Rekombinanter SARS-CoV-2 Spike S1 Antikörper (RBD)
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- Target Alle SARS-CoV-2 Spike S1 Antikörper anzeigen
- SARS-CoV-2 Spike S1
- Antikörpertyp
- Recombinant Antibody
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Bindungsspezifität
- RBD
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Reaktivität
- SARS Coronavirus-2 (SARS-CoV-2), SARS Coronavirus (SARS-CoV)
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Wirt
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Human
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Klonalität
- Monoklonal
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Konjugat
- Dieser SARS-CoV-2 Spike S1 Antikörper ist unkonjugiert
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Applikation
- ELISA, Immunofluorescence (IF), Crystallization (Crys), Surface Plasmon Resonance (SPR)
- Verwendungszweck
- Recombinant monoclonal antibody to COVID-19 & SARS-CoV S glycoprotein.
- Spezifität
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The antibody CR3022 binds the amino acids 318-510 in the S1 domain of the SARS-CoV Spike protein as well as SARS-CoV-2 (COVID-19) Spike protein. The antibody also binds to P462L-substituted S318-510 fragments of the SARS spike protein. The binding epitope is only accessible in the "open" conformation of the spike protein (Joyce et al. 2020).
While most S-protein RBD binding antibodies compete for antigen binding with ACE2, the CR3022 epitope does not overlap with the ACE2-binding site. It does thus not hinder binding of neutralizing antibodies. While CR3022 on its own exhibits only a weak neutralizing effect, it has been shown to synergize with other S-protein RBD binding antibodies to neutralize SARS-CoV. This effect still has to be confirmed in context with SARS-CoV-2 (Yuan et al. 2020).
- Kreuzreaktivität (Details)
- The anti-SARS-CoV-2 antibody CR3022 was originally discovered in a SARS patient, but it was shown to be a potent binder of SARS-CoV-2 spike protein (S1).
- Produktmerkmale
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OriginalSpeciesName: Human
OriginalFormat: IgG1
- Aufreinigung
- Affinity Purified using a recombinant lectin column
- Immunogen
- The original monoclonal antibody was generated by sequencing peripheral blood lymphocytes of a patient exposed to the SARS-CoV.
- Klon
- CR3022
- Isotyp
- IgA1 kappa
- Top Product
- Discover our top product SARS-CoV-2 Spike S1 Primärantikörper
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- Applikationshinweise
- This antibody (CR3022) binds to both SARS-CoV and SARS-CoV-2 with high affinity. The initial characterization of the binding of this antibody was performed by ELISA and indicates potential for the development of diagnostic assays, as both virus-capture assays, or as controls in serological assays measuring immune-responses to virus exposure. Human IgG1, IgG3, IgM and IgA isotypes are available to mimic antibody responses seen in COVID19 (Amanat et al. 2020). Human IgG2 is available to assess its yet unknown role in the response to SARS-CoV-2. The original human IgG1 version of the antibody works synergistically in combination with another non-competing SARS antibody CR3014 and is a potential candidate for passive immune prophylaxis of SARS-CoV infection (Meulen et al., 2006). The original antibody (human IgG1) was also reported to bind the 2019-nCoV RBD (KD of 6.3 nM). This antibody has been attributed a potential to be developed as a therapeutic agent, alone or in combination with other neutralizing antibodies for treatment of 2019-nCoV infections (Tian et al., 2020).
- Kommentare
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This reformatted human antibody was made using the variable domain sequences of the original Human IgG1 format, for improved compatibility with existing reagents, assays and techniques.
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Konzentration
- 1 mg/mL
- Buffer
- PBS with 0.02 % Proclin 300.
- Konservierungsmittel
- ProClin
- Vorsichtsmaßnahmen
- This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Lagerung
- 4 °C,-20 °C
- Informationen zur Lagerung
- Store at 4°C for up to 3 months. For longer storage, aliquot and store at -20°C.
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- Target
- SARS-CoV-2 Spike S1
- Abstract
- SARS-CoV-2 Spike S1 Produkte
- Synonyme
- E2 antikoerper, Surface Glycoprotein antikoerper, S antikoerper
- Substanzklasse
- Viral Protein
- Hintergrund
- Spike protein, COVID19, COVID 19, S protein, SARS-CoV S protein, S glycoprotein, E2, Peplomer protein, Spike protein S1, SARS Coronavirus, SARS-CoV-2, SARS CoV 2, 2019-nCoV
- UniProt
- P59594
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