Review

anti human ifnar1 (Bio X Cell)

Bio X Cell is a verified supplier

Bio X Cell manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Bio X Cell anti human ifnar1

( A to G ) PBMCs from the patients with irAE were cultured in the plate coated with anti-CD3 and anti-CD28 (10 μg/ml) in the presence of IgG1 isotype control or anti–human IL-6R (50 μg/ml), anti–human IL-12p40 (50 μg/ml), and anti–human <t>IFNAR1</t> (50 μg/ml) for 3 days; n = 9. (A) Expression of CD38 and CD127 on CD8 + T cells. Right: Percentage of CD38 + CD127 − CD8 + T cells. (B and C) CD8 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (B) Expression of granzyme B and IFN-γ. Right: Percentage of granzyme B + IFN-γ + CD8 + T cells. (C) Expression of perforin and IFN-γ. Right: Percentage of perforin + IFN-γ + CD8 + T cells. [(D) and (E)] MFIs of GluCy5 (D), TMRM, and MTDR (E) in CD8 + T cells were presented. [(F) and (G)] CD4 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (F) Expression of IL-21 and IL-2. Right: Percentage of IL-21 + IL-2 + CD4 + T cells. (G) Expression of CD38 and CXCR5 on CD4 + T cells. Right: Percentage of CD38 + CXCR5 − CD4 + T cells. Data in graphs represent mean ± SEM. Significance was tested paired Student’s t test [(A) to (G)].

Anti Human Ifnar1, supplied by Bio X Cell, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti human ifnar1/product/Bio X Cell
Average 94 stars, based on 12 article reviews

anti human ifnar1 - by Bioz Stars, 2026-05

94/100 stars

Images

1) Product Images from "Inflammatory arthritis irAE may represent a unique autoimmune disease primarily driven by T cells but likely not autoantibodies"

Article Title: Inflammatory arthritis irAE may represent a unique autoimmune disease primarily driven by T cells but likely not autoantibodies

Journal: Science Advances

doi: 10.1126/sciadv.aea4262

Figure Legend Snippet: ( A to G ) PBMCs from the patients with irAE were cultured in the plate coated with anti-CD3 and anti-CD28 (10 μg/ml) in the presence of IgG1 isotype control or anti–human IL-6R (50 μg/ml), anti–human IL-12p40 (50 μg/ml), and anti–human IFNAR1 (50 μg/ml) for 3 days; n = 9. (A) Expression of CD38 and CD127 on CD8 + T cells. Right: Percentage of CD38 + CD127 − CD8 + T cells. (B and C) CD8 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (B) Expression of granzyme B and IFN-γ. Right: Percentage of granzyme B + IFN-γ + CD8 + T cells. (C) Expression of perforin and IFN-γ. Right: Percentage of perforin + IFN-γ + CD8 + T cells. [(D) and (E)] MFIs of GluCy5 (D), TMRM, and MTDR (E) in CD8 + T cells were presented. [(F) and (G)] CD4 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (F) Expression of IL-21 and IL-2. Right: Percentage of IL-21 + IL-2 + CD4 + T cells. (G) Expression of CD38 and CXCR5 on CD4 + T cells. Right: Percentage of CD38 + CXCR5 − CD4 + T cells. Data in graphs represent mean ± SEM. Significance was tested paired Student’s t test [(A) to (G)].

Techniques Used: Cell Culture, Control, Expressing

Image Search Results

Journal: Science Advances

Article Title: Inflammatory arthritis irAE may represent a unique autoimmune disease primarily driven by T cells but likely not autoantibodies

doi: 10.1126/sciadv.aea4262

Figure Lengend Snippet: ( A to G ) PBMCs from the patients with irAE were cultured in the plate coated with anti-CD3 and anti-CD28 (10 μg/ml) in the presence of IgG1 isotype control or anti–human IL-6R (50 μg/ml), anti–human IL-12p40 (50 μg/ml), and anti–human IFNAR1 (50 μg/ml) for 3 days; n = 9. (A) Expression of CD38 and CD127 on CD8 + T cells. Right: Percentage of CD38 + CD127 − CD8 + T cells. (B and C) CD8 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (B) Expression of granzyme B and IFN-γ. Right: Percentage of granzyme B + IFN-γ + CD8 + T cells. (C) Expression of perforin and IFN-γ. Right: Percentage of perforin + IFN-γ + CD8 + T cells. [(D) and (E)] MFIs of GluCy5 (D), TMRM, and MTDR (E) in CD8 + T cells were presented. [(F) and (G)] CD4 + T cells activated for 5 days were restimulated with PMA, ionomycin, and monensin for 5 hours. (F) Expression of IL-21 and IL-2. Right: Percentage of IL-21 + IL-2 + CD4 + T cells. (G) Expression of CD38 and CXCR5 on CD4 + T cells. Right: Percentage of CD38 + CXCR5 − CD4 + T cells. Data in graphs represent mean ± SEM. Significance was tested paired Student’s t test [(A) to (G)].

