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recombinant tnfα standards  (R&D Systems)


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    R&D Systems recombinant tnfα standards
    Recombinant Tnfα Standards, supplied by R&D Systems, used in various techniques. Bioz Stars score: 97/100, based on 1694 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+tnf%CE%B1+standards/Recombinant+Human+TNF-alpha+Protein/10__3390_slash_immuno6020029-150-35-38
    Average 97 stars, based on 1694 article reviews
    recombinant tnfα standards - by Bioz Stars, 2026-09
    97/100 stars

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    Suspension:

    Article Title: Size-Based Targeting of Anti-Inflammatory Nanoparticles for Drug Delivery to Blast-Injured BBB for TBI Treatment
    Article Snippet: Cells were prepared for the assay by detaching with 0.25% trypsin and 0.02% EDTA (Sigma-Aldrich Chemical) and resuspension in culture medium supplemented with 1 μg/mL actinomycin D (Calbiochem, La Jolla, CA, USA) to a concentration of 500,000 cells/mL. .. One hundred microliters of cell suspension were added to each well of a flat-bottom 96-well tissue culture plate containing 100 μL of 2-fold serial dilutions of unknown samples, in duplicate, or known concentrations of human recombinant TNFα standards (R&D Systems, Minneapolis, MN, USA) in diluting medium, RPMI-1640, 2 mM L-glutamine, 1% fetal bovine serum, and 15 mM HEPES (Sigma-Aldrich Chemical). .. Following 20 h of incubation at 37 ◦C, 95% RH, and https://doi.org/10.3390/immuno6020029 5% CO2, 10 μL of Cell Proliferation Reagent WST-1 (a solution of the tetrazolium salt, WST-1 (4-[3-(4-iodophenyl)-2-(4nitrophenyl)-2H-5-tetrazolio]-1,3 benzene disulfonate) and the electron coupling reagent, mPMS (1-methoxy-5-methyl-phenazinium methyl sulfate); Roche Diagnostics, Indianapolis, IN, USA) in diluting medium was added to each well.

    Recombinant:

    Article Title: Size-Based Targeting of Anti-Inflammatory Nanoparticles for Drug Delivery to Blast-Injured BBB for TBI Treatment
    Article Snippet: Cells were prepared for the assay by detaching with 0.25% trypsin and 0.02% EDTA (Sigma-Aldrich Chemical) and resuspension in culture medium supplemented with 1 μg/mL actinomycin D (Calbiochem, La Jolla, CA, USA) to a concentration of 500,000 cells/mL. .. One hundred microliters of cell suspension were added to each well of a flat-bottom 96-well tissue culture plate containing 100 μL of 2-fold serial dilutions of unknown samples, in duplicate, or known concentrations of human recombinant TNFα standards (R&D Systems, Minneapolis, MN, USA) in diluting medium, RPMI-1640, 2 mM L-glutamine, 1% fetal bovine serum, and 15 mM HEPES (Sigma-Aldrich Chemical). .. Following 20 h of incubation at 37 ◦C, 95% RH, and https://doi.org/10.3390/immuno6020029 5% CO2, 10 μL of Cell Proliferation Reagent WST-1 (a solution of the tetrazolium salt, WST-1 (4-[3-(4-iodophenyl)-2-(4nitrophenyl)-2H-5-tetrazolio]-1,3 benzene disulfonate) and the electron coupling reagent, mPMS (1-methoxy-5-methyl-phenazinium methyl sulfate); Roche Diagnostics, Indianapolis, IN, USA) in diluting medium was added to each well.



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    R&D Systems recombinant tnfα standards
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    R&D Systems recombinant human tnfα protein standard
    Inhibition of LPS-stimulated <t>TNFα</t> production in PBMCs from two donors for charged triazolinium bromide salt 17 .
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    PeproTech standard recombinant human tnf-α protein
    Transduction with lentivirus vectors does not result in inflammatory activation of CHME-5 or HTB-11 cells . <t>Endogenous</t> <t>TNF-α</t> secretion into the conditioned media of cells was measured by ELISA. Cells tested were as follows: CHME-NT, HTB-NT: non-transduced CHME-5 or HTB-11 cells; CHME-Fc, HTB-Fc: CHME-5 or HTB-11 cells transduced with the empty vector expressing Fc fragment. Results shown represent mean levels <t>of</t> <t>TNF-α</t> expression from three independent experiments and error bars denote the standard deviation.
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    Inhibition of LPS-stimulated TNFα production in PBMCs from two donors for charged triazolinium bromide salt 17 .

    Journal: Molecules

    Article Title: Photochemically Assisted Synthesis of Thienobenzotriazole-Based Dual Cholinesterase Inhibitors

    doi: 10.3390/molecules30163439

    Figure Lengend Snippet: Inhibition of LPS-stimulated TNFα production in PBMCs from two donors for charged triazolinium bromide salt 17 .

