Alternative Name(s):

Structural polyprotein; PP) [Cleaved into: Precursor of VP2; Pre-VP2); Capsid protein VP2; Structural peptide 1; p1; pep46); Structural peptide 2; p2; pep7a); Structural peptide 3; p3; pep7b); Structural peptide 4; p4; pep11); Protease VP4; EC 3.4.21.-; Non-structural protein VP4; NS); Capsid protein VP3]

Species: (Organism)

Avian infectious bursal disease virus (strain Cu-1) (IBDV) (Gumboro disease virus)

Gene Names:

N/A

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

RFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRALPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE

Expression Region:

723-1012aa

Subcellular Location:

Capsid protein VP2: Virion, Host cytoplasm, SUBCELLULAR LOCATION: Capsid protein VP3: Virion, Host cytoplasm, SUBCELLULAR LOCATION: Structural peptide 1: Virion, Host cytoplasm, SUBCELLULAR LOCATION: Structural peptide 2: Virion, Host cytoplasm, SUBCELLULAR LOCATION: Structural peptide 3: Virion, Host cytoplasm, SUBCELLULAR LOCATION: Structural peptide 4: Virion, Host cytoplasm

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

36.8 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

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.

Research Areas:

Others

Function:

Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity).

Involvement in disease:

Relevance:

Capsid protein VP2 self assbles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 .The precursor of VP2 plays an important role in capsid assbly. First, pre-VP2 and VP2 oligomers assble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures .Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation..

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.

Protein Families:

Reference:

The birnavirus crystal structure reveals structural relationships among icosahedral viruses.Coulibaly F., Chevalier C., Gutsche I., Pous J., Navaza J., Bressanelli S., Delmas B., Rey F.A.Cell 120:761-772(2005)