SARS-CoV-2 Spike Protein Monoclonal Antibody [H6]

  • SARS-CoV-2 Spike Protein Monoclonal Antibody H6
  • SARS-CoV-2 Spike Protein Monoclonal Antibody H6
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SARS-CoV-2 Spike Protein Monoclonal Antibody [H6]

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.

Spike Protein Function

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.

Information Description

Uniprot No.

Target Names


Antibody Size


Alternative Names

S, S1, S1-RBD, Spike glycoprotein

Species Reactivity

Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)


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

Immunogen Species

Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)






Monoclonal mouse (varialbe region) / human (kappa / IgG1 constant)chimeric antibody

Clone No.


Purification Method



It differs from different batches. Please contact us to confirm it.


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



Tested Applications


Recommended Dilution

Application Recommended Dilution






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

Subcellular Location

Virion membrane, Single-pass type I membrane protein, Host endoplasmic reticulum-Golgi intermediate compartment membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein.

Protein Families

Betacoronaviruses spike protein family

SARS-CoV-2 Spike glycoprotein Information

Key Information Description



Spike glycoprotein




Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)

Alternative Names:

Spike glycoprotein, S glycoprotein, E2, Peplomer protein

Spike protein function

Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.

Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.

Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.

Post-Translational Modification

The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.

Specific enzymatic cleavages in vivo yield mature proteins. The precurssor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins (PubMed:32155444). Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor (By similarity). The presence of a furin polybasic cleavage site sets SARS-CoV-2 S apart from SARS-CoV S that possesses a monobasic S1/S2 cleavage site processed upon entry of target cells (PubMed:32155444).

Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface.


Homotrimer; each monomer consists of a S1 and a S2 subunit (PubMed:32155444, PubMed:32075877). The resulting peplomers protrude from the virus surface as spikes (By similarity).

Interacts with the accessory proteins 3a and 7a.

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