ELISA with SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein 3218

SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein 3218

$300.00 – $1,000.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Arg319-Phe541(G339D, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, S477N, T478K, E484A, Q493R, Q498R, N501Y, Y505H)

available size

Clear

SKU: 3218parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	QHD43416
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	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.
molecular weight	The protein has a predicted MW of 25.92 kDa. Due to glycosylation, the protein migrates to 35-42 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein 3218

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
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 at ambient temperature.
Purity > 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
Mass 141178Da
Function FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis using host TFRC and GRM2 and leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306, PubMed:34903715, PubMed:36779763). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). 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 (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270). {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32075877, ECO:0000269\|PubMed:32142651, ECO:0000269\|PubMed:32155444, ECO:0000269\|PubMed:32221306, ECO:0000269\|PubMed:32817270, ECO:0000269\|PubMed:33082293, ECO:0000269\|PubMed:33082294, ECO:0000269\|PubMed:34903715, ECO:0000269\|PubMed:35150743, ECO:0000269\|PubMed:36779763, ECO:0000303\|PubMed:33082293, ECO:0000305\|PubMed:34561887}.; FUNCTION: [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 (PubMed:32142651) or during endocytosis by host CSTL (PubMed:32703818, PubMed:34159616). 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 (PubMed:34561887). 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. {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32703818, ECO:0000269\|PubMed:34159616, ECO:0000305\|PubMed:34561887}.; FUNCTION: [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 (PubMed:32703818, PubMed:34159616). 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 (PubMed:34561887). 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. {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32703818, ECO:0000269\|PubMed:34159616, ECO:0000305\|PubMed:34561887}.
Subellular location SUBCELLULAR LOCATION: Virion membrane {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32979942}; Single-pass type I membrane protein {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:34504087}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:34504087}; Single-pass type I membrane protein {ECO:0000255\|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:34504087}; Single-pass type I membrane protein {ECO:0000255\|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion (PubMed:34504087). An average of 26 +/-15 S trimers are found randomly distributed at the surface of the virion (PubMed:32979942). {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32979942, ECO:0000269\|PubMed:34504087}.
Structure SUBUNIT: [Spike glycoprotein]: Homotrimer; each monomer consists of a S1 and a S2 subunit (PubMed:32075877, PubMed:32155444, PubMed:32245784). The resulting peplomers protrude from the virus surface as spikes (PubMed:32979942). Interacts with ORF3a protein and ORF7a protein (By similarity) (PubMed:32075877, PubMed:32155444, PubMed:32245784, PubMed:32979942). There are an average of 26 +/-15 spike trimers at the surface of virion particles (PubMed:32979942). Binds to host MBL2 (PubMed:35102342). This binding occurs via glycans and inhibits viral infectivity. Inhibition is effective against alpha, beta, gamma, and delta variants (PubMed:35102342). Interacts with host TFRC; this interaction plays a role in virus internalization (PubMed:36779763). Interacts with host GRM2; this interaction plays a role in virus internalization (PubMed:34903715). {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32075877, ECO:0000269\|PubMed:32155444, ECO:0000269\|PubMed:32245784, ECO:0000269\|PubMed:32979942, ECO:0000269\|PubMed:34903715, ECO:0000269\|PubMed:35102342}.; SUBUNIT: [Spike protein S1]: Binds to host ACE2 (PubMed:32075877, PubMed:32132184, PubMed:32155444, PubMed:32221306, PubMed:32225175, PubMed:32225176, PubMed:33607086). RBD also interacts with