Recombinant Rotavirus A Outer capsid protein VP4, partial | CSB-EP319263ROJ

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13 - 23 Working Days
€352.00 - €1,702.00


Recombinant Rotavirus A Outer capsid protein VP4, partial | CSB-EP319263ROJ | Cusabio

Alternative Name(s): Hemagglutinin

Gene Names: N/A

Research Areas: Others

Organism: Rotavirus A (strain RVA/Human/United States/DS-1/1976/G2P1B[4]) (RV-A) (Rotavirus A (strain DS1))


Source: E.coli

Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged

Expression Region: 247-479aa

Sequence Info: Partial

MW: 31.4 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Relevance: Outer capsid protein VP4: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts.Outer capsid protein VP5*: Forms the spike "foot" and "body" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.Outer capsid protein VP8*: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo-blood group antigens for viral entry.

Reference: "Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin." Ciarlet M., Ludert J.E., Iturriza-Gomara M., Liprandi F., Gray J.J., Desselberger U., Estes M.K. J. Virol. 76:4087-4095(2002)

Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.


Involvement in disease:

Subcellular Location:

Protein Families:

Tissue Specificity:


Form: Liquid or Lyophilized powder

Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Uniprot ID: P11196

HGNC Database Link: N/A

UniGene Database Link: N/A

KEGG Database Link: N/A

STRING Database Link: N/A

OMIM Database Link: N/A

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