mouse anti-human ifnar2 antibody clone mmhar-2 Search Results


monoclonal mouse anti human ifnar2  (PBL Assay)
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PBL Assay monoclonal mouse anti human ifnar2
Monoclonal Mouse Anti Human Ifnar2, supplied by PBL Assay, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse monoclonal anti human infar ii  (Miltenyi Biotec)
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Miltenyi Biotec mouse monoclonal anti human infar ii
Mouse Monoclonal Anti Human Infar Ii, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse-anti-ifnar2-pe mmhar-2  (PBL Biomedical Laboratories)
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PBL Biomedical Laboratories mouse-anti-ifnar2-pe mmhar-2
Mouse Anti Ifnar2 Pe Mmhar 2, supplied by PBL Biomedical Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti ifnα  (PBL Assay)
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PBL Assay anti ifnα
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
Anti Ifnα, supplied by PBL Assay, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pe-conjugated mouse igg1κ isotype control  (Becton Dickinson)
90
Becton Dickinson pe-conjugated mouse igg1κ isotype control
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
Pe Conjugated Mouse Igg1κ Isotype Control, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human ifnα2  (PBL Assay)
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PBL Assay human ifnα2
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
Human Ifnα2, supplied by PBL Assay, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibody mouse monoclonal antihuman cd163  (Novocastra)
86
Novocastra antibody mouse monoclonal antihuman cd163
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
Antibody Mouse Monoclonal Antihuman Cd163, supplied by Novocastra, 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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alexafluor 555 cell signaling technology  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc alexafluor 555 cell signaling technology
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
Alexafluor 555 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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goat antimouse igg  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc goat antimouse igg
Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the <t>(A)</t> <t>IFNα2/IFNAR1/IFNAR2</t> complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by <t>IFNα</t> arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.
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Image Search Results


Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the (A) IFNα2/IFNAR1/IFNAR2 complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by IFNα arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.

Journal: The Journal of Biological Chemistry

Article Title: Human interferon-ϵ and interferon-κ exhibit low potency and low affinity for cell-surface IFNAR and the poxvirus antagonist B18R

doi: 10.1074/jbc.RA118.003617

Figure Lengend Snippet: Molecular model of unique IFNϵ/κ and IFNα1 residues that modulate IFNAR2 and B18R binding. A and B, schematic models and structures of the (A) IFNα2/IFNAR1/IFNAR2 complex (PDB 3SE3) and the (B) IFNα2/B18R complex (IFNα2 from PDB 3S9D, and B18R derived from the C12R structure, PDB 3OQ3). C, ribbon diagram of the IFNα2 backbone with key residues that regulate IFNAR2 and B18R binding affinity, as discussed in the text, shown in yellow, orange, and magenta. D, superposition of IFNs in IFN/IFNAR2 and IFN/B18R structures with B18R D3 domain in red and the IFNAR2 D1 domain cyan. Three negatively charged residues conserved in IFNAR2 (green) and B18R (yellow) are positioned by IFNα arginines: Arg-35, Arg-56, and Arg=172 (magenta). E, amino acids within the AB loop region of IFNs that distinguish strong and weak IFNAR2 and B18R binders. Amino acid substitutions made to produce IFNα1 and IFNκ mutants are shown in bold.

Article Snippet: Reagents used in the assays included anti-IFNα (MMHA-2, PBL Assay Science), anti-IFNAR1 (ab10739, Abcam), and anti-IFNAR2 (MMHAR-2, PBL Assay Science) neutralizing antibodies, soluble receptors IFNAR1-FC (245-AB-050, R&D Systems) and IFNAR2-FC (4015-AB-050, R&D Systems), and viral type-I antagonist B18R (34-8185-85, eBioscience).

Techniques: Binding Assay, Derivative Assay