SARS-CoV-2 Spike Neutralizing Antibody

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SARS-CoV-2 Spike Neutralizing Antibody

Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Information Descriptio





Alternative Names

coronavirus s1,coronavirus s2,coronavirus spike,cov spike,ncov RBD,ncov s1,ncov s2,ncov spike,novel coronavirus RBD,novel coronavirus s1,novel coronavirus s2,novel coronavirus spike,RBD,S1,s2,Spike RBD




Recombinant 2019-nCoV S1 Protein (mFc Tag)(RPES0046)


Neutralization, ELISA

Recommended dilution

ELISA: 1:1,000-1:2,000


1 mg/mL

Clone No.






Storage instructions

Store at -20℃. Avoid freeze / thaw cycles

Storage buffer

0.2 μm filtered solution in PBS

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.