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camostat (BPS Bioscience)

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Structured Review

BPS Bioscience camostat
Camostat, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tmprss2+fluorogenic+assay+kit/TMPRSS2+Fluorogenic+Assay+Kit/pmc12910020-108-0-1
Average 94 stars, based on 20 article reviews

camostat - by Bioz Stars, 2026-11

94/100 stars

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In Vitro:

Article Title: Diphyllin elicits a doubled-pronged attack on the entry of SARS-CoV-2 by inhibiting cathepsin L and furin
Article Snippet: .. In vitro activities of CTSL, furin, and TMPRSS2 were measured by cathepsin L inhibitor screening assay kit (BPS Bioscience, 79591), furin protease assay kit (BPS Bioscience, 78040), and TMPRSS2 fluorogenic assay kit (BPS Bioscience, 78083) according to the manufacturer's recommendation, respectively. .. Statistical analyses were performed using GraphPad Prism 8 software (GraphPad Software Inc., La Jolla, CA, USA).

Article Title: C-Terminal Analogues of Camostat Retain TMPRSS2 Protease Inhibition: New Synthetic Directions for Antiviral Repurposing of Guanidinium-Based Drugs in Respiratory Infections.
Article Snippet: .. In vitro activities of guanidinium drug analogues 1a–1e were measured by a TMPRSS2 fluorogenic assay kit (CAT # 780837 BPS Bioscience, San Diego, CA, USA) according to the manufacturer’s recommendations. ..

Article Title: Diphyllin elicits a doubled-pronged attack on the entry of SARS-CoV-2 by inhibiting cathepsin L and furin.
Article Snippet: .. In vitro activities of CTSL, furin, and TMPRSS2 were measured by cathepsin L inhibitor screening assay kit (BPS Bioscience, 79591), furin protease assay kit (BPS Bioscience, 78040), and TMPRSS2 fluorogenic assay kit (BPS Bioscience, 78083) according to the manufacturer’s recommendation, respectively. .. Statistical analyses were performed using GraphPad Prism 8 software (GraphPad Software Inc., La Jolla, CA, USA).

Article Title: C-Terminal Analogues of Camostat Retain TMPRSS2 Protease Inhibition: New Synthetic Directions for Antiviral Repurposing of Guanidinium-Based Drugs in Respiratory Infections
Article Snippet: .. In vitro activities of guanidinium drug analogues 1a – 1e were measured by a TMPRSS2 fluorogenic assay kit (CAT # 780837 BPS Bioscience, San Diego, CA, USA) according to the manufacturer’s recommendations. ..

Screening Assay:

Protease Assay:

Analogues:

Article Title: C-Terminal Analogues of Camostat Retain TMPRSS2 Protease Inhibition: New Synthetic Directions for Antiviral Repurposing of Guanidinium-Based Drugs in Respiratory Infections
Article Snippet: .. In vitro activities of guanidinium drug analogues 1a – 1e were measured by a TMPRSS2 fluorogenic assay kit (CAT # 780837 BPS Bioscience, San Diego, CA, USA) according to the manufacturer’s recommendations. ..

Inhibition:

Article Title: Natural fucoidans inhibit coronaviruses by targeting viral spike protein and host cell furin.
Article Snippet: Fucoidans are a class of long chain sulfated polysaccharides and have multiple biological functions.. Herein, four natural fucoidans extracted from Fucus vesiculosus, F. serratus, Laminaria japonica and Undaria pinnatifida, were tested for their HCoV-OC43 inhibition and found to demonstrate EC50 values ranging from 0.15 to 0.61 μg/mL.. * Corresponding author.

Control:

Activity Assay:

Article Title: Novel compounds with dual inhibition activity against SARS-CoV-2 critical enzymes RdRp and human TMPRSS2.
Article Snippet: COVID-19 caused major worldwide problems.. The spread of variants and limited treatment encouraged the design of novel anti-SARS-CoV-2 compounds.. A series of compounds RH1-23 were designed to dually target RNA-dependent RNA polymerase (RdRp) and transmembrane serine protease 2 (TMPRSS2).

