Biotinylated Mhc-ig
Biotinylated Mhc-ig - Related Videos
07:59
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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Cited by 21 •
2014
Biochemical assays with recombinant human MHC II molecules can provide rapid, quantitative insights into immunogenic epitope identification, deletion, or design. Here, a peptide-MHC II binding assay scaled to 384-well plates is described. This cost effective format should prove useful in the fields of protein deimmunization and vaccine design and development.
09:13
Cell-surface Biotinylation Assay
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2023
A cell can regulate the amount of particular proteins on its cell membrane through endocytosis, following which cell surface proteins are effectively sequestered in the cytoplasm. Once within a cell, these surface proteins can be either destroyed or “recycled” back to the membrane. The cell surface biotinylation assay provides researchers with a way to study these phenomena. The technique makes use of a derivative of the small molecule biotin, which can label surface proteins and then be...
07:18
HLA-Ig Based Artificial Antigen Presenting Cells for Efficient ex vivo Expansion of Human CTL
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Cited by 17 •
2011
A new DC independent method for induction and expansion of antigen-specific T cells is described. HLA A2-Ig based artificial Antigen Presenting Cells (aAPC) are loaded with HLA-A2 restricted peptides to efficiently expand CTL of diverse antigen specificity. This technology holds great potential for CTL-based adoptive immunotherapy.
04:54
Evaluation of Controlled T Cell Activation with a Photoactivatable Peptide MHC
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2025
This video demonstrates a method of decaging a photoactivatable peptide-major histocompatibility complex using UV irradiation. The decaging process exposes the native peptide sequence, enabling precise T cell activation.
01:29
Assessing Impaired MHC-I Antigen Presentation in Immune Cells Infected with Bacteria
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2026
Start with an immune cell culture infected with pathogenic bacteria that form intracellular inclusion bodies.The bacterial infection impairs the antigen presentation pathway in the immune cells.Take an uninfected culture as a control.Next, add a model protein antigen and incubate.Immune cells internalize, process, and present the model antigen-derived peptides on MHC-I molecules.After incubation, wash the cells to remove any unprocessed antigen.Fix the cells, then add a quenching agent to...
FAQs
The immunoglobulin domain provides a fused protein framework that supports the soluble MHC component and its defined peptide. This engineered architecture also contributes to a modular format that can be modified through biotin-based handling. As a result, researchers can adapt the same general construct for detection, immobilization, or comparative studies of peptide-dependent T-cell recognition.
Biotin provides a specific attachment point for streptavidin, allowing biotinylated MHC-Ig molecules to form multimers. Multimer formation increases avidity, meaning the combined binding strength for matching T-cell receptors becomes greater than that of an individual interaction. This amplification helps make antigen-specific T cells more readily detectable in assays designed to measure recognition.
The MHC component displays a defined peptide, so recognition depends on whether a T-cell receptor matches that peptide-MHC combination. This arrangement links molecular design to cellular specificity: changing the presented peptide changes the recognition target being examined. Consequently, the construct can support focused analysis of antigen-specific populations rather than general T-cell binding.
Its separate functional elements provide distinct engineering roles: the MHC presents peptide, the immunoglobulin domain forms part of the soluble fusion architecture, and biotin enables streptavidin-mediated attachment or multimerization. Because these features operate together in one construct, researchers can apply it to detection, isolation, characterization, or surface-based analysis without changing the fundamental recognition design.
In flow cytometry, the construct can label cells bearing T-cell receptors that recognize the displayed peptide-MHC combination, enabling detection of antigen-specific populations. The same labeling principle can support cell sorting when researchers need to isolate those cells for further characterization. The multimeric format is useful because increased avidity strengthens the observable interaction during analysis.
Surface-based assays use the biotin-streptavidin interaction to present or immobilize the engineered MHC-Ig construct. This format enables examination of how peptide presentation and T-cell receptor recognition behave at an assay surface, rather than only in suspended cells. Such measurements can contribute to characterization of antigen-specific responses and comparison of engineered molecular configurations.
Researchers can select the platform when they need to identify, isolate, or characterize T cells directed against a defined antigenic peptide. In engineering studies, its modular construction supports investigation of peptide presentation, molecular attachment, and avidity-enhanced recognition. The same capabilities create potential relevance for diagnostic or therapeutic strategy development, while preserving a direct connection to immune-cell specificity.