pepstatin  (Roche)


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    Structured Review

    Roche pepstatin
    CD18 labeling ratio (sheared/unsheared) of circulating rat neutrophils measured with flow cytometry in response to fluid shear (5 dyne/cm 2 ) with the following protease inhibitors: control, GM6001, tumor necrosis factor α protease inhibitor-1 (TAPI-1), and 1,10-phenanthroline (phenan) ( A ); control, PMSF, elastatinal, amastatin, and bestatin ( B ); and control, phosphoramidon (phospho), E-64, <t>pepstatin,</t> and chymostatin ( C ). n = 4 animals in each group. *, P = 0.023 vs. control.
    Pepstatin, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin/product/Roche
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin - by Bioz Stars, 2021-05
    86/100 stars

    Images

    1) Product Images from "Regulation of CD18 expression on neutrophils in response to fluid shear stress"

    Article Title: Regulation of CD18 expression on neutrophils in response to fluid shear stress

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.2336130100

    CD18 labeling ratio (sheared/unsheared) of circulating rat neutrophils measured with flow cytometry in response to fluid shear (5 dyne/cm 2 ) with the following protease inhibitors: control, GM6001, tumor necrosis factor α protease inhibitor-1 (TAPI-1), and 1,10-phenanthroline (phenan) ( A ); control, PMSF, elastatinal, amastatin, and bestatin ( B ); and control, phosphoramidon (phospho), E-64, pepstatin, and chymostatin ( C ). n = 4 animals in each group. *, P = 0.023 vs. control.
    Figure Legend Snippet: CD18 labeling ratio (sheared/unsheared) of circulating rat neutrophils measured with flow cytometry in response to fluid shear (5 dyne/cm 2 ) with the following protease inhibitors: control, GM6001, tumor necrosis factor α protease inhibitor-1 (TAPI-1), and 1,10-phenanthroline (phenan) ( A ); control, PMSF, elastatinal, amastatin, and bestatin ( B ); and control, phosphoramidon (phospho), E-64, pepstatin, and chymostatin ( C ). n = 4 animals in each group. *, P = 0.023 vs. control.

    Techniques Used: Labeling, Flow Cytometry, Cytometry, Protease Inhibitor

    2) Product Images from "Plasmodium Food Vacuole Plasmepsins Are Activated by Falcipains *"

    Article Title: Plasmodium Food Vacuole Plasmepsins Are Activated by Falcipains *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M708949200

    Cleavage site specificity of E-64 and pepstatin processing activities by radiosequencing. A , plot of [ 35 S]methionine activity released for each sequencing cycle of in vitro translated pro-PM II, which had been incubated with E-64 ( dotted line ) or pepstatin
    Figure Legend Snippet: Cleavage site specificity of E-64 and pepstatin processing activities by radiosequencing. A , plot of [ 35 S]methionine activity released for each sequencing cycle of in vitro translated pro-PM II, which had been incubated with E-64 ( dotted line ) or pepstatin

    Techniques Used: Activity Assay, Sequencing, In Vitro, Incubation

    Related Articles

    Inhibition:

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: To glean further insights into the underlying molecular process of protease inhibition by compound 1, we utilized a variation of Yonetani and Theorell analysis [ , ] to evaluate the binding mode. .. Since the inhibition by compound 1 is consistent with a non-competitive mechanism, which might predict that substrate may still bind to the protease active site when compound 1 is bound, Pepstatin A was used as a cross-competitive inhibitor for analysis. .. This method of inhibitor cross-competitive analysis allows determination of the degree to which the binding of compound 1 to protease influences the binding of the second inhibitor to the active site [ , , ].

