B Cell-based Immunoprecipitation Assay

Introduction of the Immunoprecipitation Assay

Immunoprecipitation is a simple and well-established method to identify proteins that interact with specific proteins and is widely used for antibody and antigen separation and characterization. Immunoprecipitation is a powerful biochemical method used for identifying interacting proteins. In this assay, protein A, protein G, or target antigen-specific antibodies conjugated to solid support material like beads or sepharose are used to identify proteins that interact. Using detergents to disrupt cell membranes combined with an immunoprecipitation assay, we can analyze antibody-antigen epitope binding interaction and identify antigenic epitopes within an antigen.

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Fig.1 The principle of the immunoprecipitation technique. (Creative Biolabs Original)

Fig.1 Illustration of the immunoprecipitation technique.

What We Can Offer

Antibodies in Assay	Immobilized Antibody before Precipitation	Capture the Epitope-antibody Complex after Binding
Commercial antibodies. Reliable and reproducible commercial antibodies are used for the immunoprecipitation of antigenic peptides. Custom antibody production. We also have a robust antibody development platform to produce high-quality antibodies to customers' interests.	The antibody can be linked to magnetic beads or agarose beads via protein A/G to detect antigens in cell samples. The pre-immobilized antibody on support is the recommended approach and is widely used in IP.	In another similar protocol, unbound antibodies are first inoculated with antigens to form an immunocomplex and then captured by beads. The free antibody approach is adopted when the target antigen concentration is low / the binding of the antibody to the target antigen is slow and weak.

Highlights

Precision Epitope Mapping

Our assay distinguishes between both linear and conformational epitopes, providing a complete structural understanding of antibody-antigen binding. This level of detail is crucial for advanced drug and biomarker development projects.

Timely and Efficient Service

We are committed to a high-efficiency workflow that delivers accurate and actionable results. Our streamlined process ensures your project stays on track with timely reporting and consistent communication.

Expert Analytical Support

Our team of multi-skilled analytical specialists possesses deep expertise in protein science and IP. They meticulously design and execute each experiment to ensure robust and reliable data.

Partnership for Success

Beyond a service, we offer a collaborative partnership. We work closely with you to understand your research goals, ensuring our approach is perfectly aligned to deliver the insights you need.

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Customer Reviews

Efficiency and Tangible Benefits

The streamlined workflow and detailed reports from Creative Biolabs greatly facilitated our antibody validation process. We were able to confirm our lead candidate's binding to its target in its native form, which was a critical step we were struggling with. - A. L***g.

Customer Service

We chose Creative Biolabs for their reputation and were impressed by their team's proactive communication. They guided us on the necessary starting materials and provided updates at every stage, making a complex project feel simple and manageable. - R. C*****n.

FAQs

What is the primary advantage of B cell-based IP over traditional methods?

The primary advantage is the exceptional specificity and affinity of the antibodies used. Derived from natural immune responses, these antibodies are highly refined, resulting in significantly cleaner data with less non-specific background, which is crucial for identifying genuine protein interactions.

Can this assay be used to study post-translational modifications?

Yes, absolutely. The B cell-based immunoprecipitation assay is ideal for this. Since it is designed to capture proteins in their native conformation, it can effectively pull down modified proteins and their interacting partners, providing a more accurate picture of their biological state.

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