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htnfr2  (R&D Systems)


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    Structured Review

    R&D Systems htnfr2
    Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a <t>hTNFR2-hTNFα</t> trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.
    Htnfr2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/htnfr2/pm34699840-53-20-21?v=R%26D+Systems
    Average 94 stars, based on 13 article reviews
    htnfr2 - by Bioz Stars, 2026-08
    94/100 stars

    Images

    1) Product Images from "Generation and characterization of novel co-stimulatory anti-mouse TNFR2 antibodies."

    Article Title: Generation and characterization of novel co-stimulatory anti-mouse TNFR2 antibodies.

    Journal: Journal of immunological methods

    doi: 10.1016/j.jim.2021.113173

    Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a hTNFR2-hTNFα trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.
    Figure Legend Snippet: Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a hTNFR2-hTNFα trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.

    Techniques Used: Enzyme-linked Immunosorbent Assay



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    Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a <t>hTNFR2-hTNFα</t> trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.
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    Image Search Results


    Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a hTNFR2-hTNFα trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.

    Journal: Journal of immunological methods

    Article Title: Generation and characterization of novel co-stimulatory anti-mouse TNFR2 antibodies.

    doi: 10.1016/j.jim.2021.113173

    Figure Lengend Snippet: Fig. 2. Characterization of anti-mTNFR2 mAbs targeting CRDs 1–4. (A) Schematic representation of the 6 mouse-human TNF2 chimeras CRD1-CRD4 (Cystein Rich Domain). (B) The targeting CRD of each mAb were determined by cell ELISA with mouse-human TNFR2 domain swap mutants. Data represented as a three-parameter OD450–620 detection based on mean and SD of three independent experiments. (C) The domain epitopes of the 13 mAbs are indicated on a hTNFR2-hTNFα trimer structure (PDB: 3ALQ), 74% similar to mouse TNFR2. The CRDs for one TNFR2 receptor are shown in indicated colors.

    Article Snippet: Immunoreactivity to mouse TNFR2 and cross-reactivity to human TNFR2 was assessed by ELISA using recombinant mTNFR2/Fc-protein (R&D Systems, 9707-R2) and hTNFR2 (R&D Systems, 726-R2) as well as CHO-K1.mTNFR2 and CHO-K1.hTNFR2.

    Techniques: Enzyme-linked Immunosorbent Assay

    TABLE 3

    Journal: The Journal of Biological Chemistry

    Article Title: Comparative Biochemical and Functional Analysis of Viral and Human Secreted Tumor Necrosis Factor (TNF) Decoy Receptors *

    doi: 10.1074/jbc.M115.650119

    Figure Lengend Snippet: TABLE 3

    Article Snippet: Recombinant His-tagged proteins were purified from supernatants of Hi5 cells infected at high multiplicity using nickel-nitrilotriacetic acid columns (Qiagen) ( 22 ). hTNFR2-Fc was purified using protein A-coupled Sepharose (Sigma) followed by size exclusion chromatography.

    Techniques: Derivative Assay, Binding Assay