Maintenance Notice ( 4:15 AM - 3:55 PM May 24, 2025): This website is scheduled to be unavailable due to maintenance. We appreciate your patience and understanding.
Published TCIMAIL newest issue No.198
Maximum quantity allowed is 999
Please select the quantity
Biotinylated Inhibitor for the Detection of Protein Activity by Stripping
Most peptide-type protease inhibitors interact with the active site of the protease. Once these inhibitors are bound to the protease, they must be removed from the protease by macro-dilution or protein denaturation. However, KNI1293 biotin, a biotinylated HIV-1 (human immunodeficiency virus type 1) protease inhibitor,1,2) can be removed (stripped) by streptavidin after binding to the protease.3) The biotinylated protease inhibitor-streptavidin binding shift phenomenon is expected to be used to study the activity of protease-related diseases.
Related Product
References
- 1) Small-Sized Human Immunodeficiency Virus Type-1 Protease Inhibitors Containing Allophenylnorstatine to Explore the S2‘ Pocket
- 2) Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin
- 3) Acquired Removability of Aspartic Protease Inhibitors by Direct Biotinylation
