Tyrosinase Inhibitor Screening Kit (Colorimetric) provides a rapid, simple, sensitive, and reliable test suitable for high-throughput screening of tyrosinase inhibitors. Tyrosinase catalyzes the oxidation of tyrosine, producing a chromophore that can be detected at OD = 510 nm. In the presence of kojic Acid, a reversible inhibitor of tyrosinase, the rate of oxidation of the substrate is decreased.
Tyrosinase or polyphenol oxidase is an oxidoreductase that participates in the biosynthesis of melanin, a ubiquitous biological pigment found in hair, eyes, skin, etc. Inhibition of tyrosinase has been a long-time target in the skin health research, cosmetics and agricultural industries because of its role in browning reactions in skin pigmentation and during fruit harvesting and handling.
Water-soluble, substrate for sortase mediated labeling of proteins. Sortase catalyzes a transpeptidase reaction between a specific internal sequence of a protein and an amine group present on the N-terminus of triglycine recently has become an area of great interest. This method of labeling proteins has been denoted as “Sortagging”. Proteins conjugated to DBCO-Gly-Gly-Gly can be further modified with azide-containing molecules creating site-specific protein conjugates. Examples of creating protein conjugates using sortagging include site-specifically PEGylating proteins,1 site-specific protein-lipid conjugates,2 and constructing peptides and glycosylphosphatidylinositol chimeras.3 Sortase has also been used in peptide synthesis to cyclize peptides to create macrocyclic peptides, glycopeptides4 and protein−protein conjugates.
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Water-soluble, substrate for sortase mediated labeling of proteins. Sortase catalyzes a transpeptidase reaction between a specific internal sequence of a protein and an amine group present on the N-terminus of triglycine recently has become an area of great interest. This method of labeling proteins has been denoted as “Sortagging”. Proteins conjugated to DBCO-Gly-Gly-Gly can be further modified with azide-containing molecules creating site-specific protein conjugates. Examples of creating protein conjugates using sortagging include site-specifically PEGylating proteins,1 site-specific protein-lipid conjugates,2 and constructing peptides and glycosylphosphatidylinositol chimeras.3 Sortase has also been used in peptide synthesis to cyclize peptides to create macrocyclic peptides, glycopeptides4 and protein−protein conjugates.