Article Snippet: PBMCs from patients with irAE were thawed and rested in a complete medium for 1 hour and then activated with plate-coated anti–human CD3 and anti–human CD28 (10 μg/ml) with IgG1 isotype control (Bio X Cell, catalog no. CP174) or a combination of anti–human IL-6R 50 μg/ml; Bio X Cell, catalog no. SIM0014), anti–human IL-12p40 (50 μg/ml; Bio X Cell, catalog no. SIM0020), and anti–human IFNAR1 (50 μg/ml; Bio X Cell, catalog no. SIM0022) for 3 days.

Techniques: Cell Culture, Control, Expressing

PIM1 decreased IFNAR1 protein levels to promote OC43 replication. a) Luciferase assay of ISRE element activity after PIM1/K67M overexpression (n = 3). b) Immunoblots of lysates from HEK293T cells transfected with vector/PIM1 plasmids for 48 h. c) Western blot for IFNAR1 in HEK293T cells transfected with vector/WT‐PIM1/PIM1‐K67M plasmids for 48 h. d) IFNAR1 expression level in PIM1 knockdown cells. e) Immunoblots analysis of RD cells infected with OC43 at an MOI of 10 for the indicated time. f) Expression of IFNAR1 in RD cells transfected with siPIM1 RNA, followed by OC43 infection. g–j) Western blot for IFNAR1 expression in HEK293T or HepG2 cells treated with PIM1 inhibitors (CX‐6528, SGI‐1776, and AZD‐1208) at the indicated concentration for 48 h. k) The IFNAR1 expression in RD cells pre‐treated with PIM1 inhibitor 2 for 2 h, followed by OC43 infection for 48h. l)The intracellular OC43 genomic RNA in HEK293T cells transfected with vector/PIM1/PIM1 with IFNAR1 followed by the 24 h challenging of OC43 at an MOI of 0.1. Statistical analyses were conducted with Student's t‐test. * : p < 0.05, ** : p < 0.01. Data are depicted as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Journal: Advanced Science

Article Title: PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation

doi: 10.1002/advs.202503487

Figure Lengend Snippet: PIM1 decreased IFNAR1 protein levels to promote OC43 replication. a) Luciferase assay of ISRE element activity after PIM1/K67M overexpression (n = 3). b) Immunoblots of lysates from HEK293T cells transfected with vector/PIM1 plasmids for 48 h. c) Western blot for IFNAR1 in HEK293T cells transfected with vector/WT‐PIM1/PIM1‐K67M plasmids for 48 h. d) IFNAR1 expression level in PIM1 knockdown cells. e) Immunoblots analysis of RD cells infected with OC43 at an MOI of 10 for the indicated time. f) Expression of IFNAR1 in RD cells transfected with siPIM1 RNA, followed by OC43 infection. g–j) Western blot for IFNAR1 expression in HEK293T or HepG2 cells treated with PIM1 inhibitors (CX‐6528, SGI‐1776, and AZD‐1208) at the indicated concentration for 48 h. k) The IFNAR1 expression in RD cells pre‐treated with PIM1 inhibitor 2 for 2 h, followed by OC43 infection for 48h. l)The intracellular OC43 genomic RNA in HEK293T cells transfected with vector/PIM1/PIM1 with IFNAR1 followed by the 24 h challenging of OC43 at an MOI of 0.1. Statistical analyses were conducted with Student's t‐test. * : p < 0.05, ** : p < 0.01. Data are depicted as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Article Snippet: Cell surface expression of IFNAR1 was quantified by flow cytometry using a phycoerythrin (PE)‐conjugated anti‐human IFNAR1 antibody (R&D Systems, Catalog # FAB245P).

