Carrier free. Suitable for ICC/IF, WB and reacts with Human, Mouse, Rat samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR9586,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Mouse, Rat, Human,
Applications:ICC/IF, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
ab249040 is the carrier-free version of
ab151722
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Beta Crystallin A3 also known as CRYBA3 is a protein involved in the structural formation of the vertebrate eye lens. This protein belongs to the beta/gamma crystallin family characterized by double Greek key motifs. Beta Crystallin A3 has a molecular mass of approximately 24 kDa. It is synthesized in the lens fibers where it plays a role in maintaining transparency and refractive properties essential for vision. Other tissues may express it at much lower levels indicating its specific function in the lens.
Biological function summary
The protein plays a critical role in the formation of the lens's refractive index. It is not part of a complex but exists as a monomer unlike some other crystallins that form oligomers. Its function is to contribute to the lens's structural stability and its ability to focus light. The consistent production and maintenance of this protein are necessary to ensure the lens’s optical clarity over time which is vital for proper vision.
Pathways
Beta crystallin A3 interplays with stabilization pathways related to protein folding within the lens. It is connected to the cytoskeletal pathway which helps maintain the lens's shape and structure. Proteins such as alpha crystallins acting as chaperones interact with beta crystallins to prevent aggregation and maintain solubility in the dense environment of the lens.
Mutations in beta crystallin A3 associate with cataract formation in humans which leads to lens opacities and vision impairment. Cataracts are often linked with disruptions in protein folding and solubility. In this context the protein’s relationship with alpha crystallin is significant because alpha crystallin's chaperone activity can mitigate aggregation issues that lead to cataracts. Understanding these protein interactions helps develop therapeutic strategies to prevent or treat lens opacity.


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Collaboration

Tony Tang

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