The Chimeric Chimeric anti-SARS-CoV-2 Spike antibody has been validated for ELISA and GICA. It is suitable to detect SARS-CoV-2 Spike in samples from SARS Coronavirus-2 (SARS-CoV-2).
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)
SARS-CoV-2 S
Reactivity: SARS Coronavirus-2 (SARS-CoV-2)
ELISA, Neut, GICA
Host: Human
Monoclonal
A1
Fc Tag
single-domain Antibody (sdAb)
Recombinant Antibody
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 Spike (SARS-CoV-2 S)
Alternative Name
SARS-CoV-2 (SARS-CoV-2/ 2019-nCoV) S
Target Type
Viral Protein
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.