Biomarker Discovery:

Article Title: Targeting the Neuropilin-1 receptor with Ovatodiolide and progress in using periodontal ligament organoids for COVID-19 research and therapy.
Article Snippet: The discovery of SARS-CoV-2 RNA in the periodontal tissues of patients who tested positive for COVID-19, 24 days post the initial symptom onset, indicates the oral cavity could serve as a viral reservoir.. This research aims to investigate the antiviral capabilities of Ovatodiolide, introducing a novel periodontal ligament organoid model for the study of SARS-CoV-2.. We have successfully established a reliable and expandable organoid culture from the human periodontal ligament, showcasing characteristics typical of epithelial stem cells.

Image Search Results

( A ) Schematic of in-silico docking screen workflow. A panel of 48 respiratory proteases and 10 SERPINs upregulated upon viral infection were assembled. 3D structures were generated, with annotated protease active sites and SERPIN reactive center loops (RCLs). SERPIN-protease docking was performed using HADDOCK, guiding the RCL into the protease active site, and obtaining raw HADDOCK scores to reflect predicted binding energies. The dataset was normalized to the mean, and thresholds set for high-confidence in-silico binders (mean of positive controls) and high-confidence in-silico non-binders (mean of negative controls). Top-scoring complexes of interest were visually assessed for 3D RCL fit, exosite formation, and the positioning of protease active residues relative to SERPIN P4-P4’ residues. ( B ) Heatmap of docking results, with z-scores centered to the mean of control SERPIN-protease pairs and normalized for each SERPIN. The darker the red, the more favorable the binding energies. LEI leukocyte elastase inhibitor encoded by SERPINB1 , PAI-2 plasminogen activator inhibitor 2 encoded by SERPINB2 , Leupin encoded by SERPINB4 , PI-8 protease inhibitor 8 encoded by SERPINB8 , CAP-3 cytoplasmic anti-protease 3 encoded by SERPINB9 , Bomapin encoded by SERPINB10 , Headpin encoded by SERPINB13, ATIII antithrombin 3 encoded by SERPINC1, PAI-1 plasminogen activator inhibitor 1 encoded by SERPINE1, C1-INH C1 inhibitor encoded by SERPING1 . V validated pairs in vitro as shown in Fig. . ( C ) Normalized HADDOCK scores of PAI-1 with its positive controls (thrombin, active TMPRSS2, trypsin, kallikrein, uPA), negative controls (furin, uPA to PAI-1 P4-P4’ alanine substitutions, and uPA to PAI-1 P1 mutant R346A), the TMPRSS2 zymogen (TMPRSS2-z), and cathepsins. Green dotted line (mean of all positive controls in the in-silico screen) is the threshold for high-confidence binders; red dotted line (mean of all negative controls in the in-silico screen) is the threshold for high-confidence non-binders. Symbols: triangles, trypsin-like proteases; circles, subtilisin-like proteases; split circle, thrombin; hexagon, kallikreins; diamonds, cathepsins; light blue inactive serine protease, inactive; blue, serine proteases; yellow, cysteine proteases; salmon, aspartic proteases. Blue, serine proteases; yellow, cysteine proteases; red, aspartic proteases. ( D – F ) Docking structures of top-scoring complexes for PAI-1 with TMPRSS2 (zymogen), PAI-1 with TMPRSS2 (active) and CTSL, respectively. .

Journal: The EMBO Journal

Article Title: Host cell and viral protease targets of human SERPINs identified by in silico docking

