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Biotinylated SARS Spike S1 Protein 4691



  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Ser14-Arg667
SKU: 4691parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-hFc-Avi, also biotinylated

Biotinylated SARS Spike S1 Protein 4691

Size and concentration
100, 500µg and liquid
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped with dry ice.
> 95% as determined by Tris-Bis PAGE
target relevance
The spike protein (S) of coronavirus (CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
Protein names
Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
Gene names
S,S 2
Protein family
Betacoronaviruses spike protein family
FUNCTION: [Spike glycoprotein]: May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity. {ECO:0000269|PubMed:31199522}.; FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membrane fusion within endosomes. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15496474}.; FUNCTION: [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. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:19321428}.
Subellular location
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Colocalizes with S in the host endoplasmic reticulum-Golgi intermediate compartment (PubMed:20861307). Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}.
SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes (By similarity). Binds to human and palm civet ACE2 and human CLEC4M/DC-SIGNR. Interacts with the accessory proteins 3a and 7a. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15194747, ECO:0000269|PubMed:15496474, ECO:0000269|PubMed:16166518, ECO:0000269|PubMed:16840309}.
Post-translational modification
PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested by cathepsin CTSL within endosomes. {ECO:0000269|PubMed:17134730}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.; PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-Rule:MF_04099}.
Target Relevance information above includes information from UniProt accession : P59594
The UniProt Consortium


HPLC of Biotinylated SARS Spike S1 Protein
The purity of Biotinylated SARS spike S1 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated SARS Spike S1 Protein
Biotinylated SARS spike S1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



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