Recombinant Rotavirus A Outer capsid protein VP4, partial | CSB-EP339583RFU

Recombinant Rotavirus A Outer capsid protein VP4, partial | CSB-EP339583RFU | Cusabio

Alternative Name(s): Hemagglutinin

Gene Names: N/A

Research Areas: Others

Organism: Rotavirus A (isolate RVA/Cow/United States/B223/1983/G10P8[11 ]) (RV-A)

AA Sequence: ARPNEDIIISKASLWKEVQYNRDIVIRFVFANNIIKAGGLGYKWSEISYKANNYQYTYMRDGVEVVAHTTVSVNGVSVYNYNTGPLPTDFMIRNYDVLKESSFVYVDYWDDSQAFRNMVYVRSLNAELNQVRCEGGHYSFALPVGSWPVMQGGSVILTFDGVTLSTQFTDYVSLNSLRFRFRCAVSEPSFRVTGTRISNLYGLPAANPMGDQQYYEAAGRFSLILLVPSNDDY

Source: E.coli

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

Expression Region: 247-479aa

Sequence Info: Partial

MW: 31.5 kDa

Purity: Greater than 85% as determined by SDS-PAGE.

Relevance: 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 entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1

Reference: "Amino acid sequence analysis of bovine rotavirus B223 reveals a unique outer capsid protein VP4 and confirms a third bovine VP4 type." Hardy M.E., Gorziglia M., Woode G.N. Virology 191:291-300(1992)

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.

Function: 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 entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity).

Involvement in disease:

Subcellular Location: Outer capsid protein VP4: Virion, Host rough endoplasmic reticulum, Note=Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7, these enveloped particles also contain VP4, As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles (By similarity), SUBCELLULAR LOCATION: Outer capsid protein VP8*: Virion, Note=Outer capsid protein, SUBCELLULAR LOCATION: Outer capsid protein VP5*: Virion

Protein Families: Rotavirus VP4 family

Tissue Specificity:

Paythway:

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: P35746

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