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Addgene inc flipgfp tevp sensor

( A ) Schematic representation of the proposed proteolytic activation mechanism. ( B ) Workflow for constructing and evaluating protease-activatable aquaporins. ( C ) Diffusivities of CHO cells expressing hAqp1 fused with <t>TEVP-cleavable</t> DD(s). ( D ) Representative Western blot of membrane extracts from CHO cells engineered to express hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Membrane lysates from cells treated with shield-1 are included as a positive control. ( E ) Representative confocal images of CHO cells expressing hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Scale bars, 10 μm. ( F ) Diffusivities of CHO cells expressing hAqp1 tagged at the C terminus with FKBP12-DD with Gly-Ser spacers flanking the TEVP cleavage site (cs). ( G ) Diffusivities of CHO cells expressing hAqp1 with multiple TEVP cleavage sites inserted before FKBP12-DD. The optimized DD-MAPPER circuit (three cut sites) exhibits the largest fold change. ( H ) Modularity of DD-MAPPER facilitates adaptation for multiple proteases. ( I ) Representative diffusion maps of CHO cells expressing DD-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( J ) Diffusivities of CHO cells expressing HCVP- and TVMVP-activatable DD-MAPPER circuits. ( K ) Polycistronic constructs for implementing DD-MAPPER in different cell lines. ( L ) Representative diffusion maps of various cell types expressing DD-MAPPER. ( M ) Diffusivities of various cell types expressing DD-MAPPER. ( N ) Schematic illustrating the putative degradation pathways of DD-MAPPER and their inhibition by small-molecule modulators. ( O ) Representative Western blot of lysates prepared from cells expressing DD-MAPPER in the presence of chloroquine or MG132. Error bars represent SD from n ≥ 3 measurements. *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). Panels (B) and (N) created (in part) using BioRender. A. Mukherjee (2025); https://BioRender.com/xgnoc5l . IRES, internal ribosomal entry site.

Flipgfp Tevp Sensor, supplied by Addgene inc, used in various techniques. Bioz Stars score: 94/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/flipgfp tevp sensor/product/Addgene inc
Average 94 stars, based on 18 article reviews

flipgfp tevp sensor - by Bioz Stars, 2026-06

94/100 stars

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1) Product Images from "A programmable genetic platform for engineering noninvasive biosensors"

Article Title: A programmable genetic platform for engineering noninvasive biosensors

Journal: Science Advances

doi: 10.1126/sciadv.aec1211

Figure Legend Snippet: ( A ) Schematic representation of the proposed proteolytic activation mechanism. ( B ) Workflow for constructing and evaluating protease-activatable aquaporins. ( C ) Diffusivities of CHO cells expressing hAqp1 fused with TEVP-cleavable DD(s). ( D ) Representative Western blot of membrane extracts from CHO cells engineered to express hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Membrane lysates from cells treated with shield-1 are included as a positive control. ( E ) Representative confocal images of CHO cells expressing hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Scale bars, 10 μm. ( F ) Diffusivities of CHO cells expressing hAqp1 tagged at the C terminus with FKBP12-DD with Gly-Ser spacers flanking the TEVP cleavage site (cs). ( G ) Diffusivities of CHO cells expressing hAqp1 with multiple TEVP cleavage sites inserted before FKBP12-DD. The optimized DD-MAPPER circuit (three cut sites) exhibits the largest fold change. ( H ) Modularity of DD-MAPPER facilitates adaptation for multiple proteases. ( I ) Representative diffusion maps of CHO cells expressing DD-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( J ) Diffusivities of CHO cells expressing HCVP- and TVMVP-activatable DD-MAPPER circuits. ( K ) Polycistronic constructs for implementing DD-MAPPER in different cell lines. ( L ) Representative diffusion maps of various cell types expressing DD-MAPPER. ( M ) Diffusivities of various cell types expressing DD-MAPPER. ( N ) Schematic illustrating the putative degradation pathways of DD-MAPPER and their inhibition by small-molecule modulators. ( O ) Representative Western blot of lysates prepared from cells expressing DD-MAPPER in the presence of chloroquine or MG132. Error bars represent SD from n ≥ 3 measurements. *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). Panels (B) and (N) created (in part) using BioRender. A. Mukherjee (2025); https://BioRender.com/xgnoc5l . IRES, internal ribosomal entry site.

