active human tmprss2 (Cusabio)
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Cusabio
active human tmprss2
Active Human Tmprss2, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tmprss2+expression+construct/TMPRSS2/pmc08547501-227-9-12
Average 93 stars, based on 21 article reviews
Active Human Tmprss2, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tmprss2+expression+construct/TMPRSS2/pmc08547501-227-9-12
Average 93 stars, based on 21 article reviews
active human tmprss2 - by Bioz Stars,
2026-09
93/100 stars
Images
1) Product Images from "Antiviral Potential of the Antimicrobial Drug Atovaquone against SARS-CoV-2 and Emerging Variants of Concern"
Article Title: Antiviral Potential of the Antimicrobial Drug Atovaquone against SARS-CoV-2 and Emerging Variants of Concern
Journal: ACS Infectious Diseases
doi: 10.1021/acsinfecdis.1c00278
Figure Legend Snippet: Atovaquone restricts wtVSV and VSV-SARS spike infectivity in VeroE6 and VeroE6 hTMPRSS2-hACE2 cells. VeroE6 cells or VeroE6 cells stably transduced with hACE2 and TMPRSS2 were seeded at 2.5 × 10 4 cells/cm 2 in 96-well plates and treated with various concentrations of atovaquone. Fifteen minutes later, cells were infected at an MOI of 1 with wtVSV-spike (Whelan strain) or wtVSV expressing GFP. Eleven hours postinfection, cells were imaged and GFP counts were obtained using the ArrayScan High Content Platform (Thermo Scientific Cellomics). Forty-eight hours postinfection, the viability was determined using resazurin sodium salt (Sigma-Aldrich). (A, D) Graphs show % GFP counts (left axis) normalized to untreated, infected conditions for VSV-spike (green squares, N = 5) and wtVSV (blue triangles, N = 2). The right axis shows % viability normalized to untreated, uninfected conditions for atovaquone alone (black circles, N = 3), atovaquone-treated, VSV-spike-infected cells (green squares, N = 5), or atovaquone-treated, wtVSV-infected cells (blue triangles, N = 2). Symbols boxed in red demonstrate a significant difference over untreated cells ( p < 0.05 and p < 0.005 for all atovaquone-treated, VSV-spike-infected GFP counts using a t -test). Representative fluorescent images are shown for each condition (C, F), and IC 50 values are indicated for VSV-spike and wt-VSV (B,E). Vehicle = medium containing the atovaquone-diluting agent, DMSO. Media = culture medium only.
Techniques Used: Infection, Stable Transfection, Transduction, Expressing
Figure Legend Snippet: Atovaquone partially requires TMPRSS2 to drive its antiviral action against SARS-CoV-2 and reduces the interaction between the spike protein and its surface receptor ACE2. (A) Schematic of atovaquone administration. (B) VeroE6 hTMPRSS2 cells were treated with atovaquone (10 μM) for 2 h before infection (full time), at the time of infection (entry), or 1 h after infection (postentry), before challenging with original SARS-CoV-2 at an MOI of 0.1. Infection was carried out for 48 h in the presence of the drug and for all conditions. Infection was assessed by immunoblotting of the spike protein within cell lysates. (C) Structure of constructs for a split NanoLuc-based bioreporter. RBD or S1 from either SARS-CoV1 or SARS-CoV2 was linked to Large BiT (LgBiT) on its N-terminus to form LgBiT-RBD or LgBiT-S1; similarly, the Small BiT (SmBiT) peptide was linked to human ACE2 to form SmBiT-ACE2. ACE2 and RBD or S1 constructs were transfected separately or cotransfected into HEK293 cells for 48 h and lysed with a passive lysis buffer. Mixed lysates or lysates from cotransfected cells were incubated with coelenterazine, and the luminescence measured using a plate reader. (D) Following plasmid transfection into HEK293 cells, the cells were lysed in a NanoLuc-compatible passive lysis buffer and lysates were dispensed into a 96-well plate, to which atovaquone was added at a final concentration of 4 μM. The impact of atovaquone on SARS receptor binding was assessed in two ways: (1) with atovaquone added to LgBiT-RBD or LgBiT-S1 for 50 min followed by the addition of an equal quantity of SmBiT-ACE2 for another 10 min (“mixed lysates)” or (2) with atovaquone added to the preformed SmBiT-ACE2 + LgBiT-RBD/S1 complex for 1 h (“cotransfected).” Following incubation, a nanoluciferase substrate was added and the luminescence was measured. HEK293 cells were also transfected with a nanoluciferase control plasmid and lysates were incubated with 4 μM atovaquone. N = 4 per condition. The graph shows % bioreporter luminescence with the highest value in each of the respective untreated conditions taken as 100% ( N = 4 per condition, the p values were determined using a t -test). (E, F). The different cell lines mentioned were subjected to immunoblotting (E) and flow cytometry analysis (F) of TMPRSS2 and ACE2 expression. For ACE2, unstained samples of the matched cell line were used as a control. For TMPRSS2, secondary antibody-stained samples of the matched cell line were used as a control. Controls for the A549 hACE2 cell line are represented in the figure. The same controls were used for all cell lines studied. (G) Vero hTMPRSS2, Calu-3, and A549 hACE2 cells were pretreated with atovaquone (100 μM) for 2 h before infection with the original SARS-CoV-2 (MOI of 0.1). Viral RNA levels were determined 48 h postinfection by qPCR. The data represent the means ± SEM of one experiment performed in biological triplicates. (H) HEK293T cells expressing hACE2 cells were mock-transfected or transfected with a plasmid encoding hTMPRSS2. Twenty-four hours post-transfection, cells were seeded in 96-well plates and preincubated with the different drugs E64d (10 μM), camostat (25 μM), and atovaquone (100 μM) + 5 μg/mL polybrene for 1 h before infection with purified SARS-CoV-2 pseudotypes. LacZ + cells were quantified using the Beta-Glo assay system and luminescence measurement. The data are the means ± SEM of two experiments performed in biological triplicates. Similar results were obtained by X-gal staining. (I) Effector cells (zipV2+) expressing SARS-CoV-2 spike and target cells (zipV1+) expressing ACE2 with or without TMPRSS2 were cocultured for 3 h in the presence of the indicated concentration of drugs or DMSO. Cell–cell fusion was assessed by measuring the fluorescence of the Venus protein complementation (zipV1 + zipV2). Data were normalized to the fusion obtained with target cells expressing ACE2 but not TMPRSS2 (ACE2 + TMPRSS2) and are the means ± SEM of two experiments performed in triplicates. The p values were calculated using a t -test where * p < 0.05, ** p < 0.01, *** p < 0.001.
