Photoaffinity labeling has been demonstrated to be a remarkably efficient method for studying the interaction of biologically significant compounds (ligands) with their target macromolecules. The method allows identification of the target and also the binding domain within the target protein. An appropriate photoaffinity probe is usually prepared by attachment of a photoreactive labeling group and an indicator such as a biotin tag to the ligand molecule.
BCECF AM is a well known fluorescent probe that enables ratiometric monitoring of cellular pH. Intracellular pH plays an important role in modulating cellular events, including growth, calcium regulation, enzymatic activity, receptor-mediated signal transduction, ion transport, endocytosis, chemotaxis, adhesion and other cellular processes. Once inside, cellular esterases cleave the AM groups yielding a more hydrophilic BCECF trapped inside the cell. Wavelength Maxima: Excitation 505nm, Emission 520nm.
Fluorescence microscopy is currently probably the most widely used microscopy technique as it enables the molecular composition of the structures being observed to be identified through the use of fluorescently-labelled probes of high chemical specificity. These molecular and fluorescent probes can provide very powerful tools for localizing regions in which a particular gene is expressed in an organism, or in identifying the location of a particular protein.
The term bioorthogonal chemistry refers to any chemical reaction that can occur inside of living systems without interfering with native biochemical processes. Selective chemical reactions that are orthogonal to the diverse functionality of biological systems are now recognized as important tools in chemical biology. As important labeling strategies, bioorthogonal chemistry allows for selective covalent attachment of synthetic groups to biopolymers, such as proteins, nucleic acids, lipids, and glycans, are the key to many applications in biotechnology, medicine, and basic research. Such reactions have enabled the study of biomolecules in real time in living systems without interfering normal cellular functions. Bioorthogonal "click" reactions are now widely used in chemical biology for many applications such as activity-based protein profiling, monitoring cell proliferation, generating novel enzyme inhibitors, monitoring the synthesis of newly formed proteins, identifying protein targets, site-specific tagging of proteins, detection of DNA and RNA synthesis, visualization of glycans, detection of posttranslational modifications in proteins, and studying glycan processing.

BioMaxLab is dedicated to designing and developing novel probes for bioconjugation based on bioorthogonal chemistry. The probes we develop will be based on, but not limited to, a variety novel chemistry, such as photoinduced cycloaddition of diaryl tetrazole to alkene, copper-free click chemistry, strain promoted alkyne-azide cycloaddition (SPAAC), cross-metathesis with allyl sulfides and Diels-Alder reaction of tetrazine with cycloalkenem and so on.
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