CAS 146987-10-2: FMOC-LYS(BIOTIN)-OH

M06251 - Fmoc-Lys(Biotin)-OH

Fmoc-Lys(biotinyl)-OH

Bachem ID: 4026175.

Fmoc-Lys(Biotin)-OH is a biotin-conjugated peptide that is used as a reagent to measure the protease activity in cancer tissues. It has been shown to have effector protein binding properties and to inhibit the growth of influenza virus. Fmoc-Lys(Biotin)-OH has been shown to inhibit the production of epidermal growth factor by its receptor binding activity, which may be due to its ability to block the action of proteases that are involved in activating this growth factor. Fmoc-Lys(Biotin)-OH has also been shown to have protease activity against bladder carcinoma cells.

Fmoc-Lys(Biotin)-OH is a biotin-reactive derivative of the lysine amino acid. It is used to study the interactions between bacterial pathogens and human cells. Fmoc-Lys(Biotin)-OH has been shown to inhibit the growth of P. aeruginosa in thp-1 cells, which are immortalized human lung epithelial cells. This drug also inhibits the synthesis of proteins in the cell nuclei, which prevents the development of bacterial colonies on solubilized cell nuclei in human serum. The effects of Fmoc-Lys(Biotin)-OH have been observed using an unlabeled drug and preincubation with unlabeled protein to observe cytosolic protein synthesis inhibition. A confocal microscope was used to show that Fmoc-Lys(Biotin)-OH inhibited recombinant proteins that bind to human pathogens, such as Staphylococcus a

Nα-Fmoc-Nε-biotinyl-L-lysine is useful in the synthesis of site-specific biotinylated probes.This Thermo Scientific Chemicals brand product was originally part of the Alfa Aesar product portfolio. Some documentation and label information may refer to the legacy brand. The original Alfa Aesar product / item code or SKU reference has not changed as a part of the brand transition to Thermo Scientific Chemicals.

Applications Nα-Fmoc-Nε-biotinyl-L-lysine is used in the synthesis of site-specific biotinylated probes. References Macielag, M., et al.: Int. J. Pep. Protein Res., 44, 582 (1994)