MTS-4-NHS is a bifunctional ADC linker combining NHS ester and thiol-reactive methanethiosulfonate (MTS) groups. It enables efficient amine-thiol conjugation, widely used in developing cleavable, disulfide-based antibody-drug conjugates for controlled drug delivery.
Structure of 690632-55-4
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Capabilities & Facilities
MTS-4-NHS is a chemical compound commonly utilized in the field of biochemical research for its ability to modify proteins and peptides. Here are some key applications of MTS-4-NHS:
Protein Modification: MTS-4-NHS is widely used in laboratories to introduce sulfhydryl-reactive groups into proteins and peptides. This facilitates the conjugation of proteins with other biomolecules, which is essential for creating bioconjugates such as antibody-drug conjugates. These modifications are particularly useful in developing targeted therapies and diagnostic tools.
Labeling and Detection: In proteomics studies, MTS-4-NHS is employed to label proteins with fluorescent dyes or other reporter molecules. This labeling allows researchers to track proteins within cells or visualize protein interactions in real time. The precise modification capability of MTS-4-NHS enhances the sensitivity and specificity of detection assays.
Cross-Linking Applications: MTS-4-NHS serves as a cross-linking agent to stabilize protein complexes or to study protein-protein interactions. By forming covalent bonds between specific protein sites, researchers can analyze the structural conformation of multi-protein assemblies. This application is crucial for understanding cellular machinery and developing novel therapeutics.
Surface Immobilization: MTS-4-NHS is utilized in biotechnological applications to immobilize biomolecules on surfaces, such as in sensor devices or affinity chromatography. This immobilization is key for developing biosensors that can detect various biological analytes with high sensitivity and specificity. The stable attachment of proteins to surfaces ensures consistent and reliable performance in diagnostic applications.
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