Recombinant Avian infectious bursal disease virus Structural polyprotein, partial

• Product Name Alternative:

  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]

• Abbreviation:

  Recombinant Avian infectious bursal disease virus Structural polyprotein, partial

• UniProt:

  P15480

• Expression Region:

  723-1012aa

• Organism:

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

• Target Sequence:

  RFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRALPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE

• Tag:

  N-terminal 6xHis-tagged

• Type:

  Developed Protein

• Source:

  E.coli

• Field of Research:

  Others

• 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..

• Endotoxin:

  Not test

• Purity:

  Greater than 90% as determined by SDS-PAGE.

• Activity:

  Not Test

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

• 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) .

• Molecular Weight:

  36.8 kDa

• References & Citations:

  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)

• Storage Conditions:

  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.

• Protein Length:

  Partial