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Sino Biological flag ripk1
Flag Ripk1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/flag+ripk1/pm37865804-83-2-9?v=Sino+Biological
Average 91 stars, based on 3 article reviews

flag ripk1 - by Bioz Stars, 2026-08

91/100 stars

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( A ) Domain structures of human RIP kinases. RHIM = RIP homotypic interaction motif, DD = death domain, CARD = caspase activation and recruitment domain, ANK = ankyrin repeats. ( B ) Positive selection analysis of RIPK1–5 in the indicated mammalian order. Input sequences and PAML p-values can be found in . Images of model species were generated using BioRender.com . ( C ) Heat map showing the percentage of species within a clade that have the indicated protein. The clades and the number of species within each clade are indicated on the left. Complete lists of proteins and species in each group can be found in . Lancelet species were not queried for all proteins and are not included in this graph.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: ( A ) Domain structures of human RIP kinases. RHIM = RIP homotypic interaction motif, DD = death domain, CARD = caspase activation and recruitment domain, ANK = ankyrin repeats. ( B ) Positive selection analysis of RIPK1–5 in the indicated mammalian order. Input sequences and PAML p-values can be found in . Images of model species were generated using BioRender.com . ( C ) Heat map showing the percentage of species within a clade that have the indicated protein. The clades and the number of species within each clade are indicated on the left. Complete lists of proteins and species in each group can be found in . Lancelet species were not queried for all proteins and are not included in this graph.

Article Snippet: Coding sequences for human RIPK1 (Addgene #78834), human RIPK2 (ORFeome ID #4886), human RIPK3 (Addgene #78804), mouse RIPK1 (Addgene #115341), and mouse RIPK3 (Addgene #78805) were cloned into apcDNA5/FRT/TO backbone (Invitrogen, Carlsbad, CA, USA) with an N-terminal V5 tag and linker using Gibson Assembly (New England Biolabs, Ipswich, MA, USA).

Techniques: Activation Assay, Selection, Generated

Human V5-RIPK1–5 proteins were transfected into WT ( A–C ) or RIPK1 KO ( C ) HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( A ) Human RIPK1–5 activation of NF-κB in WT 293T cells. ( B ) Activation of NF-κB by catalytically active versus kinase-mutant RIPK1–5 in WT HEK293T cells. ( C ) Activation of NF-κB by RIPK1–5 in WT versus RIPK1 KO HEK293T cells. Data are representative of 3 independent experiments with n=3–6 biological replicates per group. Data were analyzed using one-way ANOVA with Dunnett’s multiple comparisons test ( A ) or two-way ANOVA with Šidák’s multiple comparisons test ( B, C ). ns = not significant, ***=p<0.001, ****=p<0.0001. Figure 1—figure supplement 1—source data 1. Raw data for the bar graphs in depicting NF-κB activation by various human RIPK proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: Human V5-RIPK1–5 proteins were transfected into WT ( A–C ) or RIPK1 KO ( C ) HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( A ) Human RIPK1–5 activation of NF-κB in WT 293T cells. ( B ) Activation of NF-κB by catalytically active versus kinase-mutant RIPK1–5 in WT HEK293T cells. ( C ) Activation of NF-κB by RIPK1–5 in WT versus RIPK1 KO HEK293T cells. Data are representative of 3 independent experiments with n=3–6 biological replicates per group. Data were analyzed using one-way ANOVA with Dunnett’s multiple comparisons test ( A ) or two-way ANOVA with Šidák’s multiple comparisons test ( B, C ). ns = not significant, ***=p<0.001, ****=p<0.0001. Figure 1—figure supplement 1—source data 1. Raw data for the bar graphs in depicting NF-κB activation by various human RIPK proteins.

