| Sequence | KNLNESLIDLQELGK |
|---|---|
| Purity | >90% (HPLC-MS) |
Application
| Cellular immune response, T-cell expansion, Antigen specific T-cell stimulation, Immune monitoring, T-cell assays |
| Primary Accession | P0DTC2 |
| Other Accession | AAP41037.1 |
| Gene ID | 4374056 |
|---|---|
| Other Names | SARS-CoV-2 Spike Glycoprotein , E2 , Peplomer |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | S {ECO:0000255|HAMAP-Rule:MF_04099} |
|---|---|
| Function | Spike glycoprotein is cleaved into S1, S2, and S3 chains. Spike protein S1 attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein. Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry . Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.Spike protein S2 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. Spike protein S2' acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. |
| Cellular Location | Virion membrane, host endoplasmic reticulum-Golgi intermediate compartment membrane |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@biotrend.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
SARS-CoV-2 is part of the Coronaviridae family, whose members are named after their crown-like appearance under the electron microscope caused by the surface glycoproteins that decorate the virus. Coronaviruses have a large (30+ kb) single-stranded positivesense RNA genome encoding for several open reading frames. One frame encodes the spike protein (S protein), a class I fusion protein that mediates attachment of the virus to cell surface receptors followed by uptake into endosomes (for most coronaviruses). Proteolytic cleavage of the S protein and fusion of viral and endosomal membranes trigger release of viral RNA into the cytosol. We know now from studies on SARS-CoV-1 and the related MERS-CoV vaccines that the S protein on the surface of the virus is an ideal target for a vaccine. In SARS-CoV-1 and SARS-CoV-2, this protein interacts with the receptor ACE2, and antibodies targeting the spike can interfere with this binding, thereby neutralizing the virus. The structure of the S protein of SARS-CoV-2 was solved in record time at high resolution, contributing to our understanding of this vaccine target. More than 90 vaccines are being developed against SARS-CoV-2 by research teams in companies and universities across the world.