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Results for "

peptide bond hydrolysis

" in MedChemExpress (MCE) Product Catalog:

7

Inhibitors & Agonists

5

Peptides

1

MCE Kits

Targets Recommended:
Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-P2661
    FA-Leu-Gly-Pro-Ala-OH

    		Biochemical Assay Reagents Bacterial Infection
    FA-Leu-Gly-Pro-Ala-OH is a furylacryloyl-terminal tetrapeptide that serves as a substrate for bacterial collagenase and spirochete metalloendopeptidase. FA-Leu-Gly-Pro-Ala-OH is specifically hydrolyzed by spirochete collagenase only at the Leu-Gly bond. FA-Leu-Gly-Pro-Ala-OH can be used to determine the equilibrium constant of peptide bond hydrolysis, and also to detect collagenase-mediated cleavage reactions via turbidimetry based on absorbance reduction .
    FA-Leu-Gly-Pro-Ala-OH
  • HY-E70574
    Trypsin/Lys-C complex protease (MS grade)

    		Biochemical Assay Reagents Others
    Trypsin/Lys-C complex protease (MS grade) combines Trypsin and Lys-C, two recombinant proteases, to achieve efficient peptide bond hydrolysis. Trypsin specifically cleaves the C-terminal peptide bonds of arginine (R) and lysine (K), while Lys-C specifically cleaves the C-terminal peptide bonds of lysine (K). This combination overcomes issues such as the slower digestion rate of lysine and arginine by rTrypsin, PTM changes on lysine, or hydrophobic C-termini (such as proline) that can lead to missed cleavage. Trypsin/Lys-C complex protease (MS grade) can be used to process complex protein samples that are difficult to enzymatically digest. Trypsin/Lys-C complex protease (MS grade) can be used for protein characterization, single-cell proteomics and large cohort proteomics studies.
    Trypsin/Lys-C complex protease (MS grade)
  • HY-P5377
    Abz-HPGGPQ-EDDnp

    Cathepsin K substrate

    		 Ser/Thr Protease Others
    Abz-HPGGPQ-EDDnp (Cathepsin K substrate) is a biological active peptide. (Cathepsins are a class of globular lysosomal proteases, playing a vital role in mammalian cellular turnover. They degrade polypeptides and are distinguished by their substrate specificities. Cathepsin K is the lysosomal cysteine protease involved in bone remodeling and resorption. It has potential as a drug target in autoimmune diseases and osteoporosis.This FRET peptide can be used to monitor selectively cathepsin K activity in physiological fluids and cell lysates. Abz-HPGGPQ-EDDnp [where Abz represents o-aminobenzoic acid and EDDnp represents N -(2, 4-dinitrophenyl)-ethylenediamine], a substrate initially developed for trypanosomal enzymes, is efficiently cleaved at the Gly-Gly bond by cathepsin K. This peptide is resistant to hydrolysis by cathepsins B, F, H, L, S and V, Ex/Em=340 nm/420 nm.)
    Abz-HPGGPQ-EDDnp
  • HY-P5415
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS

    		HIV Others
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is a biological active peptide. (DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is also called HIV protease substrate I in some literature. It is widely used for the continuous assay for HIV protease activity. The 11-Kd protease (PR) encoded by the human immunodeficiency virus 1 (HIV-1) is essential for the correct processing of viral polyproteins and the maturation of infectious virus, and is therefore a target for the design of selective acquired immunodeficiency syndrome (AIDS) therapeutics. The FRET-based fluorogenic substrate is derived from a natural processing site for HIV-1 PR. Incubation of recombinant HIV-1 PR with the fluorogenic substrate resulted in specific cleavage at the Tyr-Pro bond and a time-dependent increase in fluorescence intensity that is linearly related to the extent of substrate hydrolysis. The fluorescence quantum yields of the HIV-1 PR substrate in the FRET assay increased by 40.0- and 34.4-fold, respectively, per mole of substrate cleaved. Because of its simplicity and precision in the determination of reaction rates required for kinetic analysis, this substrate offers many advantages over the commonly used HPLC or electrophoresis-based assays for peptide substrate hydrolysis by retroviral PRs. Abs/Em = 340nm/490nm.)
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS
  • HY-E70964A
    Leucine Aminopeptidase, Porcine

    		Aminopeptidase Metabolic Disease
    Leucine Aminopeptidase, Porcine (EC 3.4.11.1) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. Leucine Aminopeptidase, Porcine (EC 3.4.11.1) rapidly catalyzes the hydrolysis of leucine containing peptides and also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins.
    Leucine Aminopeptidase, Porcine
  • HY-P2661A
    FA-Leu-Gly-Pro-Ala-OH TFA

    		Biochemical Assay Reagents Bacterial Infection
    FA-Leu-Gly-Pro-Ala-OH TFA is a furylacryloyl-terminal tetrapeptide that serves as a substrate for bacterial collagenase and spirochete metalloendopeptidase. FA-Leu-Gly-Pro-Ala-OH TFA is specifically hydrolyzed by spirochete collagenase only at the Leu-Gly bond. FA-Leu-Gly-Pro-Ala-OH TFA can be used to determine the equilibrium constant of peptide bond hydrolysis, and also to detect collagenase-mediated cleavage reactions via turbidimetry based on absorbance reduction .
    FA-Leu-Gly-Pro-Ala-OH TFA
  • HY-P11734
    Suc-AAPY-pNA

    		Ser/Thr Protease Others
    Suc-AAPY-pNA is an oligptide compound and protease substrate. Suc-AAPY-pNA undergoes hydrolysis by proteases at the peptide bond between tyrosine and p-nitroaniline, releasing p-nitroaniline with an absorption peak at OD410. Suc-AAPY-pNA functions as a substrate in preclinical assays for measuring activity of acidic, neutral, and alkaline proteases .
    Suc-AAPY-pNA

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