Techniques Used: Activation Assay, Expressing, Western Blot, Membrane, Positive Control, Diffusion-based Assay, Construct, Inhibition

( A ) Schematic representation illustrating the integration of DD-MAPPER with destabilized proteases for the detection of trimethoprim (TMP). ( B ) Quantification of diffusivities in CHO cells engineered to express the TMP-sensing DD-MAPPER circuit as depicted in (A), acquired in the presence and absence of TMP treatment for 24 hours. ( C ) Dose-response analysis of the TMP-sensing DD-MAPPER expressed in CHO cells incubated with varying concentrations of TMP for 24 hours. ( D ) Schematic depiction of the application of DD-MAPPER for the detection of small-molecule protease inhibitors. ( E ) Diffusivities of CHO cells engineered to express HCVP-modulated DD-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. ( F ) Dose-response analysis of the HCVP-based DD-MAPPER in CHO cells exposed to varying concentrations of boceprevir for 24 hours. ( G ) Schematic illustrating the detection of a protease-based two-input biological AND gate using DD-MAPPER. The corresponding genetic constructs for introducing the two-input AND gates and DD-MAPPER are shown alongside. ( H ) Diffusivities of CHO cells engineered to express the protease-based AND gate and corresponding DD-MAPPER detector. ( I ) Integration of DD-MAPPER with split protease technology to image protein-protein interactions. The corresponding genetic constructs are shown alongside. ( J ) Diffusivities of CHO cells expressing the split TEVP-based DD-MAPPER for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused coiled-coil peptides. ( K ) Schematic illustrating the engineering of split TEVP-based DD-MAPPER for calcium imaging and the corresponding genetic constructs. ( L ) Diffusivities of CHO cells expressing the calcium-sensing DD-MAPPER circuit. Control measurements are obtained in wild-type cells lacking the sensor. Error bars represent SD from n ≥ 3 measurements. ** P < 0.01; *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). HA, hemagglutinin; WT, wild type; EBFP, enhanced blue fluorescent protein.

Figure Legend Snippet: ( A ) Schematic representation illustrating the integration of DD-MAPPER with destabilized proteases for the detection of trimethoprim (TMP). ( B ) Quantification of diffusivities in CHO cells engineered to express the TMP-sensing DD-MAPPER circuit as depicted in (A), acquired in the presence and absence of TMP treatment for 24 hours. ( C ) Dose-response analysis of the TMP-sensing DD-MAPPER expressed in CHO cells incubated with varying concentrations of TMP for 24 hours. ( D ) Schematic depiction of the application of DD-MAPPER for the detection of small-molecule protease inhibitors. ( E ) Diffusivities of CHO cells engineered to express HCVP-modulated DD-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. ( F ) Dose-response analysis of the HCVP-based DD-MAPPER in CHO cells exposed to varying concentrations of boceprevir for 24 hours. ( G ) Schematic illustrating the detection of a protease-based two-input biological AND gate using DD-MAPPER. The corresponding genetic constructs for introducing the two-input AND gates and DD-MAPPER are shown alongside. ( H ) Diffusivities of CHO cells engineered to express the protease-based AND gate and corresponding DD-MAPPER detector. ( I ) Integration of DD-MAPPER with split protease technology to image protein-protein interactions. The corresponding genetic constructs are shown alongside. ( J ) Diffusivities of CHO cells expressing the split TEVP-based DD-MAPPER for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused coiled-coil peptides. ( K ) Schematic illustrating the engineering of split TEVP-based DD-MAPPER for calcium imaging and the corresponding genetic constructs. ( L ) Diffusivities of CHO cells expressing the calcium-sensing DD-MAPPER circuit. Control measurements are obtained in wild-type cells lacking the sensor. Error bars represent SD from n ≥ 3 measurements. ** P < 0.01; *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). HA, hemagglutinin; WT, wild type; EBFP, enhanced blue fluorescent protein.

Techniques Used: Incubation, Construct, Protein-Protein interactions, Expressing, Control, Imaging

( A ) Schematic representation of the proposed proteolytic activation mechanism. Genetic constructs encoding ER-MAPPER are depicted alongside. ( B ) Representative confocal images of CHO cells transduced with ER-MAPPER. ( C ) Representative diffusion maps of various cell types expressing ER-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( D ) Diffusivities of various cell types expressing ER-MAPPER. ( E ) Representative diffusion maps CHO cell pellets expressing ER-MAPPER with and without induction of the corresponding protease. ( F ) Diffusivities of CHO cells expressing ER-MAPPER with and without induction of the corresponding protease. ( G ) Diffusivities of CHO cells engineered to express HCVP-modulated ER-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. CCs, coiled-coils. ( H ) Diffusivities of CHO cells expressing the split TEVP-based ER-MAPPER sensor for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused p3/p4 coiled-coils. ( I ) Schematic illustrating the adaptation of split TEVP-based ER-MAPPER to detect rapamycin-induced dimerization of FKBP and Frb. ( J ) Diffusivities of CHO cells expressing split TEVP-based sensor depicted in ( J ). Control measurements are obtained in cells expressing split TEVP without the fused FKBP and Frb domains. ( K ) Time-dependent activation of ER-MAPPER in CHO cells engineered to express FKBP and Frb-fused split TEVP fragments upon rapamycin induction. Control measurements are obtained in cells expressing split TEVP without the fused FKBP or Frb. Error bars represent SD from n ≥ 3 measurements. Statistical significance is denoted by ** P < 0.01; *** P < 0.001; n.s., P ≥ 0.05 (two-sided t test). CID, chemically induced dimerization.

