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anti mers cov s2 antibody  (Sino Biological)


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    Sino Biological anti mers cov s2 antibody
    Anti Mers Cov S2 Antibody, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mers cov s2 antibody/product/Sino Biological
    Average 94 stars, based on 6 article reviews
    anti mers cov s2 antibody - by Bioz Stars, 2026-03
    94/100 stars

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    Anti Mers Cov S2 Antibody, supplied by Sino Biological, 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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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation <t>on</t> <t>SARS-CoV-2</t> SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and <t>MERS)</t> shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.
    Mers Cov S2 Antibody Sino Biological, supplied by Sino Biological, 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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    Average 94 stars, based on 1 article reviews
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    Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation on SARS-CoV-2 SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS) shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.

    Journal: Journal of Virology

    Article Title: Human antibody targeting of coronavirus spike S2 subunit is associated with protection mediated by Fc effector functions

    doi: 10.1128/jvi.01523-25

    Figure Lengend Snippet: Broad β-CoV binding of mAb 1871. ( A ) Sequence conservation across the panel of β-CoV SP listed in Fig. 4B shown in a colored representation on SARS-CoV-2 SP PDB ID: 6XR8 . The left panel shows conservation across sarbecovirus sequences, and the right panel shows conservation across β-CoV SP. Pink indicates conserved residues and teal indicates variable residues. Amino acids with insufficient data are shown in yellow. Coloring generated using the Consurf server ( ). Consurf mapping was generated based on sequence homology of the supplied model of SARS-CoV-2 spike, PDB ID: 6XR8 . ( B ) Comparison of apparent binding affinity (K D ) of mAb 1871 to full-length SP (SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS) shown as red circles and SARS-CoV-2 prefusion stabilized trimer shown as a black circle. K D values generated by global fitting from six different mAb concentrations from a single representative experimental data are depicted. ( C ) Sensograms showing binding kinetics of mAb 1871 to full-length SARS-CoV, SARS-CoV-2, HKU-1, OC43, RatG13, and MERS SP. Red lines represent raw data, and black lines represent global fit.

    Article Snippet: His-tagged full-length spike proteins SARS-CoV (Sino Biological, Cat#40634-V08B), SARS-CoV-2, MERS (Sino Biological, Cat#40069-V08B), HKU-1 (Sino Biological, Cat#40606-V08B), OC-43 (Sino Biological, Cat#40607-V08B), HCoV-229E (Sino Biological, Cat#40605-V08B) or S2 subunit SARS-CoV (Sino Biological, Cat#40150-V08B), SARS-CoV-2 (Sino Biological, Cat#40590-V08B), MERS (Sino Biological, Cat#40070-V08B), OC-43 or SARS-CoV-2 full-length prefusion stabilized trimer was loaded onto Ni-NTA biosensors (Sartorius ForteBio) until it achieved a 0.5–0.8 nm signal response or reached a maximum loading time of 800 s. The antigen loading time varied from 50 s to 800 s, resulting in 0.5–0.8 nm signal response depending on antigen ( ).

    Techniques: Binding Assay, Sequencing, Generated, Comparison