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human il33  (R&D Systems)


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    Structured Review

    R&D Systems human il33
    Human Il33, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+il+33/Human+IL-33+Antibody/us12594324-380-11-14
    Average 93 stars, based on 88 article reviews
    human il33 - by Bioz Stars, 2026-11
    93/100 stars

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    Related Articles

    Incubation:

    Article Title: Interleukin 33 supports squamous cell carcinoma growth via a dual effect on tumour proliferation, migration and invasion, and T cell activation.
    Article Snippet: .. After 24 h, the cells were fasted in 0.1% bovine serum albumin (BSA) for 4 h. Then, the cells were incubated with fresh complete medium in the presence of recombinant human IL-33 (rhIL-33, R&D Systems) at 0, 10, 50, and 100 ng/mL. .. The proliferation rate based on cell confluence was determined by live cell imaging (10× objective lens) using the IncuCyte ZOOM integrated software (Sartorius, Ann Arbor, MI, USA).

    Article Title: IL-1 receptor accessory protein-inhibiting antibodies and antigen-binding fragments thereof
    Article Snippet: Human IL-33 Induced IFN-γ Release in Human PBMCs: The cells were suspended in Medium RPMI 1640 (Life Technologies cat #M-106-500) with FCS 10%, P/S 1% (both Life Technologies) and recombinant human IL-12 to a final concentration of 0.6 nM (R&D Systems, Cat #219-IL-025) and seeded in 384-well plates (50000 cells/well) in a volume of 30 μl on the assay day. .. 10 μl of the test antibodies were added to the cells and incubated for 30 min. 10 uL of IL-33 was added to the cells in a final concentration of 0.05 nM (human IL-33, R&D Systems cat #3625-IL-010). ..

    Article Title: Interleukin 33 supports squamous cell carcinoma growth via a dual effect on tumour proliferation, migration and invasion, and T cell activation
    Article Snippet: .. After 24 h, the cells were fasted in 0.1% bovine serum albumin (BSA) for 4 h. Then, the cells were incubated with fresh complete medium in the presence of recombinant human IL-33 (rhIL-33, R&D Systems) at 0, 10, 50, and 100 ng/mL. .. The proliferation rate based on cell confluence was determined by live cell imaging (10× objective lens) using the IncuCyte ZOOM integrated software (Sartorius, Ann Arbor, MI, USA).

    Recombinant:

    Article Title: Interleukin 33 supports squamous cell carcinoma growth via a dual effect on tumour proliferation, migration and invasion, and T cell activation.
    Article Snippet: .. After 24 h, the cells were fasted in 0.1% bovine serum albumin (BSA) for 4 h. Then, the cells were incubated with fresh complete medium in the presence of recombinant human IL-33 (rhIL-33, R&D Systems) at 0, 10, 50, and 100 ng/mL. .. The proliferation rate based on cell confluence was determined by live cell imaging (10× objective lens) using the IncuCyte ZOOM integrated software (Sartorius, Ann Arbor, MI, USA).

    Article Title: Interleukin 33 supports squamous cell carcinoma growth via a dual effect on tumour proliferation, migration and invasion, and T cell activation
    Article Snippet: .. After 24 h, the cells were fasted in 0.1% bovine serum albumin (BSA) for 4 h. Then, the cells were incubated with fresh complete medium in the presence of recombinant human IL-33 (rhIL-33, R&D Systems) at 0, 10, 50, and 100 ng/mL. .. The proliferation rate based on cell confluence was determined by live cell imaging (10× objective lens) using the IncuCyte ZOOM integrated software (Sartorius, Ann Arbor, MI, USA).

    Article Title: Humanized anti-IL-1R3 antibodies
    Article Snippet: .. Cells were then stimulated with recombinant human IL-33 (20 ng/mL, RnD systems) for 24 hrs before harvesting supernatants and assaying for IL-8 production (Duoset ELISA, RnD Systems). ..

    Concentration Assay:

    Article Title: IL-1 receptor accessory protein-inhibiting antibodies and antigen-binding fragments thereof
    Article Snippet: Human IL-33 Induced IFN-γ Release in Human PBMCs: The cells were suspended in Medium RPMI 1640 (Life Technologies cat #M-106-500) with FCS 10%, P/S 1% (both Life Technologies) and recombinant human IL-12 to a final concentration of 0.6 nM (R&D Systems, Cat #219-IL-025) and seeded in 384-well plates (50000 cells/well) in a volume of 30 μl on the assay day. .. 10 μl of the test antibodies were added to the cells and incubated for 30 min. 10 uL of IL-33 was added to the cells in a final concentration of 0.05 nM (human IL-33, R&D Systems cat #3625-IL-010). ..

