MMP-13 Substrate is a designed peptide incorporating recognition residues tailored for matrix metalloproteinase cleavage. Researchers use it to monitor catalytic turnover, specificity signatures, and kinetic behavior. Its balanced polarity and aromatic content enable precise mechanistic studies.
CAT No: R2291
CAS No:1872435-02-3
Synonyms/Alias:MMP-13 Substrate;1872435-02-3;Dnp-Gly-Pro-Leu-Gly-Met-Arg-Gly-Leu-NH2 pound>>Dnp-GPLGMRGL-NH2 pound>>Matrix Metalloproteinase-13 Substrate pound>>MMP-13 Substrate;HY-P2414;DA-52644;PD077002;CS-0133766;(2S)-N-[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]-1-[2-(2,4-dinitroanilino)acetyl]pyrrolidine-2-carboxamide;Dnp-(Leu421)-Collagen Type VIII alpha1 Chain (419-426) amide (human, mouse) trifluoroacetate salt;
MMP-13 Substrate is a specialized peptide compound designed to serve as a highly specific target for matrix metalloproteinase-13 (MMP-13) enzymatic activity assays. As a member of the matrix metalloproteinase substrate family, it is engineered with a precise peptide sequence that is selectively recognized and cleaved by MMP-13, an enzyme implicated in extracellular matrix remodeling and various physiological as well as pathological processes. This substrate is widely utilized in biochemical research to elucidate the functional dynamics of MMP-13, providing a robust platform for the investigation of proteolytic activity, enzyme kinetics, and inhibitor screening. Its synthetic peptide structure ensures reproducibility and specificity, making it an essential tool for advancing understanding in the field of metalloproteinase biology.
Enzyme Activity Assays: MMP-13 Substrate is extensively used in fluorometric or colorimetric assays to quantitatively measure the catalytic function of MMP-13 in vitro. By incorporating a reporter group that emits a detectable signal upon cleavage, the substrate enables real-time monitoring of enzyme kinetics and substrate turnover. This facilitates detailed characterization of MMP-13 activity under varying experimental conditions, supporting studies on enzyme regulation, activation mechanisms, and the influence of cofactors or other modulators. The specificity of the peptide sequence ensures minimal cross-reactivity with other metalloproteinases, thereby enhancing assay precision.
Inhibitor Screening: The substrate plays a pivotal role in high-throughput screening platforms for the identification and characterization of small-molecule inhibitors targeting MMP-13. By providing a reliable readout of enzymatic cleavage, it allows researchers to assess the potency, selectivity, and mode of action of candidate inhibitors in a controlled biochemical context. This application is particularly valuable for drug discovery programs focused on diseases where aberrant MMP-13 activity contributes to tissue degradation, as it supports the rational design and optimization of inhibitory compounds.
Protease Specificity Profiling: Researchers utilize the substrate to delineate the substrate specificity and cleavage preferences of MMP-13 relative to other matrix metalloproteinases. Comparative studies employing panels of related substrates enable the mapping of sequence determinants that govern enzyme-substrate recognition. Insights gained from such profiling inform the development of selective probes, contribute to the understanding of protease function in matrix remodeling, and aid in distinguishing MMP-13 activity from that of closely related family members in complex biological samples.
Biomarker Validation: In translational research, the substrate is employed to validate MMP-13 as a potential biomarker for tissue remodeling, inflammation, or degenerative conditions in preclinical models. By quantifying enzyme activity in biological fluids or tissue extracts using the substrate, investigators can correlate proteolytic activity with disease progression, therapeutic intervention, or physiological states. This approach enhances the reliability of biomarker studies by providing a direct functional readout rather than relying solely on protein expression levels.
Peptide-Based Mechanistic Studies: The defined sequence of MMP-13 Substrate supports mechanistic investigations into the structural and functional determinants of proteolytic cleavage. By introducing sequence variations or chemical modifications, researchers can probe the influence of individual amino acid residues or peptide conformations on enzyme-substrate interactions. Such studies deepen understanding of substrate recognition, cleavage efficiency, and resistance to proteolysis, contributing to the broader field of peptide biochemistry and enzyme engineering.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More