    Article Snippet: TNFα concentration in supernatants was measured by ELISA using antibodies and recombinant human TNFα protein (standard) from R&D Systems.

    Techniques: Inhibition

    Transduction with lentivirus vectors does not result in inflammatory activation of CHME-5 or HTB-11 cells . Endogenous TNF-α secretion into the conditioned media of cells was measured by ELISA. Cells tested were as follows: CHME-NT, HTB-NT: non-transduced CHME-5 or HTB-11 cells; CHME-Fc, HTB-Fc: CHME-5 or HTB-11 cells transduced with the empty vector expressing Fc fragment. Results shown represent mean levels of TNF-α expression from three independent experiments and error bars denote the standard deviation.

    Journal: Journal of Neuroinflammation

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    doi: 10.1186/1742-2094-8-48

    Figure Lengend Snippet: Transduction with lentivirus vectors does not result in inflammatory activation of CHME-5 or HTB-11 cells . Endogenous TNF-α secretion into the conditioned media of cells was measured by ELISA. Cells tested were as follows: CHME-NT, HTB-NT: non-transduced CHME-5 or HTB-11 cells; CHME-Fc, HTB-Fc: CHME-5 or HTB-11 cells transduced with the empty vector expressing Fc fragment. Results shown represent mean levels of TNF-α expression from three independent experiments and error bars denote the standard deviation.

    Article Snippet: One microgram of standard recombinant human TNF-α protein (PeproTech Inc, New Jersey) was spotted onto a marked area of the NCM and allowed to dry at RT for 30-45 min.

    Techniques: Transduction, Activation Assay, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Expressing, Standard Deviation

    Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Journal: Journal of Neuroinflammation

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    doi: 10.1186/1742-2094-8-48

    Figure Lengend Snippet: Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Article Snippet: One microgram of standard recombinant human TNF-α protein (PeproTech Inc, New Jersey) was spotted onto a marked area of the NCM and allowed to dry at RT for 30-45 min.

    Techniques: Binding Assay, Western Blot, Recombinant, Incubation, Purification, Positive Control

    Functional antagonization of sTNFR-Fc against TNF-α . As described in materials and methods, TNF-α sensitive L929 cells were treated with TNF-α alone (80 ng/mL) or with TNF-α plus culture supernatants from vector-transduced cells; purified recombinant sTNFR-Fc protein (160 ng/mL) was used as a positive control. After incubation for 24 h, cell viability was then evaluated by MTT assay. Viability was significantly higher for the cells treated with conditioned medium from transduced cells expressing hTNFR-Fc (** p < 0.01 for HTB-T; *p < 0.05 for CHME-T) when compared to cultures that received TNF-α alone, or TNF-α plus culture supernatants from parental cells (CHME-N and HTB-N). Results shown represent mean levels of three independent experiments and error bars denote the standard deviation.

    Journal: Journal of Neuroinflammation

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    doi: 10.1186/1742-2094-8-48

    Figure Lengend Snippet: Functional antagonization of sTNFR-Fc against TNF-α . As described in materials and methods, TNF-α sensitive L929 cells were treated with TNF-α alone (80 ng/mL) or with TNF-α plus culture supernatants from vector-transduced cells; purified recombinant sTNFR-Fc protein (160 ng/mL) was used as a positive control. After incubation for 24 h, cell viability was then evaluated by MTT assay. Viability was significantly higher for the cells treated with conditioned medium from transduced cells expressing hTNFR-Fc (** p < 0.01 for HTB-T; *p < 0.05 for CHME-T) when compared to cultures that received TNF-α alone, or TNF-α plus culture supernatants from parental cells (CHME-N and HTB-N). Results shown represent mean levels of three independent experiments and error bars denote the standard deviation.

    Article Snippet: One microgram of standard recombinant human TNF-α protein (PeproTech Inc, New Jersey) was spotted onto a marked area of the NCM and allowed to dry at RT for 30-45 min.

    Techniques: Functional Assay, Plasmid Preparation, Purification, Recombinant, Positive Control, Incubation, MTT Assay, Expressing, Standard Deviation

