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Recombinant SARS-CoV-2 (SARS-CoV-2/ 2019-nCoV) S (AA 16-685) antibody

The Chimeric Chimeric anti- antibody has been validated for ELISA and GICA. It is suitable to detect in samples from SARS Coronavirus-2 (SARS-CoV-2).
Catalog No. ABIN6953151

Quick Overview for Recombinant SARS-CoV-2 (SARS-CoV-2/ 2019-nCoV) S (AA 16-685) antibody (ABIN6953151)

Target

SARS-CoV-2 (SARS-CoV-2/ 2019-nCoV) S

Antibody Type

Recombinant Antibody

Reactivity

SARS Coronavirus-2 (SARS-CoV-2)

Host

  • 4
Chimeric

Clonality

  • 3
  • 1
Chimeric

Conjugate

  • 1
  • 1
  • 1
  • 1
Un-conjugated

Application

  • 4
  • 1
  • 1
ELISA, Colloidal Gold Immunochromatography Assay (GICA)

Clone

H6
  • Binding Specificity

    AA 16-685

    Purpose

    S Recombinant Monoclonal Antibody

    Characteristics

    Recombinant anti-SARS-CoV-2 spike is expressed from 293 cells (HEK293) ,It is a chimeric monoclonal antibody combining the mouse variable regions with the constant domains of human IgG1.
    Monoclonal mouse (varialbe region) / human (kappa / IgG1 constant)chimeric antibody.
    AA 16-685

    Purification

    Affinity-chromatography

    Immunogen

    Recombinant Human Novel Coronavirus Spike glycoprotein (S) (16-685aa) (CSB-MP3324GMY)

    Isotype

    Ig kappa, IgG1
  • Application Notes

    ELISA:1:10000-1:50000, GICA:1:500-1:25000

    Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Preservative: 0.03 % Proclin 300
    Constituents: 50 % Glycerol, 0.01M PBS, PH 7.4

    Preservative

    ProClin

    Precaution of Use

    This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    -20 °C,-80 °C

    Storage Comment

    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze
  • Target

    SARS-CoV-2 (SARS-CoV-2/ 2019-nCoV) S

    Background

    Spike glycoprotein comprises two functional subunits responsible for binding to the host cell receptor (S1 subunit) and fusion of the viral and cellular membranes (S2 subunit). For many coronavirus (CoVs), S is cleaved at the boundary between the S1 and S2 subunits, which remain non-covalently bound in the prefusion conformation. The distal S1 subunit comprises the receptor-binding domain(s) and contributes to stabilization of the prefusion state of the membrane-anchored S2 subunit that contains the fusion machinery. S is further cleaved by host proteases at the so-called S2' site located immediately upstream of the fusion peptide in all CoVs. This cleavage has been proposed to activate the protein for membrane fusion via extensive irreversible conformational changes. However, different CoVs use distinct domains within the S1 subunit to recognize a variety of attachment and entry receptors, depending on the viral species. Endemic human coronaviruses OC43 and HKU1 attach via their S domain A to 5-N-acetyl-9-O-acetyl-sialosides found on glycoproteins and glycolipids at the host cell surface to enable entry into susceptible cells. MERS-CoV S uses domain A to recognize non-acetylated sialoside attachment receptors, which likely promote subsequent binding of domain B to the entry receptor, dipeptidyl-peptidase 4. SARS-CoV and several SARS-related coronaviruses (SARSr-CoV) interact directly with angiotensin-converting enzyme 2 (ACE2) via SB to enter target cells.

    Gene ID

    43740568

    UniProt

    P0DTC2
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