anti mouse tnfr1 Search Results


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Bio-Techne corporation mouse tnf ri/tnfrsf1a antibody
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Genzyme mouse tnfr1
Expression of mRNAs of <t>TNFR1,</t> TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for <t>TNFR1,</t> TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.
Mouse Tnfr1, supplied by Genzyme, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology mouse tnfr1
Expression of mRNAs of <t>TNFR1,</t> TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for <t>TNFR1,</t> TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.
Mouse Tnfr1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse tnfr1/product/Santa Cruz Biotechnology
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ABclonal Biotechnology anti mouse tnfr1
Expression of mRNAs of <t>TNFR1,</t> TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for <t>TNFR1,</t> TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.
Anti Mouse Tnfr1, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology mouse anti tnfr1
Expression of mRNAs of <t>TNFR1,</t> TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for <t>TNFR1,</t> TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.
Mouse Anti Tnfr1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse anti tnfr1/product/Santa Cruz Biotechnology
Average 86 stars, based on 1 article reviews
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Image Search Results


Expression of mRNAs of TNFR1, TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for TNFR1, TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.

Journal: The Journal of Experimental Medicine

Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction

doi:

Figure Lengend Snippet: Expression of mRNAs of TNFR1, TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for TNFR1, TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.

Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co. Anti–mouse TNFR1 and TNFR2 antibodies were purchased from Genzyme Diagnostics.

Techniques: Expressing, Activation Assay, Purification, Electrophoretic Mobility Shift Assay, Binding Assay

TRAP-positive cell formation induced by mouse TNF-α in M-BMMφ requires both TNFR1- and TNFR2-mediated signals. (A) M-BMMφ prepared from ddY mice were further cultured for 3 d with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) (bottom) in the presence of M-CSF (100 ng/ml). M-BMMφ were simultaneously treated with or without control IgG (30 μg/ml), anti–TNFR1 antibody (10 μg/ml), or anti–TNFR2 antibody (30 μg/ml). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of three cultures. Similar results were obtained in three independent experiments. (B) M-BMMφ were prepared from normal C57BL/6J mice (wild type), TNFR1-deficient C57BL/6J mice [TNFR1(−/−)] or TNFR2-deficient C57BL/6J mice [TNFR2(−/−)]. M-BMMφ were further cultured with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) in the presence of M-CSF (100 ng/ml) (bottom). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of four mice in each group. *Significantly different from the control (A) or wild type (B); P < 0.01.

Journal: The Journal of Experimental Medicine

Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction

doi:

Figure Lengend Snippet: TRAP-positive cell formation induced by mouse TNF-α in M-BMMφ requires both TNFR1- and TNFR2-mediated signals. (A) M-BMMφ prepared from ddY mice were further cultured for 3 d with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) (bottom) in the presence of M-CSF (100 ng/ml). M-BMMφ were simultaneously treated with or without control IgG (30 μg/ml), anti–TNFR1 antibody (10 μg/ml), or anti–TNFR2 antibody (30 μg/ml). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of three cultures. Similar results were obtained in three independent experiments. (B) M-BMMφ were prepared from normal C57BL/6J mice (wild type), TNFR1-deficient C57BL/6J mice [TNFR1(−/−)] or TNFR2-deficient C57BL/6J mice [TNFR2(−/−)]. M-BMMφ were further cultured with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) in the presence of M-CSF (100 ng/ml) (bottom). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of four mice in each group. *Significantly different from the control (A) or wild type (B); P < 0.01.

Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co. Anti–mouse TNFR1 and TNFR2 antibodies were purchased from Genzyme Diagnostics.

Techniques: Cell Culture, Staining

Schematic representation of ligand-receptor systems in osteoclast differentiation and function regulated by TNF-α, ODF/RANKL, and IL-1α. TNF-α and ODF/RANKL independently stimulate osteoclast differentiation. Osteoclast differentiation induced by TNF-α occurs via TNFR1 and TNFR2 expressed by osteoclast precursors. ODF/RANKL induces osteoclast differentiation through RANK-mediated signals. M-CSF is a common factor required for both TNF-α– and ODF/RANKL-induced osteoclast differentiation. Activation of osteoclasts is induced by ODF/RANKL and IL-1α through RANK and type 1 IL-1 receptor, respectively. Common signaling cascades such as NF-κB and JNK activation may be involved in the differentiation and activation of osteoclasts induced by TNF-α, ODF/RANKL, and IL-1α.

Journal: The Journal of Experimental Medicine

Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction

doi:

Figure Lengend Snippet: Schematic representation of ligand-receptor systems in osteoclast differentiation and function regulated by TNF-α, ODF/RANKL, and IL-1α. TNF-α and ODF/RANKL independently stimulate osteoclast differentiation. Osteoclast differentiation induced by TNF-α occurs via TNFR1 and TNFR2 expressed by osteoclast precursors. ODF/RANKL induces osteoclast differentiation through RANK-mediated signals. M-CSF is a common factor required for both TNF-α– and ODF/RANKL-induced osteoclast differentiation. Activation of osteoclasts is induced by ODF/RANKL and IL-1α through RANK and type 1 IL-1 receptor, respectively. Common signaling cascades such as NF-κB and JNK activation may be involved in the differentiation and activation of osteoclasts induced by TNF-α, ODF/RANKL, and IL-1α.

Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co. Anti–mouse TNFR1 and TNFR2 antibodies were purchased from Genzyme Diagnostics.

Techniques: Activation Assay