390 MMP FRET Substrate 2

Product Name: 390 MMP FRET Substrate 2

Sequence One Letter Code: Mca-PLGL-Dap(Dnp)-AR

Sequence Three Letter Code: Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-OH

Chemical Formula:C43H65N11O12

Molecular Weight: 1094.2

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C Protected from light

Research Area: peptide substrate

Source / Species: Bovine

Conjugation: Conjugated

Conjugation Type: Double dyes

Code Nacres: NA.26

Application: 390 MMP FRET Substrate 2 is a fluorogenic peptide designed for broad detection of matrix metalloproteinase activity in biochemical and cellular systems. Matrix metalloproteinases are zinc-dependent endopeptidases responsible for extracellular matrix degradation and regulation of signaling molecules involved in inflammation, angiogenesis, apoptosis, and tissue remodeling. This substrate functions as a generic reporter for multiple MMP family members, enabling overall assessment of proteolytic activity in complex samples. In its intact state, fluorescence quenching is maintained through resonance energy transfer. Proteolytic cleavage disrupts quenching and produces a measurable fluorescence increase with excitation and emission wavelengths of 325 and 393 nm. The substrate is suitable for kinetic analysis, comparative enzyme profiling, and inhibitor screening applications. It provides a convenient tool for evaluating MMP activity in cancer biology, inflammatory disease research, and extracellular matrix regulation studies.

Current Research: 390 MMP FRET Substrate 2 is a fluorogenic peptide engineered for broad detection of matrix metalloproteinase (MMP) activity in biochemical assays and cell-based systems. Matrix metalloproteinases comprise a family of zinc-dependent endopeptidases that regulate extracellular matrix (ECM) turnover and process signaling molecules involved in inflammation, angiogenesis, apoptosis, and tissue remodeling. Because multiple MMP isoforms are often co-expressed in pathological conditions, a generic substrate capable of reporting overall proteolytic activity is highly valuable for comprehensive enzymatic assessment. This substrate functions as a pan-MMP reporter, incorporating a cleavage sequence recognized by several MMP family members. Rather than targeting a single isoform, it enables detection of cumulative metalloproteinase activity within purified enzyme preparations, conditioned media, tissue extracts, or complex biological samples. Such versatility supports both mechanistic studies and translational investigations where multiple MMPs contribute to disease progression. The assay principle is based on fluorescence resonance energy transfer (FRET). In the intact peptide, a donor fluorophore and a corresponding quencher are positioned in close proximity, resulting in efficient energy transfer and suppression of fluorescence emission. Upon proteolytic cleavage by active MMPs, spatial separation of the donor and quencher disrupts FRET, leading to a measurable increase in fluorescence intensity. The released signal can be detected at excitation and emission wavelengths of approximately 325 nm and 393 nm, respectively. Because fluorescence generation directly correlates with substrate cleavage, enzymatic activity can be monitored continuously in real time or quantified at defined endpoints. 390 MMP FRET Substrate 2 is well suited for kinetic analyses of metalloproteinase activity. Researchers can determine reaction rates, evaluate enzyme concentration–dependent responses, and calculate kinetic parameters such as apparent Km and catalytic efficiency under controlled conditions. Continuous fluorescence monitoring enhances temporal resolution and reduces the need for secondary detection reagents, streamlining assay workflows. The substrate is also valuable for comparative profiling across different MMP isoforms. By testing individual enzymes or mixtures, investigators can assess relative cleavage efficiency and characterize substrate specificity patterns. This is particularly relevant in cancer and inflammatory diseases, where dysregulated MMP expression contributes to tumor invasion, metastasis, and tissue destruction. Profiling overall proteolytic activity provides insight into disease-associated remodeling processes and microenvironmental dynamics. In drug discovery applications, 390 MMP FRET Substrate 2 supports inhibitor screening and potency evaluation. The fluorescence-based readout offers a robust assay window compatible with microplate formats and automated high-throughput platforms. Candidate small molecules, peptides, or biologics targeting metalloproteinases can be assessed by measuring reductions in fluorescence increase relative to untreated controls. Such assays facilitate structure–activity relationship studies and optimization of selective MMP inhibitors. Beyond oncology, the substrate is widely applied in research on chronic inflammatory disorders, wound healing, fibrosis, and vascular remodeling. In cell-based experiments, it enables quantification of secreted MMP activity under physiologically relevant conditions, supporting investigation of regulatory pathways that control enzyme activation and inhibition. Overall, 390 MMP FRET Substrate 2 provides a convenient and sensitive tool for monitoring matrix metalloproteinase activity. Its FRET-based detection mechanism, compatibility with kinetic and high-throughput formats, and utility in complex biological systems make it an effective reagent for studying extracellular matrix regulation and protease-driven pathophysiology in both basic and translational research settings.