Techniques: Transfection, Luciferase, Control, Activity Assay, Activation Assay, Mutagenesis

WT ( A ) and RIPK1 KO ( B ) HEK293T cells were transfected with WT or kinase mutant V5-RIPK1–5. Protein expression was analyzed at 18 hr post-transfection by western blot using the indicated antibodies. Figure 1—figure supplement 3—source data 1. Original western blots for . Figure 1—figure supplement 3—source data 2. PDF file containing original western blots for , indicating the relevant bands and treatments.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: WT ( A ) and RIPK1 KO ( B ) HEK293T cells were transfected with WT or kinase mutant V5-RIPK1–5. Protein expression was analyzed at 18 hr post-transfection by western blot using the indicated antibodies. Figure 1—figure supplement 3—source data 1. Original western blots for . Figure 1—figure supplement 3—source data 2. PDF file containing original western blots for , indicating the relevant bands and treatments.

Techniques: Transfection, Mutagenesis, Expressing, Western Blot

( A ) Percent similarity of RIPK3 from the indicated species compared to humans. ( B ) RIPK3 proteins were transfected into WT or RIPK1 KO HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( C ) RIPK3 proteins were transfected into HEK293T cells with and without human ZBP1 and MLKL. At 18 hr post-transfection, cells were stained using the ReadyProbe Cell Viability kit, and fluorescence was measured using a plate reader. Species shown are mouse ( M. musculus ), cat ( F. catus ), pig ( S. scrofa ), lizard ( A. carolinensis ), turtle ( C. mydas ), and lamprey ( P. marinus ). Data are representative of 3–5 independent experiments with n=3–6 replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test. ns = not significant, ****=p<0.0001. Figure 2—source data 1. Raw data for the bar graphs in depicting NF-κB (B) and cell death (C) activation by various vertebrate RIPK3 proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: ( A ) Percent similarity of RIPK3 from the indicated species compared to humans. ( B ) RIPK3 proteins were transfected into WT or RIPK1 KO HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( C ) RIPK3 proteins were transfected into HEK293T cells with and without human ZBP1 and MLKL. At 18 hr post-transfection, cells were stained using the ReadyProbe Cell Viability kit, and fluorescence was measured using a plate reader. Species shown are mouse ( M. musculus ), cat ( F. catus ), pig ( S. scrofa ), lizard ( A. carolinensis ), turtle ( C. mydas ), and lamprey ( P. marinus ). Data are representative of 3–5 independent experiments with n=3–6 replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test. ns = not significant, ****=p<0.0001. Figure 2—source data 1. Raw data for the bar graphs in depicting NF-κB (B) and cell death (C) activation by various vertebrate RIPK3 proteins.

Techniques: Transfection, Luciferase, Control, Activity Assay, Staining, Fluorescence, Activation Assay

WT or RIPK1 KO HEK293T cells were transfected with the indicated protein. Protein expression was analyzed at 18 hr post-transfection by western blot using the indicated antibodies. Figure 2—figure supplement 1—source data 1. Original western blots for . Figure 2—figure supplement 1—source data 2. PDF files containing original western blots for , indicating the relevant bands and treatments.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: WT or RIPK1 KO HEK293T cells were transfected with the indicated protein. Protein expression was analyzed at 18 hr post-transfection by western blot using the indicated antibodies. Figure 2—figure supplement 1—source data 1. Original western blots for . Figure 2—figure supplement 1—source data 2. PDF files containing original western blots for , indicating the relevant bands and treatments.

Techniques: Transfection, Expressing, Western Blot

WT and RIPK1 KO cells were transfected with the indicated plasmids, and cell death was analyzed by ReadyProbes assay at 18 hr post-transfection. RM = RHIM mutant, KM = kinase mutant. Data indicative of 1–2 independent experiments with n=3 biological replicates per group. Data were analyzed by two-way ANOVA with Šidák’s multiple comparisons test. ****=p<0.0001. Figure 2—figure supplement 2—source data 1. Raw data for the bar graph in depicting cell death activation by human MLKL, ZBP1, and/or RIPK3.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: WT and RIPK1 KO cells were transfected with the indicated plasmids, and cell death was analyzed by ReadyProbes assay at 18 hr post-transfection. RM = RHIM mutant, KM = kinase mutant. Data indicative of 1–2 independent experiments with n=3 biological replicates per group. Data were analyzed by two-way ANOVA with Šidák’s multiple comparisons test. ****=p<0.0001. Figure 2—figure supplement 2—source data 1. Raw data for the bar graph in depicting cell death activation by human MLKL, ZBP1, and/or RIPK3.

