tmprss2 (Proteintech)
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Proteintech
tmprss2
Tmprss2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tmprss2+expression+construct/TMPRSS2+Antibody/pmc09352574-350-17-19
Average 93 stars, based on 55 article reviews
Tmprss2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tmprss2+expression+construct/TMPRSS2+Antibody/pmc09352574-350-17-19
Average 93 stars, based on 55 article reviews
tmprss2 - by Bioz Stars,
2026-11
93/100 stars
Images
1) Product Images from "SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway"
Article Title: SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
Journal: Nature Microbiology
doi: 10.1038/s41564-022-01143-7
Figure Legend Snippet: a , Virus-induced fusion of co-cultured cells expressing split GFP (GFP-10 and GFP-11, respectively) reconstitutes fluorescence (image generated in BioRender, agreement SX23HJ6GY8SX23HJ6GY8). b , Co-cultured GFP-10 and GFP-11 A549-ACE2-TMPRSS2 cells were infected with B.1, Delta and Omicron/BA.1, photomicrographs taken at 22 h post infection: GFP, green; nucleocapsid (N), red; DAPI nuclei, blue; scale bars, 100 µm. c , Fluorescence over 20 h ( n = 4 technical repeats, 3 independent experiments, 2 virus stocks). d , Calu-3 cell infection with B.1, Delta and Omicron/BA.1. Supernatants were assessed by RT-qPCR ( n = 3 technical repeats, 2 independent experiments). e , SARS-CoV-2 entry routes: route 1 – fusion at the cell surface following processing by TMPRSS2; route 2 – fusion occurs post endocytosis after processing by cathepsins. Routes 1 and 2 are inhibited by Camostat and E64d, respectively. f , SARS-CoV-2 pseudotype infection of cell lines, mean luciferase values (1 experiment, n = 8 technical repeats, representative of 3 independent experiments). Route 1 predominates in Calu-3, route 2 in HEK, and both routes are supported by A549-ACE2-TMPRSS2. Control is Pangolin CoV (route 2 only), negative control is no glycoprotein pseudotypes (No). g , Relative pseudotype infection (compared to untreated) of 10 μM protease inhibitor-treated cells; mean of 4 biological repeats, **** P < 0.0001, one-way ANOVA, Dunnett’s multiple comparisons test. h , Camostat (left) and E64d (right) titration against Delta, Omicron/BA.1 and Pangolin CoV in A549-ACE2-TMPRSS2; mean relative infection compared to untreated control ( n = 2 biological repeats). i , Immunoblot of spike-expressing HEK lysates with anti-spike (S2) and anti-actin. j , HEK infection by Omicron/BA.2 pseudotype; mean luciferase values (1 experiment, n = 8 technical repeats, representative of 3 independent experiments). k , hNEC infection with Delta and Omicron/BA.1 clinical isolates, supernatants assessed by RT-qPCR; mean of 2 independent biological repeats. l , Immunoblots of uninfected (left) and infected (right) hNEC and Calu-3 lysates. Immunoblots probed for ACE2, TMPRSS2, Cathepsin-L, GAPDH, Spike S1 and N. m , Cell–cell fusion (as in a ) in Omicron/BA.1-transfected cells treated with trypsin. Plot displays mean fluorescence (1 experiment, 3 technical repeats, representative of 2 independent experiments). n , Cell–cell fusion in Delta or Omicron/BA.1-transfected cells, ±0.3 µg ml −1 trypsin. Data are relative to fusion by Omicron/BA.1 spike (−trypsin, 8 h), mean of 2 biological repeats. All error bars represent s.e.m.
Techniques Used: Virus, Cell Culture, Expressing, Fluorescence, Generated, Infection, Quantitative RT-PCR, Luciferase, Control, Negative Control, Protease Inhibitor, Titration, Western Blot, Transfection
Figure Legend Snippet: GFP-10 and GFP-11 A549 ACE2 TMPRSS2 cells were co-cultured and infected with Delta and Omicron BA.1 clinical isolates or with live reverse-genetics virus in which the Delta or Omicron BA.1 spike is presented in the context of the ancestral wildtype B lineage genome. Fusion was quantified by measuring GFP signal, as in Fig. .
Techniques Used: Cell Culture, Infection, Virus
Figure Legend Snippet: SARS-CoV-2 infection of A549 ACE2 TMPRSS2 cells in the presence of 10 µM Camostat or E64d, data is expressed relative to untreated control, values represent mean across two independent experiments, asterisks indicate statistical significance (Two tailed T-test) between E64d treated Delta and Omicron infections. Error bars indicate standard error of the mean.
Techniques Used: Infection, Control, Two Tailed Test
Figure Legend Snippet: a , Top: schematic representation of domain swap constructs between WT (lineage B) and Omicron spike. Bottom: linear representation illustrates the junction points between the chimeric proteins. b , Domain swap pseudotype infection of HEK cells. Data represent mean luciferase values from a representative experiment ( n = 8 technical repeats, data are representative of 3 independent experiments). c , Sensitivity of domain swap pseudotypes to camostat and E64d in A549-ACE2-TMPRSS2 cells. Data are expressed relative to the untreated control for each virus. Values represent the mean of 3 biological repeats. d , Immunoblot analyses of lysates from HEK cells producing domain swap pseudotypes. Blots were probed for spike (S1 and processed S2), actin loading control and HIV Gag p55 transfection control. The actin control relates to the S1 blot, while the p55 control relates to the processed S2 blot. e , Quantification of spike proteolytic processing in WT (lineage B), Omicron BA.1 and the reciprocal RBD swaps. Data are expressed relative to the total for a given spike and represent the mean of 5 independent blots. f , Cell fusion assay using cells transfected with WT (lineage B) (left), Omicron BA.1 (right) and the reciprocal RBD swap spikes. Plot displays mean GFP fluorescence signal from 1 representative experiment. g , Cell–cell fusion (as in f ). Data are expressed relative to fusion by WT (lineage B) spike (at 16 h) and are the mean of 4 independent experiments. One-way ANOVA, * P < 0.01, **** P < 0.0001. In all plots, error bars represent s.e.m.
Techniques Used: Construct, Infection, Luciferase, Control, Virus, Western Blot, Transfection, Cell Fusion Assay, Fluorescence
Figure Legend Snippet: a , Vero ACE2 TMPRSS2 (VAT) and BHK-hACE2 cells were inoculated with diluted clinical samples. Viral progeny was quantified in the medium 5 dpi by RT-qPCR. b , Aliquots of the medium from samples named 204 and 205 were used to generate a P1 in BHK-hACE2 and Calu-3 cells and, limited to sample 205, a P2 in Calu-3 and Caco2 cells. Viral stocks were quantified by RT-qPCR.
Techniques Used: Quantitative RT-PCR
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![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)
