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CreMap™ B Cell Epitope Mapping Service

Identification of the B cell epitopes has been widely used in the field of new therapeutics drug discovery, vaccines designing, and disease diagnostics.With the extensive experience in immunology, Creative Biolabs has developed a series of methods for screening B cell epitopes of a target protein.

Typical Methods of CreMap™ B Cell Epitope Mapping Service

Peptide/Protein Microarray Service

This technique takes advantage of a library of oligopeptide sequences from overlapping and non-overlapping segments of a target antigen and tests for their ability to bind the antibody of interest. This method is fast and relatively inexpensive, and specifically suited to the epitope profiling for a large number of candidate antibodies against a defined target. Read more…

Limited Proteolysis Coupled With Mass Spectrometry

Limited proteolysis method was invented several decades ago. Coupling with mass spectrometry ensures the high efficacy and precision Proteases with different restriction sites are applied to the antigen-antibody complex and the native antigen is treated in the same condition. The proteolytically robust paratope on the antibody protects the epitope from proteolysis. Fragments released from the different cleavage sites in the presence and absence of the antibody are detected by MS to reveal the bound fragments to the antibody. Read more…

Amide Hydrogen/Deuterium Exchange

Derived from the limited proteolysis method, amide hydrogen/deuterium exchange method takes advantage of the fact that a covalently bonded hydrogen atom would be replaced by a deuterium atom. When the antigen is diluted into a solution of D2O, Labile protons, such as those on primary amines, exchange nearly instantaneously. Meanwhile, the amides buried in the protein core or located interaction surfaces are protected against hydrogen exchange due to the limited solvent exposure and shows slower exchange kinetics. The antigen is mixed a deuterium buffer in solution, and the mixture was incubated for a series of time points before the exchange reaction is quenched by eluting out in a low pH buffer and digested by pepsin. The fragments would, therefore, be measured by HPLC and MS. Read more…

Nuclear Magnetic Resonance (NMR) Analysis

NMR emerges as a useful tool for epitope mapping analysis. Through NMR, the 3D-structure of the target protein could be constructed by measuring distances and angles between amino acids residues. For identifying epitopes, NMR analysis provides a detailed structure analysis for epitope-Fab interaction, therefore the nature of epitope recognition could be accurately explained. The NMR chemical shift map was developed to describe and determine the epitope residues by comparing changes in the NMR spectral signals before and after the formation of the antigen-antibody complex. Read more…

Surface Plasmon Resonance (SPR)

Monitored in real time, SPR is a powerful method for characterizing antigen-antibody interactions. The basic Surface plasmon resonance (SPR) analysis involves immobilizing the antigen on the sensor chip surface of a flow-cell, and then an antibody solution flows over the antigen and the sensor detects the changes in refractive index of the surface layer of a solution in contact with the sensor chip that is caused by a variation of the mass on the sensor chip surface. Real-time measurements allow for the calculation of the association and dissociation kinetic rate constants, ka and kd of the interaction. A small amount of reagent is required for SPR and no labeling or modification is needed before analysis. Read more…

Crystallography-based Methods

X-ray crystallography is the gold standard among all the epitope mapping methods. In this technique, the highly purified antigens are obtained and allowed to co-crystallize with their corresponding antibodies. Then, the atomic structure of the complex is solved using X-ray diffraction analysis. The amino acids that are within a distance of 4 Å of each other are considered to be counteracting. Accordingly, epitope regions of an antigen that contact with the antibody molecule could be identified. Obviously, this co-crystallization method is able to detect continuous linear epitopes as well. Read more…

Alanine Scanning Mutagenesis

High-throughput Mutagenesis Mapping is based on a comprehensive mutation library, in which residues of a target protein are substituted for a certain kind of amino acid (often alanine substitution) at selected positions by site-directed mutagenesis. All the plasmid clones from the mutation library are individually arrayed in microplates, expressed in mammalian cells and tested for their antibody binding capacity. Read more…

Microfluidic Peptide Microarray

Creative Biolabs has developed an advanced microfluidic microarray technology service for epitope mapping and other immunoassays, which utilizes the microfluidics during the process of synthesis of the arrays as well as the binding assay reactions. This technology could achieve high throughput peptide screening on a comprehensive scale. Read more…

Surface Display Methods

This technique is based on testing the binding capacity of a variety of peptides displayed on the surface of a bacteriophage to the monoclonal antibody of interest. The foreign DNA is inserted into the genome of bacteriophage. Viral peptides including the foreign DNA are then synthesized and displayed on the amino-terminal portion of the viral coat protein. After that, the binding ability of the peptide displayed on the phage surface to the antibody would be tested and the epitope mapping performed. Read more…

Creative Biolabs offers comprehensive as well as professional technologies for your epitope discovery and we are so honored to provide a customized schedule to help you with your research. If you are interested in our CreMap™ B cell epitope mapping, please contact us for more information and a detailed quote.




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