doi: 10.1038/s44318-025-00546-6

Figure Lengend Snippet: ( A ) Schematic of in-silico docking screen workflow. A panel of 48 respiratory proteases and 10 SERPINs upregulated upon viral infection were assembled. 3D structures were generated, with annotated protease active sites and SERPIN reactive center loops (RCLs). SERPIN-protease docking was performed using HADDOCK, guiding the RCL into the protease active site, and obtaining raw HADDOCK scores to reflect predicted binding energies. The dataset was normalized to the mean, and thresholds set for high-confidence in-silico binders (mean of positive controls) and high-confidence in-silico non-binders (mean of negative controls). Top-scoring complexes of interest were visually assessed for 3D RCL fit, exosite formation, and the positioning of protease active residues relative to SERPIN P4-P4’ residues. ( B ) Heatmap of docking results, with z-scores centered to the mean of control SERPIN-protease pairs and normalized for each SERPIN. The darker the red, the more favorable the binding energies. LEI leukocyte elastase inhibitor encoded by SERPINB1 , PAI-2 plasminogen activator inhibitor 2 encoded by SERPINB2 , Leupin encoded by SERPINB4 , PI-8 protease inhibitor 8 encoded by SERPINB8 , CAP-3 cytoplasmic anti-protease 3 encoded by SERPINB9 , Bomapin encoded by SERPINB10 , Headpin encoded by SERPINB13, ATIII antithrombin 3 encoded by SERPINC1, PAI-1 plasminogen activator inhibitor 1 encoded by SERPINE1, C1-INH C1 inhibitor encoded by SERPING1 . V validated pairs in vitro as shown in Fig. . ( C ) Normalized HADDOCK scores of PAI-1 with its positive controls (thrombin, active TMPRSS2, trypsin, kallikrein, uPA), negative controls (furin, uPA to PAI-1 P4-P4’ alanine substitutions, and uPA to PAI-1 P1 mutant R346A), the TMPRSS2 zymogen (TMPRSS2-z), and cathepsins. Green dotted line (mean of all positive controls in the in-silico screen) is the threshold for high-confidence binders; red dotted line (mean of all negative controls in the in-silico screen) is the threshold for high-confidence non-binders. Symbols: triangles, trypsin-like proteases; circles, subtilisin-like proteases; split circle, thrombin; hexagon, kallikreins; diamonds, cathepsins; light blue inactive serine protease, inactive; blue, serine proteases; yellow, cysteine proteases; salmon, aspartic proteases. Blue, serine proteases; yellow, cysteine proteases; red, aspartic proteases. ( D – F ) Docking structures of top-scoring complexes for PAI-1 with TMPRSS2 (zymogen), PAI-1 with TMPRSS2 (active) and CTSL, respectively. .

Article Snippet: TMPRSS2 Activity Assay Kit , BPS Bioscience , #78083.

Techniques: In Silico, Infection, Generated, Binding Assay, Control, Protease Inhibitor, In Vitro, Mutagenesis

( A , B ) Normalized reaction rates for uPA, TMPRSS2, cathepsin L, and cathepsin B in the absence or presence of PAI-1 ( A ), or PAI-2 ( B ) from in vitro fluorometric assays. Statistical analysis by One-way ANOVA and Kruskal–Wallis test, * P < 0.05. Exact P values in ( A ). uPA, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; TMPRSS2, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; CTSL, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; CTSB, 0 vs. 0.025 nM P > 0.9999, 0 vs. 0.25 nM P = 0.5934. Exact P values in ( B ). uPA, 0 vs. 1 nM P = 0.3594, 0 vs. 10 nM P = 0.0146; TMPRSS2, 0 vs. 1 nM P > 0.9999, 0 vs. 10 nM P = 0.9121; CTSL, 0 vs. 1 nM P > 0.9999, 0 vs. 10 nM P = 0.0722; CTSB, 0 vs. 1 nM P = 0.3594, 0 vs. 10 nM P = 0.0146. Mean ± SD, n = 3 replicates. Raw data in Dataset EV . ( C ) SDS-PAGE and silver stain of mixed recombinant active uPA (32 kDa, not visible) and PAI-1 (43 kDa). ( D ) SDS-PAGE and silver stain of mixed recombinant active TMPRSS2 (31 kDa) and PAI-1 (43 kDa). ( E ) SDS-PAGE and silver stain of mixed recombinant cathepsin L (32 kDa) and PAI-1 (43 kDa). *Denotes use of PAI-1 inhibitor triplaxinin and PAI-1 cleavage products. (F) SDS-PAGE and silver stain of mixed recombinant cathepsin L with PAI-1, reactions were conducted at pH 6.5 and pH 5.5. ( G ) SDS-PAGE and silver stain of mixed recombinant cathepsin B with PAI-1. ( H ) Schematic of importance of activity of TMPRSS2 and cathepsin L in SARS-CoV-2 entry by lineage. .

Journal: The EMBO Journal

Article Title: Host cell and viral protease targets of human SERPINs identified by in silico docking