the N-linked glycan on 'Asn-90' of ACE2 (PubMed:33607086). Cleavage of S generates a polybasic C-terminal sequence on S1 that binds to host Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors (PubMed:33082293, PubMed:33082294). Interacts with host integrin alpha-5/beta-1 (ITGA5:ITGB1) and with ACE2 in complex with integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:33102950). May interact via cytoplasmic c-terminus with M protein (PubMed:33229438). May interact (via N-terminus) with host bilirubin and biliverdin, thereby preventing antibody binding to the SARS-CoV-2 spike NTD via an allosteric mechanism (PubMed:33888467). May interact with host LRRC15, thereby allowing attachment to host cells (PubMed:36735681). {ECO:0000269\|PubMed:32075877, ECO:0000269\|PubMed:32132184, ECO:0000269\|PubMed:32155444, ECO:0000269\|PubMed:32221306, ECO:0000269\|PubMed:32225175, ECO:0000269\|PubMed:32225176, ECO:0000269\|PubMed:33082293, ECO:0000269\|PubMed:33082294, ECO:0000269\|PubMed:33102950, ECO:0000269\|PubMed:33229438, ECO:0000269\|PubMed:33607086, ECO:0000269\|PubMed:33888467, ECO:0000269\|PubMed:36735681}.
Post-translational modification PTM: The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs. {ECO:0000269\|PubMed:34599882}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32155444, PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835). {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32142651, ECO:0000269\|PubMed:32155444, ECO:0000269\|PubMed:32221306, ECO:0000269\|PubMed:32362314, ECO:0000269\|PubMed:32703818, ECO:0000269\|PubMed:33417835, ECO:0000269\|PubMed:33465165, ECO:0000269\|PubMed:34159616, ECO:0000305\|PubMed:34561887}.; PTM: Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32363391, PubMed:32366695, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138). {ECO:0000269\|PubMed:32075877, ECO:0000269\|PubMed:32155444, ECO:0000269\|PubMed:32363391, ECO:0000269\|PubMed:32366695, ECO:0000269\|PubMed:32929138}.; PTM: O-glycosylated by host GALNT1 at the end of S1. This could reduce the efficiency of S1/S2 cleavage. {ECO:0000269\|PubMed:34732583}.
Domain DOMAIN: Contains sequence and structural motifs very similar to those of a bacterial superantigen and can directly bind and activate T-cell receptors. Activation of a broad T-cell repertoire may be involved in the hyperinflammatory syndrome in acute COVID disease. {ECO:0000303\|PubMed:32989130}.; DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds COPI in vitro. {ECO:0000250\|UniProtKB:P59594}.; DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function cooperatively and have a membrane-ordering effect on lipid headgroups and shallow hydrophobic regions of target bilayers. They are considered as two domains of an extended, bipartite FP. The membrane-ordering activity is calcium-dependent and also dependent on correct folding, which is maintained by an internal disulfide bond in FP2. {ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000305\|PubMed:34561887}.
Biotechnology BIOTECHNOLOGY: Main component of the anti-COVID19 vaccines BNT162b2/Pfizer-Biontech and mRNA-1273/Moderna; in which the mutations of Lys-986 (K986P) and Val-987 (V987P) have been added to stabilize the protein in the prefusion state. {ECO:0000305\|PubMed:34322129}.; BIOTECHNOLOGY: Main component of the anti-COVID19 vaccine Ad26.COV2.S/Janssen Pharmaceutical; in which the mutations Arg-682 (R682S), Arg-685 (R685G), Lys-986 (K986P) and Val-987 (V987P) have been added to stabilize the protein in the prefusion state. {ECO:0000305\|PubMed:34322129}.; BIOTECHNOLOGY: Main component of the anti-COVID vaccine Chadox1/AZD1222/AstraZeneca; in which the human tPA leader sequence is added in N-terminus to enhance protein secretion. {ECO:0000305\|PubMed:34322129}.
Target Relevance information above includes information from UniProt accession: P0DTC2
The UniProt Consortium

Data

ELISA with SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein

Immobilized SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1), His Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Human ACE2, hFc Tag with the EC50 of 6.9ng/ml determined by ELISA.

HPLC of SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein

The purity of SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) Protein

SARS-Cov-2 Spike RBD (Omicron BA.2/BA.2.2.1) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

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.