| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Spike glycoprotein (S) (A67V; ?69-70; T95I; G142D; ?143-145; ?211; L212I; ins214-215EPE; G339D; S371L; S373P; S375F; K417N; N440K; G446S; S477N; T478K; E484A; Q493R; G496S; Q498R; N501Y; Y505H; T547K; D614G; H655Y; N679K; P681H); partial; (S glycoprotein)(E2)(Peplomer protein) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Reconstitution | |
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| Target | |
| UniProt # |
Overview
Recombinant Severe acute respiratory syndrome coronavirus 2 Spike glycoprotein (S) (A67V,?69-70,T95I,G142D,?143-145,?211,L212I,ins214-215EPE,G339D,S371L,S373P,S375F,K417N,N440K,G446S,S477N,T478K,E484A,Q493R,G496S,Q498R,N501Y,Y505H,T547K,D614G,H655Y,N679K,P681H), partial is a recombinant protein reagent derived from Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) and produced in E.coli. It is commonly used to support Cancer research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 16-685aa(A67V,?69-70,T95I,G142D,?143-145,?211,L212I,ins214-215EPE,G339D,S371L,S373P,S375F,K417N,N440K,G446S,S477N,T478K,E484A,Q493R,G496S,Q498R,N501Y,Y505H,T547K,D614G,H655Y,N679K,P681H). Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
- Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
- Tag / fusion: N-terminal 6xHis-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 81.0 kDa. Apparent size may vary with tags, processing, and gel conditions.
When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.
Biological background
The gene commonly associated with this target is S. SARS2-S-ins214EPE_K417N_N501Y-P refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.
Research relevance and current trends
- Mapping pathway dependencies and signaling networks that drive tumor growth and drug resistance.
- Developing and benchmarking biomarker assays (e.g., immunoassays or binding reagents) for candidate targets.
- Characterizing protein variants, domains, or interaction partners relevant to targeted therapeutics and precision oncology.
Relevance: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 . When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane . When S2/s2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis leading to fusion of the virion membrane with the host endosomal membrane . Alternatively, may use NRP1/NRP2 and integrin as entry receptors . The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels . The stalk domain of S contains three hinges, giving the head unexpected orientational freedom . [Spike protein S2]: Precursor of the fusion protein processed in the biosynthesis of the S protein and the formation of virus particle. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains two viral fusion peptides that are unmasked after cleavage. The S2/S2' cleavage occurs during virus entry at the cell membrane by host TMPRSS2 or during endocytosis by host CSTL . In either case, this triggers an extensive and irreversible conformational change leading to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm . 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 fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes. [Spike protein S2']: Subunit of the fusion protein that is processed upon entry into the host cell. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains a viral fusion peptide that is unmasked after S2 cleavage. This cleavage can occur at the cell membrane by host TMPRSS2 or during endocytosis by host CSTL . In either case, this triggers an extensive and irreversible conformational change that leads to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm . 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 fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes.
Common research applications
- Assay and standard development for immunoassays or binding-based detection methods.
- Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
- Structure–function analysis, including domain mapping or evaluation of sequence variants.
In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.
Notes for experimental interpretation
- Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
- Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
- Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
- E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.
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