Techniques: Luciferase, Activity Assay, Over Expression, Western Blot, Transfection, Plasmid Preparation, Expressing, Knockdown, Infection, Concentration Assay, Control

$PIM1 promoted IFNAR1 degradation via ubiquitination. a) IFNAR1 mRNA level in HEK293T cells transfected with vector/PIM1 plasmids for 48 h. b) The mRNA level of IFNAR1 in RD cells transfected with scramble/PIM1‐specific siRNA for 48 h. c) The mRNA level of IFNAR1 in RD cells after challenging with/without OC43 at an MOI of 1 or 10. d) IFNAR1‐overexpressed HEK293T cells were transfected with scramble/PIM1‐specific siRNA, followed by 50 µ m of CHX treatment for the indicated periods. IFNAR1 protein level were determined by western blot. e) IFNAR1 expression level after PIM1/K67M overexpression followed by MG132 or NH 4 Cl treatment. f) Flow Cytometry of cell surface IFNAR1 after PIM1 overexpression, stained with IFNAR1‐PE (n = 3). g) IFNAR1 expression in cell membrane or cytosol fractions after PIM1/K67M overexpression. h) Immunoblots of IFNAR1 in HEK293T cells transfected with WT‐IFNAR1 or mutated IFNAR1 (S535A, S539A) with/without PIM1. i) Western blot analysis for ubiquitination and IFNAR1 in HEK293T cells co‐transfected with HA‐Ubiquitin, IFNAR1 and vector/PIM1/PIM1 K67M constructs. j) Immunoprecipitation of IFNAR1 and HA‐tagged ubiquitination from lysates of HEK293T cells co‐transfected with HA‐K48 ubi/HA‐K63 ubi, IFNAR1 and vector/PIM1 plasmids. Statistical analyses were conducted with Student's t‐test. * : p < 0.05, ** : p < 0.01. Data are depicted as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.$

Journal: Advanced Science

Article Title: PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation

doi: 10.1002/advs.202503487

Figure Lengend Snippet: PIM1 promoted IFNAR1 degradation via ubiquitination. a) IFNAR1 mRNA level in HEK293T cells transfected with vector/PIM1 plasmids for 48 h. b) The mRNA level of IFNAR1 in RD cells transfected with scramble/PIM1‐specific siRNA for 48 h. c) The mRNA level of IFNAR1 in RD cells after challenging with/without OC43 at an MOI of 1 or 10. d) IFNAR1‐overexpressed HEK293T cells were transfected with scramble/PIM1‐specific siRNA, followed by 50 µ m of CHX treatment for the indicated periods. IFNAR1 protein level were determined by western blot. e) IFNAR1 expression level after PIM1/K67M overexpression followed by MG132 or NH 4 Cl treatment. f) Flow Cytometry of cell surface IFNAR1 after PIM1 overexpression, stained with IFNAR1‐PE (n = 3). g) IFNAR1 expression in cell membrane or cytosol fractions after PIM1/K67M overexpression. h) Immunoblots of IFNAR1 in HEK293T cells transfected with WT‐IFNAR1 or mutated IFNAR1 (S535A, S539A) with/without PIM1. i) Western blot analysis for ubiquitination and IFNAR1 in HEK293T cells co‐transfected with HA‐Ubiquitin, IFNAR1 and vector/PIM1/PIM1 K67M constructs. j) Immunoprecipitation of IFNAR1 and HA‐tagged ubiquitination from lysates of HEK293T cells co‐transfected with HA‐K48 ubi/HA‐K63 ubi, IFNAR1 and vector/PIM1 plasmids. Statistical analyses were conducted with Student's t‐test. * : p < 0.05, ** : p < 0.01. Data are depicted as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Article Snippet: Cell surface expression of IFNAR1 was quantified by flow cytometry using a phycoerythrin (PE)‐conjugated anti‐human IFNAR1 antibody (R&D Systems, Catalog # FAB245P).

