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Addgene inc tspan11
( A ) Schematic of biolayer interferometry (BLI) setup for <t>Tspan12-Norrin</t> binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of <t>Tspan11.</t> Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .
Tspan11, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "The co-receptor Tetraspanin12 directly captures Norrin to promote ligand-specific β-catenin signaling"

Article Title: The co-receptor Tetraspanin12 directly captures Norrin to promote ligand-specific β-catenin signaling

Journal: eLife

doi: 10.7554/eLife.96743

( A ) Schematic of biolayer interferometry (BLI) setup for Tspan12-Norrin binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of Tspan11. Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .
Figure Legend Snippet: ( A ) Schematic of biolayer interferometry (BLI) setup for Tspan12-Norrin binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of Tspan11. Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .

Techniques Used: Binding Assay, Concentration Assay



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( A ) Schematic of biolayer interferometry (BLI) setup for <t>Tspan12-Norrin</t> binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of <t>Tspan11.</t> Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .
Tspan11, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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( A ) Schematic of biolayer interferometry (BLI) setup for <t>Tspan12-Norrin</t> binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of <t>Tspan11.</t> Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .
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Image Search Results


( A ) Schematic of biolayer interferometry (BLI) setup for Tspan12-Norrin binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of Tspan11. Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .

Journal: eLife

Article Title: The co-receptor Tetraspanin12 directly captures Norrin to promote ligand-specific β-catenin signaling

doi: 10.7554/eLife.96743

Figure Lengend Snippet: ( A ) Schematic of biolayer interferometry (BLI) setup for Tspan12-Norrin binding: Tspan12 lacking the C-terminal tail (∆C), inserted into biotinylated nanodiscs, is immobilized on a streptavidin-coated biosensor, and Norrin association and dissociation are monitored in real time. ( B ) BLI traces of Norrin at indicated concentrations binding to and dissociating from Tspan12. ( C ) Steady-state binding curve fit to Norrin-Tspan12 binding (mean ± SD from three independent replicates at each concentration of Norrin) gives a K D of 10.4±1.2 nM (mean ± SEM). ( D ) Observed association rate constant (K obs ), determined from fitting BLI association traces (mean ± SD in three independent experiments), is linearly dependent on Norrin concentration with a slope K on = 0.00019 ± 0.00003 nM –1 s –1 (mean ± SEM). When combined with the K off = 0.0014 ± 0.00016 s –1 (mean ± SEM) determined from fitting the dissociation traces, we obtain a kinetic K D of 7.4±1.4 nM (mean ± SEM). ( E ) BLI traces of the soluble MBP-tagged Tspan12 LEL domain, at the indicated concentrations, associating to and dissociating from a biosensor loaded with MBP-tagged Norrin. Kinetic fitting gives an apparent affinity of 16±3 nM (mean ± SEM). ( F ) BLI traces of 10, 32, or 100 nM Norrin show no binding to a biosensor loaded with a nanodisc-embedded chimeric Tspan12 with the LEL replaced by that of Tspan11. Figure 1—source data 1. Steady-state interference shift and K obs values used to generate .

Article Snippet: Human Tspan12 (DNASU) truncated after the fourth transmembrane domain (∆C, residues 1–252) and Tspan12 with the LEL replaced by that of TSPAN11 (Tspan12-LEL11, Addgene plasmid #115785 from Harald Junge; ) were C-terminally tagged with the Rho-1D4 antibody recognition sequence TETSQVAPA.

Techniques: Binding Assay, Concentration Assay

Expression box diagram of gene expression in pan-cancer. a – f The gene expression of HOXD9, CPRC5B, ITLN1, CXCL13, TSPAN11 and TIMP1 in different tumors, respectively

Journal: Cancer Cell International

Article Title: Identification and development of a novel invasion-related gene signature for prognosis prediction in colon adenocarcinoma

doi: 10.1186/s12935-021-01795-1

Figure Lengend Snippet: Expression box diagram of gene expression in pan-cancer. a – f The gene expression of HOXD9, CPRC5B, ITLN1, CXCL13, TSPAN11 and TIMP1 in different tumors, respectively

Article Snippet: We used primary antibodies raised against GAPDH, CXCL13, ITLN1, HOXD9, and GPRC5B (Santa-Cruz Biotechnology, CA, USA), as well as TIMP1 and TSPAN11 (Proteintech, China).

Techniques: Expressing, Gene Expression