Outer capsid protein VP4, partial, Rotavirus X, recombinant

Organism: Rotavirus X (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)). Source: E.coli. Expression Region: 1-249aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: MSLRSLLITT EAVGETTQTS DHQTSFSTRT YNEINDRPSL RVEKDGEKAY CFKNLDPVRY DTRMGEYPFD YGGQSTENNQ LQFDLFTKDL MADTDIGLSD DVRDDLKRQI KEYYQQGYRA IFLIRPQNQE QQYIASYSST NLNFTSQLSV GVNLSVLNKI QENKLHIYST QPHIPSVGCE MITKIFRTDV DNENSLINYS VPVTVTISVT KATFEDTFVW NQNNDYPNMN YKDLIPAVTK NSIYHDVKR. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. 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. 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 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Outer capsid protein VP4: 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 Ca2+ 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.Outer capsid protein VP5*: 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.Outer capsid protein VP8*: 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. Reference: "Whole genomic characterization of a human rotavirus strain B219 belonging to a novel group of the genus Rotavirus." Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K., Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H. J. Med. Virol. 80:2023-2033(2008). Function: nan