Techniques: Ubiquitin Proteomics, Transfection, Plasmid Preparation, Western Blot, Expressing, Over Expression, Flow Cytometry, Staining, Membrane, Construct, Immunoprecipitation, Control

PIM1 promoted IFNAR1 degradation via β‐TrCP1. a) IFNAR1 protein level in IFNAR1‐expressed HEK293T cells transfected with diverse siRNAs. b) IFNAR1 protein level in IFANR1‐expressed HEK293T cells transfected with scramble/β‐TrCP1 specific siRNA with/without PIM1 plasmids. c) IFNAR1 protein level in IFNAR1‐expressed HEK293T cells with β‐TrCP1 and/or PIM1 siRNA knockdown. d) Viral genomic RNA of OC43 in RD cells transfected with scramble/β‐TrCP1 specific siRNA followed by infection at an MOI of 0.1 for 24 h (n = 4). e) Viral genomic RNA level of OC43 in HEK293T cells transfected with increasing amounts of β‐TrCP1 followed by the challenging of HCoV‐OC43 at an MOI of 0.1 for 24 h (n = 3). f) Viral genomic RNA level in HEK293T cells after β‐TrCP1 siRNA knockdown with or without ectopic expression of PIM1, followed by OC43 infection at an MOI of 0.1 for 24 h (n = 3). g) Viral genomic RNA level in RD cells treated with PIM1 inhibitor (CX6528=8 µ m ) with or without β‐TrCP1 inhibitor (GS143) at indicated concentration for 2 h, followed by OC43 infection at MOI of 0.01 for 72 h (n = 4). Statistical analyses were conducted with Student's t‐test. * : p <0.05, ** : p < 0.01. Data are shown as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Journal: Advanced Science

Article Title: PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation

doi: 10.1002/advs.202503487

Figure Lengend Snippet: PIM1 promoted IFNAR1 degradation via β‐TrCP1. a) IFNAR1 protein level in IFNAR1‐expressed HEK293T cells transfected with diverse siRNAs. b) IFNAR1 protein level in IFANR1‐expressed HEK293T cells transfected with scramble/β‐TrCP1 specific siRNA with/without PIM1 plasmids. c) IFNAR1 protein level in IFNAR1‐expressed HEK293T cells with β‐TrCP1 and/or PIM1 siRNA knockdown. d) Viral genomic RNA of OC43 in RD cells transfected with scramble/β‐TrCP1 specific siRNA followed by infection at an MOI of 0.1 for 24 h (n = 4). e) Viral genomic RNA level of OC43 in HEK293T cells transfected with increasing amounts of β‐TrCP1 followed by the challenging of HCoV‐OC43 at an MOI of 0.1 for 24 h (n = 3). f) Viral genomic RNA level in HEK293T cells after β‐TrCP1 siRNA knockdown with or without ectopic expression of PIM1, followed by OC43 infection at an MOI of 0.1 for 24 h (n = 3). g) Viral genomic RNA level in RD cells treated with PIM1 inhibitor (CX6528=8 µ m ) with or without β‐TrCP1 inhibitor (GS143) at indicated concentration for 2 h, followed by OC43 infection at MOI of 0.01 for 72 h (n = 4). Statistical analyses were conducted with Student's t‐test. * : p <0.05, ** : p < 0.01. Data are shown as mean ±SD. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Article Snippet: Cell surface expression of IFNAR1 was quantified by flow cytometry using a phycoerythrin (PE)‐conjugated anti‐human IFNAR1 antibody (R&D Systems, Catalog # FAB245P).

Techniques: Transfection, Knockdown, Infection, Expressing, Concentration Assay, Control

PIM1 promoted IFNAR1 and β‐TrCP1 interaction. a,b) Protein level of β‐TrCP1 in HEK293T cells transfected with vector/PIM1 construct or scramble/PIM1 specific siRNA. c) Immunoprecipitation of IFNAR1 and HA‐tagged β‐TrCP1 from lysates mixture of vector/PIM1/PIM1 mutant expressed HEK293T and IFNAR1 expressed HEK293T. d) IP blots for purified PIM1 post incubation with or without purified βTrCP1 in the IP buffer. e) Immunofluorescent assay of HEK293T cells co‐transfected with PIM1 and HA‐ β‐TrCP1 plasmids under 40× microscope. PIM1 was in Red and HA‐ β‐TrCP1 was in Green. Scale bar = 10 µ m . Line intensity profiles (indicated as white line) and Scatter plots (boxed ROI ) for PIM1 and β‐TrCP1 were analyzed by Image J software. Pearson's r = 0.62. f) Purified β‐TrCP1 incubated with/without recombinant PIM1 in a kinase assay buffer at 37 °C for 30 min. Lambda protein phosphatase (lambda PP) was added to one tube of the PIM1 and β‐TrCP1 mixture for another 30 min. The products were visualized post Phos‐tag PAGE separation, which separates the phosphorylated β‐TrCP1 as up‐shifted migration bands from the non‐phosphorylated ones. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Journal: Advanced Science

