Z gly pro arg amc

Manufactured by Bachem

Sourced in United Kingdom, United States

Z-Gly-Pro-Arg-AMC is a laboratory reagent composed of the peptide sequence Z-Gly-Pro-Arg linked to the fluorogenic reporter molecule 7-amino-4-methylcoumarin (AMC). This compound is commonly used as a substrate for the detection and measurement of proteolytic enzyme activity, particularly trypsin-like serine proteases.

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Lab products found in correlation

Acetyl ile glu pro asp amc, by Bachem (2 mentions) Infinite m1000, by Tecan (2 mentions) Z phe arg amc, by Bachem (1 mentions) H gly phe 7 amino 4 methylcoumarin amc, by Bachem (1 mentions) H arg amc, by Bachem (1 mentions) Ca 074, by Bachem (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions) Anti ddk antibody, by OriGene (1 mentions) Ca074, by Peptide Institute (1 mentions) Trypsin edta, by Thermo Fisher Scientific (1 mentions) Dimethyl sulfoxide (dmso), by Merck Group (1 mentions) Sodium bicarbonate, by Merck Group (1 mentions) Dulbecco s modified eagle s medium, by Merck Group (1 mentions)

Close spelling variants of this product

Z-Gly-Gly-Arg-AMC Z-Gly-Pro-AMC Z-Arg-Arg-AMC Gly-Pro-Arg-Pro Gly-Pro-AMC

4 protocols using z gly pro arg amc

Recombinant Serpins Inhibit MASPs

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To investigate whether the F. hepatica recombinant serpins inhibit native serum-derived MASPs, samples of NHS diluted 1:10 in barbital buffer were incubated with either rFhSrp1 (1 μM), rFhSrp2 (1 μM), rFhSrps (1 μM), FUT-175 (100 μM) or PBS at RT for 25 min and then added to S. cerevisiae mannan-coated plates (20 μg/mL). The plates were incubated at 37°C for 5 min before the addition of the fluorogenic substrate, Z-Gly-Pro-Arg-AMC (20 μM; Bachem, UK). The proteolytic activity of serum derived MASPs was measured continuously over 1 hr at 37°C in a PolarStar Omega Spectrophotometer as relative fluorescent units (RFU). All assays were carried out in triplicate and the average activity, presented as a percentage, was calculated relative to the activity within the NHS-PBS sample, set as 100% activity. Serum MASPs activity was also determined in the NHS in which F. hepatica NEJ were cultured and compared to the NHS-control incubated without NEJ.

De Marco Verissimo C., Jewhurst H.L., Dobó J., Gál P., Dalton J.P, & Cwiklinski K. (2022). Fasciola hepatica is refractory to complement killing by preventing attachment of mannose binding lectin (MBL) and inhibiting MBL-associated serine proteases (MASPs) with serpins. PLoS Pathogens, 18(1), e1010226.

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Granzyme B and A Activity Assay

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The enzyme activities were determined using acetyl-Ile-Glu-Pro-Asp-AMC (50 µM) and Z-Gly-Pro-Arg-AMC (200 µM; both from Bachem) for granzyme B and A, respectively. The following assay buffers were used: 50 mM Tris-HCl and 100 mM NaCl, pH 7.4 (for granzyme B) and 20 mM Tris and 150 mM NaCl, pH 8.1 (for granzyme A). Whole-cell lysates were first activated in assay buffer for 30 min at 37 °C. The substrate was then added, and the formation of fluorescent products was measured continuously on a microplate reader Infinite M1000 (Tecan, Männedorf, Switzerland).

Perišić Nanut M., Pawelec G, & Kos J. (2021). Human CD4+ T-Cell Clone Expansion Leads to the Expression of the Cysteine Peptidase Inhibitor Cystatin F. International Journal of Molecular Sciences, 22(16), 8408.

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Fluorometric Enzyme Activity Assay

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Enzyme activities were determined using the following substrates: 70 µM H-Gly-Phe-7-amino-4-methylcoumarin (AMC) (Bachem) for cathepsin C, 20 µM H-Arg-AMC (Bachem) for cathepsin H, 50 µM Z-Phe-Arg-AMC for cathepsin L (Bachem), 50 µM acetyl-Ile-Glu-Pro-Asp-AMC for granzyme B (Bachem), and 200 µM Z-Gly-Pro-Arg-AMC for granzyme A (Bachem). The following assay buffers were used: 25 mM MES, 100 mM NaCl, 5 mM cysteine, pH 6 (for cathepsin C); 100 mM MES, 2 mM EDTA, 5 mM cysteine, pH 6.5 (for cathepsins H and L); 50 mM Tris-HCl, 100 mM NaCl, pH 7.4 (for granzyme B); and 20 mM Tris, 150 mM NaCl, pH 8.1 (for granzyme A). Whole-cell lysates were first activated in assay buffer for 15 min at RT for cathepsins or for 30 min at 37 °C for granzymes. The substrate was then added, and formation of fluorescent products was measured continuously on a microplate reader Infinite M1000 (Tecan, Männedorf, Switzerland). To determine cathepsin L activity, 5 µM of irreversible inhibitor of cathepsin B, CA-074 (Bachem), was added before the addition of substrate.

Prunk M., Perišić Nanut M., Jakoš T., Sabotič J., Švajger U, & Kos J. (2020). Extracellular Cystatin F Is Internalised by Cytotoxic T Lymphocytes and Decreases Their Cytotoxicity. Cancers, 12(12), 3660.

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Cathepsin Inhibitor Assay Protocol

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Dulbecco’s modified Eagle’s medium, sodium bicarbonate, antibiotics, dimethyl sulfoxide, and other chemicals, unless otherwise stated, were obtained from Sigma (St. Louis, MO, USA). Fetal bovine serum and trypsin-EDTA were obtained from Fisher Scientific (Waltham, MA, USA). The fluorogenic substrate Z-Gly-Pro-Arg-AMC was purchased from Bachem (King of Prussia, PA, USA). CA074 was purchased from Peptides International (Louisville, KY, USA) and CK inhibitor L-873724 (Compound 1) was obtained from (Merck-Frosst, Canada) (Gauthier et al., 2008 (link)) Compounds 2 (Palmer et al., 2005 (link)), 3 (Yamashita et al., 1997 ), 4 (Altmann et al., 2006 (link)) and 5 (Respondek et al., 2014 (link)) were synthesized using literature protocols. DQ- collagen I substrate was from Life Technologies (Carlsbad, CA, USA) and Cultrex ^™ (reconstituted basement membrane; rBM) was from Trevigen (Gaithersburg, MD, USA). Rabbit anti-human CK antibodies were purchased from Abcam (Cambridge, MA, USA) and anti-DDK antibodies were from OriGene (Rockville, MD, USA). Horseradish peroxidase-labeled goat anti-rabbit IgG was from Pierce (Rockford, IL, USA).

Herroon M.K., Sharma R., Rajagurubandara E., Turro C., Kodanko J.J, & Podgorski I. (2016). Photoactivated inhibition of cathepsin K in a 3D tumor model. Biological chemistry, 397(6), 571-582.

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