Enzyme Substrate Sets
The most efficient way to study enzyme activity and enzyme substrate specificity (e.g. for phosphatase substrates, kinase substrates or protease substrates) is by incubating the enzyme of interest with multiple enzyme substrates or enzyme ligands (peptide sets) in parallel. JPT Peptide Technologies offers Enzyme Substrate Sets with Kinase Substrates, Phosphatase Substrates and Protease Substrates.
Our ready-to-screen peptide sets are comprised of large numbers of enzyme substrate peptides derived from human phosphorylation sites (phosphatase substrate and kinase subtrates) or cleavage sites (protease substrates), which were carefully selected from scientific databases or publications. The Enzyme Substrate Sets with substrates for kinase, substrates for phosphatase or substrates for protease come in 96- or 384-well microtiter plates, each well containing one specific enzyme substrate.
Read-out is optimized for each enzyme class. Kinase Substrates are incubated with radioactive (hot) ATP and detected by radioautography, whereas the phosphatase substrate set uses phosphate binding dyes for read-out. Protease substrates are internally quenched (Dabcyl/EDANS), therefore fluorescence read-out is applicable.
For details, please have a look at the application protocols.
Available Enzyme Substrate Sets
Applications for Enzyme Substrate Sets
- Identification of kinase substrates, phosphatase substrates or protease substrates
- Determination of enzyme consensus sequences
- Identification of potential in vivo substrates and enzyme inhibitors
- Elucidation of signal transduction pathways
- Reliable identification of contaminating enzymes
Benefits of Enzyme Substrate Sets
- Screen hundreds of potential enzyme substrates simultaneously at low cost
- Save time for HTS-Assay development
- Learn more about the biology of your enzyme
- Determine kinetic constants
Testimonials for Enzyme Substrate Sets
“We were very pleased with how easy it was to do the experiment (with Kinase Substrate Sets) using the equipment we had on hand - for example, we just used our 8-channel micropipette to add the enzyme/ATP mix.“
Betty A. Eipper, Ph.D, University of Connecticut, Farmington, CT, USA
“For several years, my group at the Tumor Biology Center has been using JPT’s Protease Profiling Tools for analyzing the substrate specificity of tumor-associated proteases as well as for identifying cancer specific protease patterns.”
Dr. Felix Kratz (Clinic for Tumor Biology, Freiburg, Germany)
"Our research relies heavily on developing robust high-throughput screens with fluorescent peptides. We have found that JPT’s are the best on the market because the signal-to-noise ratio is very high, providing the sensitivity we need for the screens. Their peptides always perform well. In addition, the knowledge, wonderful customer support, and fast turnaround time provided by JPT have been invaluable in helping us develop the best peptides for our assays."
Professor Carla Koehler, PhD (UCLA, Los Angeles, CA, USA)
References for Enzyme Substrates Sets
Structural Characterization of Zinc-bound Zmp1, a Zinc-dependent Metalloprotease Secreted by Clostridium Difficile
Rubino et al., J Biol Inorg Chem. (2015) – PMID: 26711661
Matrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates with Pleiotropic Functions
Schlage et al., Mol Cell Proteomics. (2015) - PMID: 26475864
Insights into the Molecular Evolution of HslU ATPase through Biochemical and Mutational Analyses
Sung et al., PloS One (2014) - PMID: 25050622
Generation and Characterization of Antibodies Specific for Caspase-cCeaved Neo-Epitopes: a Novel Approach
Therien et al., Antimicrob. Agents Chemother. (2012) - PMID: 22710113
Proteolytic Cleavage of Covalently Linked Cell Wall Proteins by Candida Albicans Sap9 and Sap10
Ai et al., Cell Death and Disease (2011) - PMID: 21881607
Broadening the Spectrum of β-Lactam Antibiotics through Inhibition of Signal Peptidase Type I
Schild et al., Eukaryot. Cell (2010) - PMID: 21097664 Characterization of the Catalytic Activity of the Membrane-anchored Metalloproteinase ADAM15 in Cell-based Assays
Maretzky et al., Biochem. J. (2009) - PMID: 19207106
Related Products and Services
Single Kinase Substrate Peptides
The substrates represent 13meric peptides derived from phosphorylation sites of human proteins. Please select from the list of nearly 800 peptides currently available.
Enzyme Peptide Microarrays
Kinase Peptide Microarrays: Peptide microarrays containing either annotated human phosphorylation site derived peptides or randomly generated peptide for identification of kinase substrates and profiling of kinase substrate specificities (also available with full incubation service).
Phosphorylation Site Detectors: Compilation of kinase substrate peptides on ready-to-use peptide microarrays.
Peptide Microarray Assay Service
Profiling service using high content enzyme substrate microarrays.