Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Uniprot No.

P17465

Research Area

Others

Alternative Names

Outer capsid protein VP4; Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]

Species

Rotavirus A (strain RVA/Cow/United States/NCDV-Lincoln/1969/G6P6[1]) (RV-A) (Rotavirus A (strain Nebraska calf diarrhea virus))

Source

E.coli

Expression Region

248-480aa

Target Protein Sequence

AQPNQDIVVSKTSLWKEMQYNRDIVIRFKFANSIIKSGGLGYKWSEVSFKPANYQYTYTRDGEEVTAHTTCSVNGINDFNYNGGSLPTDFVISKYEVIKENSFVYIDYWDDSQAFRNMVNVRSLAADLNSVMCTGGDYSFALPVGNYPVMTGGAVSLHSAGVTLSTQFTDFVSLNSLRFRFRLSVEEPPFSILRTRVSGLYGLPAARPNNSQEYYEIAGRFSLISLVPSNDDY
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

33.2 kDa

Protein Length

Partial

Tag Info

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

Producing recombinant Rotavirus A Outer capsid protein VP4 in E. coli involves co-cloning the gene encoding the partial Rotavirus A VP4 protein (248-480aa) into an expression vector, followed by transformation into E. coli cells. These cells are cultured under conditions that induce protein expression. After sufficient growth is achieved, the cells are lysed to release the recombinant VP4 protein. Purification is achieved using affinity chromatography techniques. The purity of the Rotavirus A Outer capsid protein VP4 is confirmed using SDS-PAGE, exceeding 85%.

Rotavirus A outer capsid protein VP4 is crucial in the infectivity of rotavirus particles. Upon activation for cell entry, VP4 undergoes trypsin cleavage into hemagglutinin and a membrane penetration protein, which are essential for the virus to enter host cells [1]. The VP4 protein also exhibits hemagglutinin activity, contributing to its role in viral attachment and entry [2]. Furthermore, VP4 is a major protective antigen, although there is still limited understanding of the antigenic relationships of VP4 among different human rotavirus strains [3].

References:
[1] P. Dormitzer, H. Greenberg, & S. Harrison, Proteolysis of monomeric recombinant rotavirus vp4 yields an oligomeric vp5* core, Journal of Virology, vol. 75, no. 16, p. 7339-7350, 2001. https://doi.org/10.1128/jvi.75.16.7339-7350.2001
[2] M. Yeager, K. Dryden, N. Olson, H. Greenberg, & T. Baker, Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction., The Journal of Cell Biology, vol. 110, no. 6, p. 2133-2144, 1990. https://doi.org/10.1083/jcb.110.6.2133
[3] M. Gorziglia, G. Larralde, A. Kapikian, & R. Chanock, Antigenic relationships among human rotaviruses as determined by outer capsid protein vp4., Proceedings of the National Academy of Sciences, vol. 87, no. 18, p. 7155-7159, 1990. https://doi.org/10.1073/pnas.87.18.7155

Target Background

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 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 Ca(2+) 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.; 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.; 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 (HBGAs) for viral entry.

Subcellular Location

[Outer capsid protein VP4]: Virion. Host rough endoplasmic reticulum. Host cell membrane. Host cytoplasm, host cytoskeleton. Host endoplasmic reticulum-Golgi intermediate compartment.; [Outer capsid protein VP8*]: Virion.; [Outer capsid protein VP5*]: Virion.

Protein Families

Rotavirus VP4 family

Code	CSB-EP325504RIV
Abbreviation	Recombinant Rotavirus A Outer capsid protein VP4 protein, partial
MSDS	MSDS Datasheet
Size	$388
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Rotavirus A Outer capsid protein VP4, partial

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