Recombinant Rotavirus A Intermediate capsid protein VP6

CAT:
399-CSB-EP321618RGK-01
Size:
20 µg
  • Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
  • Dry Ice Shipment: No
Recombinant Rotavirus A Intermediate capsid protein VP6 - image 1

Recombinant Rotavirus A Intermediate capsid protein VP6

  • Product Name Alternative:

    Intermediate capsid protein VP6
  • Abbreviation:

    Recombinant Rotavirus A Intermediate capsid protein VP6 protein
  • UniProt:

    P04509
  • Expression Region:

    1-397aa
  • Organism:

    Rotavirus A (strain Cow/France/RF/1975 G6-P6[1]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A)
  • Target Sequence:

    MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLIKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVITSADGATTWYFNPVILRPNNVEIEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATVGLTLRIESAVCESVLADASETMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK
  • Tag:

    N-terminal 6xHis-tagged
  • Type:

    In Stock Protein
  • Source:

    E.coli
  • Field of Research:

    Others
  • Relevance:

    Intermediate capsid protein that self assbles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid rain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP.
  • 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:

    Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP.
  • Molecular Weight:

    48.8 kDa
  • References & Citations:

    A zinc ion controls assembly and stability of the major capsid protein of rotavirus.Erk I., Huet J.-C., Duarte M., Duquerroy S., Rey F.A., Cohen J., Lepault J.J. Virol. 77:3595-3601 (2003)
  • 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:

    Full Length