Techniques: Transfection, Mutagenesis, Activation Assay

The indicated RIPK3 proteins were transfected into WT or RIPK1 KO HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. Data are representative of 2 independent experiments with n=4–6 biological replicates per group. Data were analyzed using two-way ANOVA with Tukey’s multiple comparison test. ns = not significant, *p<0.05, ***p <0.001, ****p<0.0001. Figure 3—figure supplement 1—source data 1. Raw data for the bar graphs in depicting cell death activation by wild-type, kinase mutant, and RIPK3 proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: The indicated RIPK3 proteins were transfected into WT or RIPK1 KO HEK293T cells, along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. Data are representative of 2 independent experiments with n=4–6 biological replicates per group. Data were analyzed using two-way ANOVA with Tukey’s multiple comparison test. ns = not significant, *p<0.05, ***p <0.001, ****p<0.0001. Figure 3—figure supplement 1—source data 1. Raw data for the bar graphs in depicting cell death activation by wild-type, kinase mutant, and RIPK3 proteins.

Techniques: Transfection, Luciferase, Control, Activity Assay, Comparison, Activation Assay, Mutagenesis

( A ) Alignment of RIPK1 RHIM across diverse vertebrates. Residue numbers refer to the human sequence. Lancelet species is Branchiostoma floridae . ( B ) Diverse vertebrate RIPK1 CT proteins were transfected into HEK293T cells along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( C ) Alignment of ZBP1 RHIMs across diverse vertebrates. Residue numbers refer to the human sequence. ( D ) Activation of NF-κB by WT and RHIM mutant ZBP1 proteins. ( E ) NF-κB activation by human RIPK3 with the indicated RHIM tetrad variant. ( F ) Human RIPK3 proteins with the indicated RHIM tetrad variants were transfected into HEK293T cells with MLKL (gray circles) or MLKL and ZBP1 (orange squares), and viability was measured at 18 hr post-transfection. Data are representative of 2–5 independent experiments with n=3–6 replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test ( A, D ), one-way ANOVA with Tukey’s multiple comparisons test ( E ), or two-way ANOVA with Tukey’s multiple comparisons test ( F ). ns = not significant, ****=p<0.0001. Figure 4—source data 1. Raw data for the bar graphs in depicting NF-κB (B, D, E) and cell death (F) activation by various RHIM-containing proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: ( A ) Alignment of RIPK1 RHIM across diverse vertebrates. Residue numbers refer to the human sequence. Lancelet species is Branchiostoma floridae . ( B ) Diverse vertebrate RIPK1 CT proteins were transfected into HEK293T cells along with NF-κB firefly luciferase and control renilla luciferase reporter plasmids (see Materials and methods), and NF-κB activity was measured at 18 hr post-transfection. ( C ) Alignment of ZBP1 RHIMs across diverse vertebrates. Residue numbers refer to the human sequence. ( D ) Activation of NF-κB by WT and RHIM mutant ZBP1 proteins. ( E ) NF-κB activation by human RIPK3 with the indicated RHIM tetrad variant. ( F ) Human RIPK3 proteins with the indicated RHIM tetrad variants were transfected into HEK293T cells with MLKL (gray circles) or MLKL and ZBP1 (orange squares), and viability was measured at 18 hr post-transfection. Data are representative of 2–5 independent experiments with n=3–6 replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test ( A, D ), one-way ANOVA with Tukey’s multiple comparisons test ( E ), or two-way ANOVA with Tukey’s multiple comparisons test ( F ). ns = not significant, ****=p<0.0001. Figure 4—source data 1. Raw data for the bar graphs in depicting NF-κB (B, D, E) and cell death (F) activation by various RHIM-containing proteins.

Techniques: Residue, Sequencing, Transfection, Luciferase, Control, Activity Assay, Activation Assay, Mutagenesis, Variant Assay

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: WT or RIPK1 KO HEK293T cells were transfected with the indicated protein. Protein expression was analyzed at 18 hr post-transfection by western blot using the indicated antibodies. Figure 4—figure supplement 1—source data 1. Original western blots for . Figure 4—figure supplement 1—source data 2. PDF files containing original western blots for , indicating the relevant bands and treatments.