    Enzyme-linked Immunosorbent Assay:

    Article Title: Epidermal growth factor receptor controls sex differences in lung type 2 responses to inhaled allergen.
    Article Snippet: Hormonal disruptions are associated with poor asthma control in females, yet how these phenomena are linked remains unknown.. Here, we investigated distinct allergeninduced immune responses between the sexes during maturation.. By 6 weeks of life, female mice exposed to the aeroallergen house dust mite (HDM) from postnatal day 7 exhibited stronger type 2 (T2) immune responses and higher lung interleukin33 (IL33) than males.

    Article Title: A skin isolate of Micrococcus luteus negates the Staphylococcus aureus- induced release of type 2 cytokines from keratinocytes
    Article Snippet: .. To quantify IL-33 and TSLP in NHEK conditioned medium, human IL-33 (R&D systems) and human TSLP (R&D Systems) DuoSet ELISA Kits were used according to manufacturer’s instructions. .. 99.9% Acetone (Fisher Scientific) chilled to -20 ̊C was added to bacterial supernatant at a ratio of 4:1.

    Article Title: Humanized anti-IL-1R3 antibodies
    Article Snippet: .. Cells were then stimulated with recombinant human IL-33 (20 ng/mL, RnD systems) for 24 hrs before harvesting supernatants and assaying for IL-8 production (Duoset ELISA, RnD Systems). ..

    Binding Assay:

    Article Title: Anti-IL-33 antibodies and uses thereof
    Article Snippet: Binding competition between a panel of different anti-IL-33 monoclonal antibodies was determined using a real time, label-free bio-layer interferometry assay on an Octet® HTX biosensor (ForteBio, A Division of Pall Life Sciences). .. To assess whether two antibodies were able to compete with one another for binding to human IL-33, a pre-mix assay format was used where 100 nM of human IL-33 (R&D Systems; #3625-IL-010/CF) was pre-mixed with 500 nM of different anti-IL-33 monoclonal antibodies (subsequently referred to as mAb-2) for at least 2 hours prior to running the binding competition assay. .. Octet biosensors coated with either an anti-mouse Fc polyclonal antibody (Pall ForteBio Corp., #18-5088; subsequently referred as AMC) or with an anti-human Fc polyclonal antibody (Pall ForteBio Corp., #18-5060; subsequently referred as AHC) were first submerged into wells containing 20 μg/mL of individual anti-IL-33 monoclonal antibodies for 3 minutes to capture anti-IL-33 monoclonal antibodies expressed either a with mouse Fc or with a human Fc, respectively (subsequently referred to as mAb-1).

    Bioprocessing:

    Article Title: Anti-IL-33 antibodies and uses thereof
    Article Snippet: Binding competition between a panel of different anti-IL-33 monoclonal antibodies was determined using a real time, label-free bio-layer interferometry assay on an Octet® HTX biosensor (ForteBio, A Division of Pall Life Sciences). .. To assess whether two antibodies were able to compete with one another for binding to human IL-33, a pre-mix assay format was used where 100 nM of human IL-33 (R&D Systems; #3625-IL-010/CF) was pre-mixed with 500 nM of different anti-IL-33 monoclonal antibodies (subsequently referred to as mAb-2) for at least 2 hours prior to running the binding competition assay. .. Octet biosensors coated with either an anti-mouse Fc polyclonal antibody (Pall ForteBio Corp., #18-5088; subsequently referred as AMC) or with an anti-human Fc polyclonal antibody (Pall ForteBio Corp., #18-5060; subsequently referred as AHC) were first submerged into wells containing 20 μg/mL of individual anti-IL-33 monoclonal antibodies for 3 minutes to capture anti-IL-33 monoclonal antibodies expressed either a with mouse Fc or with a human Fc, respectively (subsequently referred to as mAb-1).