Techniques Used: Infection, Western Blot, Construct, Transfection, Lysis, Incubation, Plasmid Preparation, Concentration Assay, Binding Assay, Control, Flow Cytometry, Expressing, Staining, Purification, Glo Assay, Fluorescence
Related Articles
Recombinant:Article Title: Structural insights into frog skin-derived cyclic peptides as selective matriptase inhibitors. Article Snippet: Matriptase is a type II transmembrane serine protease implicated in epithelial integrity and cancer progression, making it a promising therapeutic target.. However, the development of highly selective matriptase inhibitors remains a major challenge due to its structural homologies and similar proteolytic specificities with related proteases such as TMPRSS6.. In this study, we investigated a series of cyclic peptides derived from the frog-skin Bowman–Birk inhibitor HV-BBI, focusing on their inhibitory activity and selectivity toward matriptase. Article Title: Simulations and active learning enable efficient identification of an experimentally-validated broad coronavirus inhibitor. Article Snippet: Data normalization was performed using GraphPad Prism (GraphPad Software, San Diego, CA). .. Article Title: Simulations and active learning enable efficient identification of an experimentally-validated broad coronavirus inhibitor Article Snippet: Data normalization was performed using GraphPad Prism (GraphPad Software, San Diego, CA). .. Recombinant Human TMPRSS2 protein expressed from Purification:Article Title: Structural insights into frog skin-derived cyclic peptides as selective matriptase inhibitors. Article Snippet: Matriptase is a type II transmembrane serine protease implicated in epithelial integrity and cancer progression, making it a promising therapeutic target.. However, the development of highly selective matriptase inhibitors remains a major challenge due to its structural homologies and similar proteolytic specificities with related proteases such as TMPRSS6.. In this study, we investigated a series of cyclic peptides derived from the frog-skin Bowman–Birk inhibitor HV-BBI, focusing on their inhibitory activity and selectivity toward matriptase. Concentration Assay:Article Title: Structural Basis of Serine Protease Inhibition by Antibodies from Biased Fab Phage-Display Libraries Article Snippet: Point mutants to alanine and other residues were made from the wildtype plasmid using QuikChange ® Site-Directed Mutagenesis Kit (NEB) and oligos purchased from Azenta. .. These mutants were expressed as described previously and their inhibitory potency was measured against 30 nM commercial |
![FIGURE 3 SF-EVs and recombinant TMPRSS2 both display specific trypsin-like enzyme activity. (A) Michaelis–Menten plot of initial reaction velocities (V0) for kinetic parameter estimation of the generic Boc-QAR-AMC fluorogenic substrate cleaved by SF-EVs (± 3.3 × 1010 vesicles/mL), after curve fitting in GraphPad (Supporting Information Equation 1). Michaelis constant (Km: 278 ± 52 µM) is indicated by dotted line. (B) Plot of the fractional enzyme activity in SF-EVs (3.3 × 1010 vesicles/mL) versus [Nafamostat mesylate] by measuring the initial reaction velocities at 37◦C in the presence of 100 µM Boc-QAR-AMC fluorogenic substrate and curve fitting for absolute IC50 determination in GraphPad (Supporting Information Equation 2). IC50 (31 ± 5 pM) is indicated by dotted line. (C) Michaelis–Menten plot of initial reaction velocities for kinetic parameter estimation of the generic Boc-QAR- AMC fluorogenic substrate cleaved by recombinant TMPRSS2 (50 pM), after curve fitting in GraphPad (Supporting Information Equation 1). Michaelis constant (Km: 133 ± 16 µM) is indicated by dotted line. (D) Plot of the fractional enzyme activity of recombinant TMPRSS2 (50 pM) versus [Nafamostat mesylate] by measuring the initial reaction velocities at 37◦C in the presence of 100 µM Boc-QAR-AMC fluorogenic substrate and curve fit for absolute IC50 in GraphPad (Supporting Information Equation 2). IC50 (68 ± 3 pM) is indicated by dotted line. All data are shown as mean ± s.d. and were all performed in biological triplicate (n = 3). Graphs were created with GraphPad Prism v9.1.1.](https://pub-med-unpaywalled-images-cdn.bioz.com/pub_med_ids_ending_with_1430/pm40091430/pm40091430__page9_image1.jpg)
