Product Description
Suc-Leu-Leu-Val-Tyr-AMC is a substrate peptide with fluorescent color reaction. The C-terminal is a fluorescent coumarin, the N-terminal is blocked by succinic anhydride, and the active group is a carboxyl group. When producing Suc-Leu-Leu-Val-Tyr-AMC, the peptide fragment Suc-Leu-Leu-Val is synthesized first, and finally coumarin is connected.
AI Product Description
*The following content is generated by AI and is for reference only.
Suc-Leu-Leu-Val-Tyr-AMC is a widely utilized chromogenic substrate specifically designed for the quantitative analysis of lysosomal proteases, with a primary focus on cathepsin L and, to a lesser extent, cathepsin B. Chemically designated by the CAS number 120863-74-9, this peptide consists of four amino acid residues—succinyl (Suc), leucine (Leu), leucine (Leu), valine (Val), and tyrosine (Tyr)—capped at the C-terminus with 7-amino-4-methylcoumarin (AMC). The molecular formula is typically represented as C32H45N5O8, though exact variations may occur depending on specific salt forms or hydration states associated with commercial preparations.
The fundamental mechanism of action relies on the release of the fluorescent AMC group upon enzymatic cleavage. In its intact state, the substrate exhibits minimal fluorescence due to intramolecular quenching. However, when specific proteases recognize and hydrolyze the peptide bond preceding the tyrosine residue, the AMC moiety is liberated. This free fluorophore displays intense blue-green fluorescence under ultraviolet excitation (typically around 380 nm) with an emission maximum near 460 nm. This dramatic increase in signal intensity allows researchers to monitor enzyme kinetics with high sensitivity and specificity using standard microplate readers or spectrofluorometers.
In biomedical research, Suc-Leu-Leu-Val-Tyr-AMC serves as a critical tool for studying protein degradation pathways, particularly within the ubiquitin-proteasome system and lysosomal compartments. It is extensively employed in drug discovery programs aimed at developing selective inhibitors for cysteine proteases involved in various pathological conditions, including cancer metastasis, viral infections, and autoimmune disorders. Furthermore, it aids in characterizing the expression levels and catalytic activities of cathepsins in different tissue types, providing insights into cellular homeostasis and disease progression. Its reliability and well-defined kinetic parameters make it a standard reagent in both academic laboratories and industrial pharmaceutical settings for screening potential therapeutic agents targeting proteolytic enzymes.