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AB235851

Recombinant Spike glycoprotein (His tag)

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Recombinant Spike glycoprotein (His tag) is a Bovine coronavirus Mebus Fragment protein, in the 326 to 540 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

3, S, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

3 Images
Mass Spectrometry - Recombinant Spike glycoprotein (His tag) (AB235851)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Spike glycoprotein (His tag) (AB235851)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab235851 could indicate that this peptide derived from E.coli-expressed Bovine coronavirus (strain Mebus) Spike glycoprotein.

Mass Spectrometry - Recombinant Spike glycoprotein (His tag) (AB235851)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Spike glycoprotein (His tag) (AB235851)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab235851 could indicate that this peptide derived from E.coli-expressed Bovine coronavirus (strain Mebus) Spike glycoprotein.

SDS-PAGE - Recombinant Spike glycoprotein (His tag) (AB235851)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Spike glycoprotein (His tag) (AB235851)

ab235851 analyzed by (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P15777

Animal free

No

Carrier free

No

Species

Bovine coronavirus Mebus

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"PNLPDCNIEAWLNDKSVPSPLNWERKTFSNCNFNMSSLMSFIQADSFTCNNIDAAKIYGMCFSSITIDKFAIPNGRKVDLQLGNLGYLQSFNYRIDTTATSCQLYYNLPAANVSVSRFNPSTWNRRFGFTEQFVFKPQPVGVFTHHDVVYAQHCFKAPSNFCPCKLDGSLCVGNGPGIDAGYKNSGIGTCPAGTNYLTCHNAAQCNCLCTPDPIT","proteinLength":"Fragment","predictedMolecularWeight":"27.2 kDa","actualMolecularWeight":null,"aminoAcidEnd":540,"aminoAcidStart":326,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P15777","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Spike glycoprotein also known as S protein or surface glycoprotein plays an important role in the mechanism of viral entry into host cells. This protein is important for mediating the fusion of the viral envelope with the host cell membrane facilitating viral entry. It is a trimeric glycoprotein typically expressed on the surface of coronaviruses including SARS-CoV-2 and has a mass of approximately 180 kDa. Each monomer within the trimer structure contains S1 and S2 subunits that are important for host cell attachment and membrane fusion respectively.
Biological function summary

This glycoprotein facilitates the attachment of the virus to host cells by binding to specific receptors. The Spike glycoprotein engages with the angiotensin-converting enzyme 2 (ACE2) receptor a step essential for viral entry and infection. It is part of a complex process that involves changes in the conformation of the protein to expose fusion peptides that drive membrane fusion. The structure allows the virus to effectively latch onto the surface of host cells initiating invasion and replication cycles.

Pathways

The Spike glycoprotein functions in the viral entry pathway a critical mechanism for viral infection. This pathway involves other proteins such as the TMPRSS2 enzyme which aids in the priming of the Spike protein for effective entry. The process of cell entry also associates the glycoprotein with endocytosis where it collaborates with clathrin-mediated pathways for successful internalization. These pathways are integral for the virus’s life cycle and replication within host cells.

The Spike glycoprotein is closely linked with COVID-19 the disease caused by SARS-CoV-2. The interaction between the Spike protein and ACE2 is significant in understanding the viral pathology and the severity of infections. Additionally mutations in the Spike protein can affect transmissibility and immune evasion influencing vaccine efficacy. The glycoprotein’s role in facilitating virus-host interactions implicates its importance in potential treatment strategies targeting viral entry.

Specifications

Form

Liquid

General info

Function

Spike protein S1. Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.. 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.

Sequence similarities

Belongs to the betacoronaviruses spike protein family.

Post-translational modifications

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.. The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.

Product protocols

Target data

Spike protein S1. Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.. 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.
See full target information S

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