Article Title: PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation

doi: 10.1002/advs.202503487

Figure Lengend Snippet: PIM1 promoted IFNAR1 and β‐TrCP1 interaction. a,b) Protein level of β‐TrCP1 in HEK293T cells transfected with vector/PIM1 construct or scramble/PIM1 specific siRNA. c) Immunoprecipitation of IFNAR1 and HA‐tagged β‐TrCP1 from lysates mixture of vector/PIM1/PIM1 mutant expressed HEK293T and IFNAR1 expressed HEK293T. d) IP blots for purified PIM1 post incubation with or without purified βTrCP1 in the IP buffer. e) Immunofluorescent assay of HEK293T cells co‐transfected with PIM1 and HA‐ β‐TrCP1 plasmids under 40× microscope. PIM1 was in Red and HA‐ β‐TrCP1 was in Green. Scale bar = 10 µ m . Line intensity profiles (indicated as white line) and Scatter plots (boxed ROI ) for PIM1 and β‐TrCP1 were analyzed by Image J software. Pearson's r = 0.62. f) Purified β‐TrCP1 incubated with/without recombinant PIM1 in a kinase assay buffer at 37 °C for 30 min. Lambda protein phosphatase (lambda PP) was added to one tube of the PIM1 and β‐TrCP1 mixture for another 30 min. The products were visualized post Phos‐tag PAGE separation, which separates the phosphorylated β‐TrCP1 as up‐shifted migration bands from the non‐phosphorylated ones. The densities of all proteins of interest were quantified using ImageJ and normalized to the respective control indicated beneath the bands.

Article Snippet: Cell surface expression of IFNAR1 was quantified by flow cytometry using a phycoerythrin (PE)‐conjugated anti‐human IFNAR1 antibody (R&D Systems, Catalog # FAB245P).

Techniques: Transfection, Plasmid Preparation, Construct, Immunoprecipitation, Mutagenesis, Purification, Incubation, Microscopy, Software, Recombinant, Kinase Assay, Migration, Control

Phosphorylated β‐TrCP1 at S82 by PIM1 enhanced its interaction with IFNAR1. a) Predicted PIM1‐phosphorylation sites on β‐TrCP1. b) ISRE luciferase assays using HEK293T cells transfected with ISRE‐Luci and β‐TrCP1 / β‐TrCP1 mutants, followed by stimulation with 500U IFNα for 16 h (n = 3). c) Protein level of IFNAR1 in HEK293T cells ectopically expressed with WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A. d) Protein level of phosphorylated STAT1/2 (p‐STAT1/2) in HEK293T cells ectopically expressed with vector/WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A followed by the stimulation of IFNα for 16 h. e) Quantification of intracellular viral genomic RNA in HEK293T cells ectopically expressed with WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A followed by the infection with HCoV‐OC43 at an MOI of 1 for 36 h (n = 3). f) Western blot analysis of HEK293T cells transfected with WT/S82A/S521A β‐TrCP1 plasmids with/without PIM1. Blots of IP assay using p‐Ser/Thr antibody were shown in the bottom panel. g) Co‐IP assay of IFNAR1 from the cell lysate mixture of HEK293T cells transfected with IFNAR1/HA‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A separately.

Journal: Advanced Science

Article Title: PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation

doi: 10.1002/advs.202503487

Figure Lengend Snippet: Phosphorylated β‐TrCP1 at S82 by PIM1 enhanced its interaction with IFNAR1. a) Predicted PIM1‐phosphorylation sites on β‐TrCP1. b) ISRE luciferase assays using HEK293T cells transfected with ISRE‐Luci and β‐TrCP1 / β‐TrCP1 mutants, followed by stimulation with 500U IFNα for 16 h (n = 3). c) Protein level of IFNAR1 in HEK293T cells ectopically expressed with WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A. d) Protein level of phosphorylated STAT1/2 (p‐STAT1/2) in HEK293T cells ectopically expressed with vector/WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A followed by the stimulation of IFNα for 16 h. e) Quantification of intracellular viral genomic RNA in HEK293T cells ectopically expressed with WT‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A followed by the infection with HCoV‐OC43 at an MOI of 1 for 36 h (n = 3). f) Western blot analysis of HEK293T cells transfected with WT/S82A/S521A β‐TrCP1 plasmids with/without PIM1. Blots of IP assay using p‐Ser/Thr antibody were shown in the bottom panel. g) Co‐IP assay of IFNAR1 from the cell lysate mixture of HEK293T cells transfected with IFNAR1/HA‐ β‐TrCP1 / β‐TrCP1 S82A/ β‐TrCP1 S521A separately.