    Competitive Binding Assay:

    Article Title: Anti-IL-33 antibodies and uses thereof
    Article Snippet: Binding competition between a panel of different anti-IL-33 monoclonal antibodies was determined using a real time, label-free bio-layer interferometry assay on an Octet® HTX biosensor (ForteBio, A Division of Pall Life Sciences). .. To assess whether two antibodies were able to compete with one another for binding to human IL-33, a pre-mix assay format was used where 100 nM of human IL-33 (R&D Systems; #3625-IL-010/CF) was pre-mixed with 500 nM of different anti-IL-33 monoclonal antibodies (subsequently referred to as mAb-2) for at least 2 hours prior to running the binding competition assay. .. Octet biosensors coated with either an anti-mouse Fc polyclonal antibody (Pall ForteBio Corp., #18-5088; subsequently referred as AMC) or with an anti-human Fc polyclonal antibody (Pall ForteBio Corp., #18-5060; subsequently referred as AHC) were first submerged into wells containing 20 μg/mL of individual anti-IL-33 monoclonal antibodies for 3 minutes to capture anti-IL-33 monoclonal antibodies expressed either a with mouse Fc or with a human Fc, respectively (subsequently referred to as mAb-1).



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    Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 <t>(IL-33),</t> and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.
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    Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 <t>(IL-33),</t> and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.
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    R&D Systems recombinant murine il33
    Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 <t>(IL-33),</t> and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.
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    Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 <t>(IL-33),</t> and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.
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    Image Search Results


    Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 (IL-33), and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.

    Journal: Research

    Article Title: Integrated Single-Cell Profiling Reveals TL1A as a Biomarker and Driver of Type 2 Inflammation via Macrophage-Dependent Immunoregulation in Asthma

    doi: 10.34133/research.1190

    Figure Lengend Snippet: Mechanism underlying tumor necrosis factor-like ligand 1A (TL1A)–C-C motif chemokine ligand 8 (CCL8) axis activation in the context of allergic inflammation. (A and B) Expression levels of TL1A induced by different stimuli in human airway epithelial cells or macrophages. (C) TL1A expression in uninduced macrophages, macrophages induced by interleukin 33 (IL-33), and macrophages induced by IL-33 plus interleukin 2 (IL-2). (D and E) Comparison of the expression levels of CCL8 induced by different concentrations of TL1A, quantified using reverse transcription polymerase chain reaction (RT-PCR) or transcriptomic sequencing. The messenger RNA (mRNA) levels of CCL8 after the transfection of TL1A-M plasmids, quantified using RT-PCR (F) or transcriptomic sequencing (G). (H) Death receptor 3 (DR3) knockdown abolished the elevation of CCL8 induced by TL1A stimulation. (I) CCL8 level in CD14 + macrophages treated or not with TL1A. (J) RT-PCR analysis of CCL8 transcript following DR3 small interfering RNA (siRNA) treatment. Representative data from CD14 + cells from a single donor. (K) A schematic for the administration of different signaling pathway inhibitors to investigate the pathways involved in TL1A–CCL8 axis activation (BAY11-7082, a nuclear factor kappa B [NF-κB] inhibitor; LY294002, a phosphoinositide 3-kinase [PI3K inhibitor]; PD98059, an extracellular signal-regulated kinase [ERK] inhibitor; SB203580, a p38 inhibitor; and SP600125, a c-Jun N-terminal kinase [JNK] inhibitor). Data are presented as the mean ± SD of triplicate measurements from at least 3 independent cell culture experiments. For primary human macrophage experiments (I and J), cells were derived from n = 4 healthy donors. * P < 0.05 and ** P < 0.01 compared with the respective groups. All in vitro stimulation and inhibitor treatments were analyzed in a blinded manner.

    Article Snippet: The recombinant proteins, small-molecular compounds, or inhibitors were purchased as indicated: recombinant mouse IL-13, IL-33, and TSLP protein (MCE); recombinant human IL-2, IL-4, TNF-α, and IFN-γ protein (Abbkine); poly(I:C) (Selleck); lipopolysaccharide (Sigma-Aldrich); IL-1β (Thermo Fisher); and small-molecule inhibitors BAY11-7082, LY294002, PD98059, SB203580, and SP600125 (Selleck).

    Techniques: Activation Assay, Expressing, Comparison, Reverse Transcription, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Sequencing, Transfection, Knockdown, Small Interfering RNA, Cell Culture, Derivative Assay, In Vitro