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: This method of inhibitor cross-competitive analysis allows determination of the degree to which the binding of compound 1 to protease influences the binding of the second inhibitor to the active site [ , , ]. .. The choice of Pepstatin A was based on the ability to inhibit protease [ ], the well established biochemical and structural reports of its binding location in the active site [ ], that it has a competitive inhibition mechanism [ , ], and the reported use of Acetyl-pepstatin A for inhibitor cross-competitive studies for non-active site inhibitors [ ]. .. The graphical findings from a representative cross-competitive study utilizing compound 1 and Pepstatin A is shown .

    other:

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: In each case, non-parallel lines were obtained which converged at the x-axis, which is consistent with the interpretation that compound 1 and Pepstatin A may bind independent sites [ , , ].

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: The graphical findings from a representative cross-competitive study utilizing compound 1 and Pepstatin A is shown .

    Article Title: In-depth, reproducible analysis of human plasma using IgY 14 and SuperMix Immunodepletion
    Article Snippet: Final concentrations should be: 1μg/mL Leupeptin, 1 μg/mL Pepstatin-A, and 0.15mM PMSF.

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: Pepstatin A was used at concentrations from 0.6 to 3.0 µM, while compound 1 was held constant at 45, 30, 20, or 0 µM.

    Article Title: Glucocorticoid Elevation of Dexamethasone-induced Gene 2 (Dig2/RTP801/REDD1) Protein Mediates Autophagy in Lymphocytes *
    Article Snippet: As described under “Results,” the experiments were performed both in the presence and absence of lysosomal protease inhibitors, E64d (5 μg/ml) and pepstatin A (10 μg/ml).

    Binding Assay:

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries
    Article Snippet: This method of inhibitor cross-competitive analysis allows determination of the degree to which the binding of compound 1 to protease influences the binding of the second inhibitor to the active site [ , , ]. .. The choice of Pepstatin A was based on the ability to inhibit protease [ ], the well established biochemical and structural reports of its binding location in the active site [ ], that it has a competitive inhibition mechanism [ , ], and the reported use of Acetyl-pepstatin A for inhibitor cross-competitive studies for non-active site inhibitors [ ]. .. The graphical findings from a representative cross-competitive study utilizing compound 1 and Pepstatin A is shown .

    Purification:

    Article Title: An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
    Article Snippet: GST-Osh6p and mutants were expressed in E. coli (BL21-Gold(DE3) competent cells, Stratagene) at 30 °C overnight whereas the GST-PHFAPP and GST-C2Lact were expressed at 37 °C for 3 h upon induction with 1 mM IPTG (when the optical density (OD) of the bacterial suspension, measured at 600 nm, reached a value of 0.6). .. All purification steps were conducted in a buffer with 50 mM Tris, pH 7.4, 120 mM NaCl, 2 mM DTT, supplemented during the first purification steps with 1 mM PMSF, 1 µM bestatine, 10 µM pepstatine, 10 µM phosphoramidon and protease inhibitor tablets (Roche). .. Cells were lysed by a French press and the lysate was centrifuged at 200,000 × g for 1 h. The supernatant was applied to Glutathione Sepharose 4B beads.

    Protease Inhibitor:

    Article Title: An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
    Article Snippet: GST-Osh6p and mutants were expressed in E. coli (BL21-Gold(DE3) competent cells, Stratagene) at 30 °C overnight whereas the GST-PHFAPP and GST-C2Lact were expressed at 37 °C for 3 h upon induction with 1 mM IPTG (when the optical density (OD) of the bacterial suspension, measured at 600 nm, reached a value of 0.6). .. All purification steps were conducted in a buffer with 50 mM Tris, pH 7.4, 120 mM NaCl, 2 mM DTT, supplemented during the first purification steps with 1 mM PMSF, 1 µM bestatine, 10 µM pepstatine, 10 µM phosphoramidon and protease inhibitor tablets (Roche). .. Cells were lysed by a French press and the lysate was centrifuged at 200,000 × g for 1 h. The supernatant was applied to Glutathione Sepharose 4B beads.