Figure Legend Snippet: ( A ) Schematic representation of the proposed proteolytic activation mechanism. Genetic constructs encoding ER-MAPPER are depicted alongside. ( B ) Representative confocal images of CHO cells transduced with ER-MAPPER. ( C ) Representative diffusion maps of various cell types expressing ER-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( D ) Diffusivities of various cell types expressing ER-MAPPER. ( E ) Representative diffusion maps CHO cell pellets expressing ER-MAPPER with and without induction of the corresponding protease. ( F ) Diffusivities of CHO cells expressing ER-MAPPER with and without induction of the corresponding protease. ( G ) Diffusivities of CHO cells engineered to express HCVP-modulated ER-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. CCs, coiled-coils. ( H ) Diffusivities of CHO cells expressing the split TEVP-based ER-MAPPER sensor for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused p3/p4 coiled-coils. ( I ) Schematic illustrating the adaptation of split TEVP-based ER-MAPPER to detect rapamycin-induced dimerization of FKBP and Frb. ( J ) Diffusivities of CHO cells expressing split TEVP-based sensor depicted in ( J ). Control measurements are obtained in cells expressing split TEVP without the fused FKBP and Frb domains. ( K ) Time-dependent activation of ER-MAPPER in CHO cells engineered to express FKBP and Frb-fused split TEVP fragments upon rapamycin induction. Control measurements are obtained in cells expressing split TEVP without the fused FKBP or Frb. Error bars represent SD from n ≥ 3 measurements. Statistical significance is denoted by ** P < 0.01; *** P < 0.001; n.s., P ≥ 0.05 (two-sided t test). CID, chemically induced dimerization.

Techniques Used: Activation Assay, Construct, Transduction, Diffusion-based Assay, Expressing, Control

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Journal: Science Advances

Article Title: A programmable genetic platform for engineering noninvasive biosensors

doi: 10.1126/sciadv.aec1211

Figure Lengend Snippet: ( A ) Schematic representation of the proposed proteolytic activation mechanism. ( B ) Workflow for constructing and evaluating protease-activatable aquaporins. ( C ) Diffusivities of CHO cells expressing hAqp1 fused with TEVP-cleavable DD(s). ( D ) Representative Western blot of membrane extracts from CHO cells engineered to express hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Membrane lysates from cells treated with shield-1 are included as a positive control. ( E ) Representative confocal images of CHO cells expressing hAqp1 fused at its C terminus to the TEVP-cleavable FKBP12-DD. Scale bars, 10 μm. ( F ) Diffusivities of CHO cells expressing hAqp1 tagged at the C terminus with FKBP12-DD with Gly-Ser spacers flanking the TEVP cleavage site (cs). ( G ) Diffusivities of CHO cells expressing hAqp1 with multiple TEVP cleavage sites inserted before FKBP12-DD. The optimized DD-MAPPER circuit (three cut sites) exhibits the largest fold change. ( H ) Modularity of DD-MAPPER facilitates adaptation for multiple proteases. ( I ) Representative diffusion maps of CHO cells expressing DD-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( J ) Diffusivities of CHO cells expressing HCVP- and TVMVP-activatable DD-MAPPER circuits. ( K ) Polycistronic constructs for implementing DD-MAPPER in different cell lines. ( L ) Representative diffusion maps of various cell types expressing DD-MAPPER. ( M ) Diffusivities of various cell types expressing DD-MAPPER. ( N ) Schematic illustrating the putative degradation pathways of DD-MAPPER and their inhibition by small-molecule modulators. ( O ) Representative Western blot of lysates prepared from cells expressing DD-MAPPER in the presence of chloroquine or MG132. Error bars represent SD from n ≥ 3 measurements. *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). Panels (B) and (N) created (in part) using BioRender. A. Mukherjee (2025); https://BioRender.com/xgnoc5l . IRES, internal ribosomal entry site.

Article Snippet: Plasmid containing the FlipGFP TEVP sensor was obtained from Addgene (#124429).