    sTNFR-Fc mediated protection of neuronal cells from TNF-α, HIV-Tat and gp120 . (A) Non-transduced human neuronal cells, HTB-11, were treated with TNF-α alone (80 ng/mL), or with TNF-α plus culture supernatants (1:10 dilution) from vector-transduced cells (as indicated). Cells were incubated at 37°C for 3 days, and viability of the cells was determined by the trypan blue exclusion assay. sTNFR-Fc = supernatant collected from HTB-11 or CHME-5 cells transduced with the hTNFR-Fc encoding vector; Fc = supernatant collected from HTB-11 or CHME-5 cells transduced with the vector encoding human Fc only; rTNFR = purified commercial recombinant TNFR-Fc protein (160 ng/mL), used as a positive control. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (B) Vector transduced human HTB-11 cells were exposed to TNF-α as described in 7A. HTB-11 cells transduced either with the sTNFR-Fc or Fc encoding vector were used in this experiment, along with non-transduced cells as controls. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (C) sTNFR-Fc protects primary rat neurons against HIV-1 Tat-mediated toxicity. Medium from vector-transduced or parental HTB-11 cells was collected at day 10, diluted and mixed with 500 nM HIV-1 Tat protein, prior to addition to primary rat neurons. Following 24 hours incubation at 37°C, these test cultures along with the control were analyzed by TUNEL assay. Cell death was significantly reduced in neuronal cultures that were treated with Tat plus conditioned medium from HTB-11 cells transduced with the sTNRF-Fc encoding lentiviral vector (HTB-T 10d) versus cells treated with Tat plus conditioned medium from parental HTB-11 cells (HTB 10d) (*p < 0.01). NT, normal neuronal cells received no Tat, and -, neuronal cells exposed to Tat as a positive control. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (D) sTNFR-Fc mediated neuronal protection of human HTB-11 cells against HIV-1 gp120 toxicity. Conditioned media from hTNFR-Fc or Fc vector transduced HTB-11 cells were collected, diluted and mixed with 100 ng/mL (gp120A) or 250 ng/mL (gp120B) HIV-1 gp120 protein, with or without HIV-1 Tat, prior to addition to HTB-11 cells. Following 3 days incubation at 37°C, cell viability of these cultures, together with control cultures, was determined by trypan blue exclusion assay (***p < 0.001). Results shown represent mean levels of three independent experiments and error bars denote the standard deviation.

    Journal: Journal of Neuroinflammation

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    doi: 10.1186/1742-2094-8-48

    Figure Lengend Snippet: sTNFR-Fc mediated protection of neuronal cells from TNF-α, HIV-Tat and gp120 . (A) Non-transduced human neuronal cells, HTB-11, were treated with TNF-α alone (80 ng/mL), or with TNF-α plus culture supernatants (1:10 dilution) from vector-transduced cells (as indicated). Cells were incubated at 37°C for 3 days, and viability of the cells was determined by the trypan blue exclusion assay. sTNFR-Fc = supernatant collected from HTB-11 or CHME-5 cells transduced with the hTNFR-Fc encoding vector; Fc = supernatant collected from HTB-11 or CHME-5 cells transduced with the vector encoding human Fc only; rTNFR = purified commercial recombinant TNFR-Fc protein (160 ng/mL), used as a positive control. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (B) Vector transduced human HTB-11 cells were exposed to TNF-α as described in 7A. HTB-11 cells transduced either with the sTNFR-Fc or Fc encoding vector were used in this experiment, along with non-transduced cells as controls. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (C) sTNFR-Fc protects primary rat neurons against HIV-1 Tat-mediated toxicity. Medium from vector-transduced or parental HTB-11 cells was collected at day 10, diluted and mixed with 500 nM HIV-1 Tat protein, prior to addition to primary rat neurons. Following 24 hours incubation at 37°C, these test cultures along with the control were analyzed by TUNEL assay. Cell death was significantly reduced in neuronal cultures that were treated with Tat plus conditioned medium from HTB-11 cells transduced with the sTNRF-Fc encoding lentiviral vector (HTB-T 10d) versus cells treated with Tat plus conditioned medium from parental HTB-11 cells (HTB 10d) (*p < 0.01). NT, normal neuronal cells received no Tat, and -, neuronal cells exposed to Tat as a positive control. Results shown represent mean levels of three independent experiments and error bars denote the standard deviation. (D) sTNFR-Fc mediated neuronal protection of human HTB-11 cells against HIV-1 gp120 toxicity. Conditioned media from hTNFR-Fc or Fc vector transduced HTB-11 cells were collected, diluted and mixed with 100 ng/mL (gp120A) or 250 ng/mL (gp120B) HIV-1 gp120 protein, with or without HIV-1 Tat, prior to addition to HTB-11 cells. Following 3 days incubation at 37°C, cell viability of these cultures, together with control cultures, was determined by trypan blue exclusion assay (***p < 0.001). Results shown represent mean levels of three independent experiments and error bars denote the standard deviation.

    Article Snippet: One microgram of standard recombinant human TNF-α protein (PeproTech Inc, New Jersey) was spotted onto a marked area of the NCM and allowed to dry at RT for 30-45 min.

    Techniques: Plasmid Preparation, Incubation, Trypan Blue Exclusion Assay, Transduction, Purification, Recombinant, Positive Control, Standard Deviation, TUNEL Assay