doi: 10.1038/s44318-025-00546-6

Figure Lengend Snippet: ( A , B ) Normalized reaction rates for uPA, TMPRSS2, cathepsin L, and cathepsin B in the absence or presence of PAI-1 ( A ), or PAI-2 ( B ) from in vitro fluorometric assays. Statistical analysis by One-way ANOVA and Kruskal–Wallis test, * P < 0.05. Exact P values in ( A ). uPA, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; TMPRSS2, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; CTSL, 0 vs. 0.025 nM P = 0.3594, 0 vs. 0.25 nM P = 0.0146; CTSB, 0 vs. 0.025 nM P > 0.9999, 0 vs. 0.25 nM P = 0.5934. Exact P values in ( B ). uPA, 0 vs. 1 nM P = 0.3594, 0 vs. 10 nM P = 0.0146; TMPRSS2, 0 vs. 1 nM P > 0.9999, 0 vs. 10 nM P = 0.9121; CTSL, 0 vs. 1 nM P > 0.9999, 0 vs. 10 nM P = 0.0722; CTSB, 0 vs. 1 nM P = 0.3594, 0 vs. 10 nM P = 0.0146. Mean ± SD, n = 3 replicates. Raw data in Dataset EV . ( C ) SDS-PAGE and silver stain of mixed recombinant active uPA (32 kDa, not visible) and PAI-1 (43 kDa). ( D ) SDS-PAGE and silver stain of mixed recombinant active TMPRSS2 (31 kDa) and PAI-1 (43 kDa). ( E ) SDS-PAGE and silver stain of mixed recombinant cathepsin L (32 kDa) and PAI-1 (43 kDa). *Denotes use of PAI-1 inhibitor triplaxinin and PAI-1 cleavage products. (F) SDS-PAGE and silver stain of mixed recombinant cathepsin L with PAI-1, reactions were conducted at pH 6.5 and pH 5.5. ( G ) SDS-PAGE and silver stain of mixed recombinant cathepsin B with PAI-1. ( H ) Schematic of importance of activity of TMPRSS2 and cathepsin L in SARS-CoV-2 entry by lineage. .

Article Snippet: TMPRSS2 Activity Assay Kit , BPS Bioscience , #78083.

Techniques: In Vitro, SDS Page, Silver Staining, Recombinant, Activity Assay

( A – C ) Schematic of fit of substrate residues into protease pockets for uPA, TMPRSS2, and cathepsin L, respectively. Substrates include zymogen self-cleavage region, canonical or previously described substrate, PAI-1 and fluorophore-linked peptide substrate used in this study. Amino acids are colored according to their side chain chemistry (Unipro UGENE): basic (R, K) litmus blue with R being more basic and darker; acidic (E, D) litmus red with more acidic being darker; hydrophobic (I, L, V, A), yellow with intensity corresponding to hydrophobic character; sulfur-containing (C, M) green; aromatic (F, Y, W) in teal; polar (N, Q, S, T) magenta/pink with darker coloring for more polarity; non-polar glycine (G) in dark gray and proline (P) in light gray. Assembled from references (Koga et al, ; Menard et al, ; Rossignol et al, ; Shrimp et al, ) and UNIPROT.

Journal: The EMBO Journal

Article Title: Host cell and viral protease targets of human SERPINs identified by in silico docking

doi: 10.1038/s44318-025-00546-6

Figure Lengend Snippet: ( A – C ) Schematic of fit of substrate residues into protease pockets for uPA, TMPRSS2, and cathepsin L, respectively. Substrates include zymogen self-cleavage region, canonical or previously described substrate, PAI-1 and fluorophore-linked peptide substrate used in this study. Amino acids are colored according to their side chain chemistry (Unipro UGENE): basic (R, K) litmus blue with R being more basic and darker; acidic (E, D) litmus red with more acidic being darker; hydrophobic (I, L, V, A), yellow with intensity corresponding to hydrophobic character; sulfur-containing (C, M) green; aromatic (F, Y, W) in teal; polar (N, Q, S, T) magenta/pink with darker coloring for more polarity; non-polar glycine (G) in dark gray and proline (P) in light gray. Assembled from references (Koga et al, ; Menard et al, ; Rossignol et al, ; Shrimp et al, ) and UNIPROT.

Article Snippet: TMPRSS2 Activity Assay Kit , BPS Bioscience , #78083.