Techniques: Activation Assay, Expressing, Western Blot, Membrane, Positive Control, Diffusion-based Assay, Construct, Inhibition

Journal: Science Advances

Article Title: A programmable genetic platform for engineering noninvasive biosensors

doi: 10.1126/sciadv.aec1211

Figure Lengend Snippet: ( A ) Schematic representation illustrating the integration of DD-MAPPER with destabilized proteases for the detection of trimethoprim (TMP). ( B ) Quantification of diffusivities in CHO cells engineered to express the TMP-sensing DD-MAPPER circuit as depicted in (A), acquired in the presence and absence of TMP treatment for 24 hours. ( C ) Dose-response analysis of the TMP-sensing DD-MAPPER expressed in CHO cells incubated with varying concentrations of TMP for 24 hours. ( D ) Schematic depiction of the application of DD-MAPPER for the detection of small-molecule protease inhibitors. ( E ) Diffusivities of CHO cells engineered to express HCVP-modulated DD-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. ( F ) Dose-response analysis of the HCVP-based DD-MAPPER in CHO cells exposed to varying concentrations of boceprevir for 24 hours. ( G ) Schematic illustrating the detection of a protease-based two-input biological AND gate using DD-MAPPER. The corresponding genetic constructs for introducing the two-input AND gates and DD-MAPPER are shown alongside. ( H ) Diffusivities of CHO cells engineered to express the protease-based AND gate and corresponding DD-MAPPER detector. ( I ) Integration of DD-MAPPER with split protease technology to image protein-protein interactions. The corresponding genetic constructs are shown alongside. ( J ) Diffusivities of CHO cells expressing the split TEVP-based DD-MAPPER for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused coiled-coil peptides. ( K ) Schematic illustrating the engineering of split TEVP-based DD-MAPPER for calcium imaging and the corresponding genetic constructs. ( L ) Diffusivities of CHO cells expressing the calcium-sensing DD-MAPPER circuit. Control measurements are obtained in wild-type cells lacking the sensor. Error bars represent SD from n ≥ 3 measurements. ** P < 0.01; *** P < 0.001; and n.s., P ≥ 0.05 (two-sided t test). HA, hemagglutinin; WT, wild type; EBFP, enhanced blue fluorescent protein.

Article Snippet: Plasmid containing the FlipGFP TEVP sensor was obtained from Addgene (#124429).

Techniques: Incubation, Construct, Protein-Protein interactions, Expressing, Control, Imaging

Journal: Science Advances

Article Title: A programmable genetic platform for engineering noninvasive biosensors

doi: 10.1126/sciadv.aec1211

Figure Lengend Snippet: ( A ) Schematic representation of the proposed proteolytic activation mechanism. Genetic constructs encoding ER-MAPPER are depicted alongside. ( B ) Representative confocal images of CHO cells transduced with ER-MAPPER. ( C ) Representative diffusion maps of various cell types expressing ER-MAPPER. The minimum and maximum diffusivity values (μm 2 /ms) are specified at the edges of the color bars. ( D ) Diffusivities of various cell types expressing ER-MAPPER. ( E ) Representative diffusion maps CHO cell pellets expressing ER-MAPPER with and without induction of the corresponding protease. ( F ) Diffusivities of CHO cells expressing ER-MAPPER with and without induction of the corresponding protease. ( G ) Diffusivities of CHO cells engineered to express HCVP-modulated ER-MAPPER, with and without treatment using antiviral HCVP inhibitors: boceprevir (BV) or telaprevir (TV) for 24 hours. CCs, coiled-coils. ( H ) Diffusivities of CHO cells expressing the split TEVP-based ER-MAPPER sensor for detecting protein-protein interaction. Control measurements are obtained in cells expressing split TEVP fragments without the fused p3/p4 coiled-coils. ( I ) Schematic illustrating the adaptation of split TEVP-based ER-MAPPER to detect rapamycin-induced dimerization of FKBP and Frb. ( J ) Diffusivities of CHO cells expressing split TEVP-based sensor depicted in ( J ). Control measurements are obtained in cells expressing split TEVP without the fused FKBP and Frb domains. ( K ) Time-dependent activation of ER-MAPPER in CHO cells engineered to express FKBP and Frb-fused split TEVP fragments upon rapamycin induction. Control measurements are obtained in cells expressing split TEVP without the fused FKBP or Frb. Error bars represent SD from n ≥ 3 measurements. Statistical significance is denoted by ** P < 0.01; *** P < 0.001; n.s., P ≥ 0.05 (two-sided t test). CID, chemically induced dimerization.

Article Snippet: Plasmid containing the FlipGFP TEVP sensor was obtained from Addgene (#124429).

Techniques: Activation Assay, Construct, Transduction, Diffusion-based Assay, Expressing, Control

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