Article Snippet: Cell surface expression of IFNAR1 was quantified by flow cytometry using a phycoerythrin (PE)‐conjugated anti‐human IFNAR1 antibody (R&D Systems, Catalog # FAB245P).

Techniques: Phospho-proteomics, Luciferase, Transfection, Plasmid Preparation, Infection, Western Blot, Co-Immunoprecipitation Assay

A Schematic overview of the experimental design for generating conditioned media (CM) from HPCs treated ± 1 ng/ml TNF-⍺, ± 10 µg/ml anifrolumab (IFNAR antagonist), and ± 0.16 nM JAK inhibitor I for 24 hrs. B We probed if interfering with JAK and IFNAR signalling could abrogate the chemotaxis of T cells towards TNF-⍺-CM from HPCs. C and D Quantification of the chemotactic response (chemotaxis index) of C CD4+ T cells and D CD8+ T cells in response to the CM generated as outlined in A . Data is represented as mean ± SEM of three healthy donors. Statistical analysis: one-way ANOVA followed by Bonferroni’s multiple comparisons test.

Journal: bioRxiv

Article Title: TNF-α-induced type I IFN signalling decreases neurogenesis and drives T cell chemotaxis

doi: 10.1101/2025.06.18.660440

Figure Lengend Snippet: A Schematic overview of the experimental design for generating conditioned media (CM) from HPCs treated ± 1 ng/ml TNF-⍺, ± 10 µg/ml anifrolumab (IFNAR antagonist), and ± 0.16 nM JAK inhibitor I for 24 hrs. B We probed if interfering with JAK and IFNAR signalling could abrogate the chemotaxis of T cells towards TNF-⍺-CM from HPCs. C and D Quantification of the chemotactic response (chemotaxis index) of C CD4+ T cells and D CD8+ T cells in response to the CM generated as outlined in A . Data is represented as mean ± SEM of three healthy donors. Statistical analysis: one-way ANOVA followed by Bonferroni’s multiple comparisons test.

Article Snippet: To probe the dependency of IFNAR in TNF-⍺-induced type I IFN signalling, we utilised a non-therapeutic biosimilar antibody with the identical variable regions from the therapeutic antibody anifrolumab (SIM0022, Bio X Cell).

Techniques: Chemotaxis Assay, Generated

A Representative images showing the expression of MAP2 (green) and DCX (orange) ion seven days differentiated HPCs treated chronically ± 1 TNF-⍺ ± 10 µg/ml anifrolumab. Scale bar represents 100 µm. B and C Quantification of the percentage of B MAP2+ cells and C DCX+ cells respectively based on A . Data represent mean ± SEM from five independent experiments. Statistical analysis: B Kruskal-Wallis test followed by Dunn’s post hoc correction and C one-way ANOVA followed by Bonferroni’s multiple comparisons test.

Journal: bioRxiv

Article Title: TNF-α-induced type I IFN signalling decreases neurogenesis and drives T cell chemotaxis

doi: 10.1101/2025.06.18.660440

Figure Lengend Snippet: A Representative images showing the expression of MAP2 (green) and DCX (orange) ion seven days differentiated HPCs treated chronically ± 1 TNF-⍺ ± 10 µg/ml anifrolumab. Scale bar represents 100 µm. B and C Quantification of the percentage of B MAP2+ cells and C DCX+ cells respectively based on A . Data represent mean ± SEM from five independent experiments. Statistical analysis: B Kruskal-Wallis test followed by Dunn’s post hoc correction and C one-way ANOVA followed by Bonferroni’s multiple comparisons test.

Techniques: Expressing

Review

Structured Review

Images

1) Product Images from "Inflammatory arthritis irAE may represent a unique autoimmune disease primarily driven by T cells but likely not autoantibodies"

Similar Products

Image Search Results