Techniques: Transfection, Expressing, Western Blot

( A ) Schematic of RIPK1 CT compared to full-length RIPK1. ( B ) WT and RHIM mutant RIPK1 full length and RIPK1 CT were transfected into HEK293T cells along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data were analyzed using one-way ANOVA with Tukey’s multiple comparison test. ns = not significant. Figure 4—figure supplement 2—source data 1. Raw data for the bar graphs in depicting NF-κB activation by human RIPK1 proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: ( A ) Schematic of RIPK1 CT compared to full-length RIPK1. ( B ) WT and RHIM mutant RIPK1 full length and RIPK1 CT were transfected into HEK293T cells along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data were analyzed using one-way ANOVA with Tukey’s multiple comparison test. ns = not significant. Figure 4—figure supplement 2—source data 1. Raw data for the bar graphs in depicting NF-κB activation by human RIPK1 proteins.

Techniques: Mutagenesis, Transfection, Activation Assay, Comparison

WT and RIPK1 KO HEK293T cells were transfected with the indicated RIPK1 CT along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data are representative of 3 independent experiments with 3–6 biological replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test. ns = not significant, *=p<0.05, **=p<0.01. Figure 4—figure supplement 3—source data 1. Raw data for the bar graphs in depicting NF-κB activation by various vertebrate RIPK1 CT proteins in wild-type and RIPK1 KO HEK293T cells.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: WT and RIPK1 KO HEK293T cells were transfected with the indicated RIPK1 CT along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data are representative of 3 independent experiments with 3–6 biological replicates per group. Data were analyzed using two-way ANOVA with Šidák’s multiple comparisons test. ns = not significant, *=p<0.05, **=p<0.01. Figure 4—figure supplement 3—source data 1. Raw data for the bar graphs in depicting NF-κB activation by various vertebrate RIPK1 CT proteins in wild-type and RIPK1 KO HEK293T cells.

Techniques: Transfection, Activation Assay

( A ) TRIF sequences from vertebrate species highlighting the RHIM core tetrad. Residue numbers refer to the human sequence. Vertebrate species shown include mouse ( M. musculus ), pig ( S. scrofa ), cat ( F. catus ), lizard ( A. carolinensis ), frog ( Xenopus laevis ), fish ( Danio rerio ), and lamprey ( P. marinus ). ( B–C ) WT ( B–C ) and RIPK1 KO ( C ) HEK293T cells were transfected with the indicated plasmids along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data are representative of 3 independent experiments with 3 biological replicates per group. Data were analyzed using a t-test ( B ) or a two-way ANOVA with Šidák’s multiple comparisons test ( C ). ns = not significant, *=p<0.05. Figure 4—figure supplement 4—source data 1. Raw data for the bar graphs in depicting NF-κB activation by human TRIF proteins.

Journal: eLife

Article Title: Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates

doi: 10.7554/eLife.102301

Figure Lengend Snippet: ( A ) TRIF sequences from vertebrate species highlighting the RHIM core tetrad. Residue numbers refer to the human sequence. Vertebrate species shown include mouse ( M. musculus ), pig ( S. scrofa ), cat ( F. catus ), lizard ( A. carolinensis ), frog ( Xenopus laevis ), fish ( Danio rerio ), and lamprey ( P. marinus ). ( B–C ) WT ( B–C ) and RIPK1 KO ( C ) HEK293T cells were transfected with the indicated plasmids along with Dual-Glo plasmids (see Materials and methods). NF-κB activation was analyzed at 18 hr post-transfection. Data are representative of 3 independent experiments with 3 biological replicates per group. Data were analyzed using a t-test ( B ) or a two-way ANOVA with Šidák’s multiple comparisons test ( C ). ns = not significant, *=p<0.05. Figure 4—figure supplement 4—source data 1. Raw data for the bar graphs in depicting NF-κB activation by human TRIF proteins.

Techniques: Residue, Sequencing, Transfection, Activation Assay

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