Techniques:

( A – D ) SARS-CoV-2 WA-1 ( A , B ) or Omicron BA.1 ( C , D ) multi-cycle infection in Calu-3 cells with extracellular addition of buffer, 12.5 or 25 ng/mL of active PAI-1 or of 25 ng/mL heat-inactivated (HI) PAI-1 (48 hpi); or 10 or 100 ng/mL anti-PAI-1 depleting antibody or 10 ng/mL isotype IgG control (48 hpi) by high-content microscopy. Statistical analysis by One-way ANOVA and Holm-Sidak’s multiple comparison test, ** P < 0.005. Exact P values in ( A ). buffer vs. HI rPAI-1 P = 0.9407; buffer vs. rPAI-1 P < 0.0001; anti-PAI-1 (1:100) vs. IgG control P = 0.0059; anti-PAI-1 (1:50) vs. IgG control P < 0.0001. Exact P values in ( C ). buffer vs. HI rPAI-1 P = 0.5441; buffer vs. rPAI-1 P < 0.0001; IgG vs. anti-PAI-1 (1:100) P = 0.7968; IgG vs. anti-PAI-1 (1:50) P = 0.1473. n = 6 biological replicates. Representative images, DAPI (blue, nuclei), SARS-CoV-2 nucleoprotein (red). ( E ) Extracellular titers of SARS-CoV-2 WA-1 grown at low MOI-infection on Calu-3 cells for 48 h. Infectious titers were determined by TCID 50 assay on Calu-3. Statistical analysis by one-sided t test, * P < 0.05.Exact P value P = 0.05, n = 3 biological replicates ( F ). BHK cells co-transfected to express SARS-CoV-2 spike, TMPRSS2, and PAI-1. Spike S2 and 2’ band intensities by western blot and densitometry. % S2’ cleaved determined by ratio of S2’ vs S2’ + S2 band intensity from the blot shown. FL full-length. ( G ) BHK cells co-transfected to express SARS-CoV-2 spike and TMPRSS2, and rPAI-1 or buffer control added to the cell supernatant. Spike S2 and 2’ band intensities by western blot and densitometry. S2’ % cleaved determined by the ratio of S2 vs S2’ band intensity from the blot shown. FL full-length. .

Journal: The EMBO Journal

Article Title: Host cell and viral protease targets of human SERPINs identified by in silico docking

doi: 10.1038/s44318-025-00546-6

Figure Lengend Snippet: ( A – D ) SARS-CoV-2 WA-1 ( A , B ) or Omicron BA.1 ( C , D ) multi-cycle infection in Calu-3 cells with extracellular addition of buffer, 12.5 or 25 ng/mL of active PAI-1 or of 25 ng/mL heat-inactivated (HI) PAI-1 (48 hpi); or 10 or 100 ng/mL anti-PAI-1 depleting antibody or 10 ng/mL isotype IgG control (48 hpi) by high-content microscopy. Statistical analysis by One-way ANOVA and Holm-Sidak’s multiple comparison test, ** P < 0.005. Exact P values in ( A ). buffer vs. HI rPAI-1 P = 0.9407; buffer vs. rPAI-1 P < 0.0001; anti-PAI-1 (1:100) vs. IgG control P = 0.0059; anti-PAI-1 (1:50) vs. IgG control P < 0.0001. Exact P values in ( C ). buffer vs. HI rPAI-1 P = 0.5441; buffer vs. rPAI-1 P < 0.0001; IgG vs. anti-PAI-1 (1:100) P = 0.7968; IgG vs. anti-PAI-1 (1:50) P = 0.1473. n = 6 biological replicates. Representative images, DAPI (blue, nuclei), SARS-CoV-2 nucleoprotein (red). ( E ) Extracellular titers of SARS-CoV-2 WA-1 grown at low MOI-infection on Calu-3 cells for 48 h. Infectious titers were determined by TCID 50 assay on Calu-3. Statistical analysis by one-sided t test, * P < 0.05.Exact P value P = 0.05, n = 3 biological replicates ( F ). BHK cells co-transfected to express SARS-CoV-2 spike, TMPRSS2, and PAI-1. Spike S2 and 2’ band intensities by western blot and densitometry. % S2’ cleaved determined by ratio of S2’ vs S2’ + S2 band intensity from the blot shown. FL full-length. ( G ) BHK cells co-transfected to express SARS-CoV-2 spike and TMPRSS2, and rPAI-1 or buffer control added to the cell supernatant. Spike S2 and 2’ band intensities by western blot and densitometry. S2’ % cleaved determined by the ratio of S2 vs S2’ band intensity from the blot shown. FL full-length. .

Article Snippet: TMPRSS2 Activity Assay Kit , BPS Bioscience , #78083.

Techniques: Infection, Control, Microscopy, Comparison, Transfection, Western Blot

Review

camostat (BPS Bioscience)

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In Vitro:

Screening Assay:

Protease Assay:

Analogues:

Inhibition:

Control:

Activity Assay:

Biomarker Discovery:

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