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    Roche pepstatin a
    Comparison of active sites of P. falciparum plasmepsin II (PDB, 1LF3) and P. chabaudi plasmepsin (homology model) showing side chain variations. <t>Pepstatin</t> A residues (P) are shown bound to P. falciparum plasmepsin II binding sites (S). Prime and nonprime designations distinguish C-terminal from N-terminal sides of the cleavage site. Subsite pocket residue differences in P. falciparum versus P. chabaudi (residues in italics) are as follows: S4 (I290 T ), S3 (T114 I ), S2 (L292 V ), S1 (F111 L ), S1′ (V78 G ; N76 V ), S2′ (N76 V ) (all residues numbered according to PfPM-II numbering).
    Pepstatin A, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin a/product/Roche
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin a - by Bioz Stars, 2021-05
    86/100 stars
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    Comparison of active sites of P. falciparum plasmepsin II (PDB, 1LF3) and P. chabaudi plasmepsin (homology model) showing side chain variations. Pepstatin A residues (P) are shown bound to P. falciparum plasmepsin II binding sites (S). Prime and nonprime designations distinguish C-terminal from N-terminal sides of the cleavage site. Subsite pocket residue differences in P. falciparum versus P. chabaudi (residues in italics) are as follows: S4 (I290 T ), S3 (T114 I ), S2 (L292 V ), S1 (F111 L ), S1′ (V78 G ; N76 V ), S2′ (N76 V ) (all residues numbered according to PfPM-II numbering).

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Potencies of Human Immunodeficiency Virus Protease Inhibitors In Vitro against Plasmodium falciparum and In Vivo against Murine Malaria

    doi: 10.1128/AAC.50.2.639-648.2006

    Figure Lengend Snippet: Comparison of active sites of P. falciparum plasmepsin II (PDB, 1LF3) and P. chabaudi plasmepsin (homology model) showing side chain variations. Pepstatin A residues (P) are shown bound to P. falciparum plasmepsin II binding sites (S). Prime and nonprime designations distinguish C-terminal from N-terminal sides of the cleavage site. Subsite pocket residue differences in P. falciparum versus P. chabaudi (residues in italics) are as follows: S4 (I290 T ), S3 (T114 I ), S2 (L292 V ), S1 (F111 L ), S1′ (V78 G ; N76 V ), S2′ (N76 V ) (all residues numbered according to PfPM-II numbering).

    Article Snippet: To determine the in vitro effects of drugs on P. falciparum -parasitized erythrocytes, Dd2 ring-stage-parasitized erythrocytes were incubated for 20 h with 10 μM E64, pepstatin A, ritonavir, saquinavir (Fortivase; Roche), or atazanavir (Reyataz; Bristol-Myers Squibb).

    Techniques: Binding Assay

    Yonetani and Theorell plot of v/vi versus concentration of Pepstatin A and compound 1 0 µM of compound 1 (▼); 20 µM of compound 1 (▲); 30 µM of compound 1 (■); 45 µM of compound 1 (●) with varying concentrations of Pepstatin A. Each point was in triplicate and this is a representative result from 1 of 4 experiments. Assay conditions and curve fitting described in Materials and Methods.

    Journal: The Biochemical journal

    Article Title: Identification of Broad-Based HIV-1 Protease Inhibitors From Combinatorial Libraries

    doi: 10.1042/BJ20091645

    Figure Lengend Snippet: Yonetani and Theorell plot of v/vi versus concentration of Pepstatin A and compound 1 0 µM of compound 1 (▼); 20 µM of compound 1 (▲); 30 µM of compound 1 (■); 45 µM of compound 1 (●) with varying concentrations of Pepstatin A. Each point was in triplicate and this is a representative result from 1 of 4 experiments. Assay conditions and curve fitting described in Materials and Methods.

    Article Snippet: The graphical findings from a representative cross-competitive study utilizing compound 1 and Pepstatin A is shown .

    Techniques: Concentration Assay