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primary goat antimouse cd147  (R&D Systems)


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    Structured Review

    R&D Systems primary goat antimouse cd147
    Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse <t>CD147</t> allele (flanking primers BSGC and BSGD)
    Primary Goat Antimouse Cd147, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/goat+antimouse+primary+antibody/pm35690792-94-5-9?v=R%26D+Systems
    Average 93 stars, based on 3 article reviews
    primary goat antimouse cd147 - by Bioz Stars, 2026-07
    93/100 stars

    Images

    1) Product Images from "Development of a novel human CD147 knock-in NSG mouse model to test SARS-CoV-2 viral infection."

    Article Title: Development of a novel human CD147 knock-in NSG mouse model to test SARS-CoV-2 viral infection.

    Journal: Cell & bioscience

    doi: 10.1186/s13578-022-00822-6

    Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse CD147 allele (flanking primers BSGC and BSGD)
    Figure Legend Snippet: Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse CD147 allele (flanking primers BSGC and BSGD)

    Techniques Used: Expressing

    Fig. 5 Diagram of proposed working hypothesis of CD147 in SARS-CoV-2 infection. (1) SARS-CoV-2 virions infect human cells via the canonical pathway where host Angiotensin-converting Enzyme 2 (ACE2) receptors bind to viral spike proteins (red) and facilitate viral entry and infection. (2) CD147 proteins, via binding to surface binding partners (e.g., E-selectin), facilitate cell–cell adhesion, membrane fusion, and intercellular transfer of SARS-CoV-2 virions. (3) Erythrocytes and platelets which strongly express CD147, bind SARS-CoV-2 virions, and increase thrombosis risk and other clinical manifestations of COVID-19
    Figure Legend Snippet: Fig. 5 Diagram of proposed working hypothesis of CD147 in SARS-CoV-2 infection. (1) SARS-CoV-2 virions infect human cells via the canonical pathway where host Angiotensin-converting Enzyme 2 (ACE2) receptors bind to viral spike proteins (red) and facilitate viral entry and infection. (2) CD147 proteins, via binding to surface binding partners (e.g., E-selectin), facilitate cell–cell adhesion, membrane fusion, and intercellular transfer of SARS-CoV-2 virions. (3) Erythrocytes and platelets which strongly express CD147, bind SARS-CoV-2 virions, and increase thrombosis risk and other clinical manifestations of COVID-19

    Techniques Used: Infection, Binding Assay, Membrane



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    Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse <t>CD147</t> allele (flanking primers BSGC and BSGD)
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    Image Search Results


    Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse CD147 allele (flanking primers BSGC and BSGD)

    Journal: Cell & bioscience

    Article Title: Development of a novel human CD147 knock-in NSG mouse model to test SARS-CoV-2 viral infection.

    doi: 10.1186/s13578-022-00822-6

    Figure Lengend Snippet: Fig. 1 Schematic representation of genotyping primers used to confirm hCD147KI expression. A combination of 4 primers was used to screen mice (internal primers hCD147A and hCD147B) and confirm proper integration into the mouse CD147 allele (flanking primers BSGC and BSGD)

    Article Snippet: Mouse CD147 was stained using primary goat antimouse CD147 (R&D Systems, BAF772) and visualized using Cy5-conjugated polyclonal donkey anti-goat IgG secondary (Jackson ImmunoResearch; 705–175-147).

    Techniques: Expressing

    Fig. 5 Diagram of proposed working hypothesis of CD147 in SARS-CoV-2 infection. (1) SARS-CoV-2 virions infect human cells via the canonical pathway where host Angiotensin-converting Enzyme 2 (ACE2) receptors bind to viral spike proteins (red) and facilitate viral entry and infection. (2) CD147 proteins, via binding to surface binding partners (e.g., E-selectin), facilitate cell–cell adhesion, membrane fusion, and intercellular transfer of SARS-CoV-2 virions. (3) Erythrocytes and platelets which strongly express CD147, bind SARS-CoV-2 virions, and increase thrombosis risk and other clinical manifestations of COVID-19

    Journal: Cell & bioscience

    Article Title: Development of a novel human CD147 knock-in NSG mouse model to test SARS-CoV-2 viral infection.

    doi: 10.1186/s13578-022-00822-6

    Figure Lengend Snippet: Fig. 5 Diagram of proposed working hypothesis of CD147 in SARS-CoV-2 infection. (1) SARS-CoV-2 virions infect human cells via the canonical pathway where host Angiotensin-converting Enzyme 2 (ACE2) receptors bind to viral spike proteins (red) and facilitate viral entry and infection. (2) CD147 proteins, via binding to surface binding partners (e.g., E-selectin), facilitate cell–cell adhesion, membrane fusion, and intercellular transfer of SARS-CoV-2 virions. (3) Erythrocytes and platelets which strongly express CD147, bind SARS-CoV-2 virions, and increase thrombosis risk and other clinical manifestations of COVID-19

    Article Snippet: Mouse CD147 was stained using primary goat antimouse CD147 (R&D Systems, BAF772) and visualized using Cy5-conjugated polyclonal donkey anti-goat IgG secondary (Jackson ImmunoResearch; 705–175-147).

    Techniques: Infection, Binding Assay, Membrane