Structural polyprotein, partial, Sindbis virus, recombinant

Organism: Sindbis virus (SINV). Source: in vitro E.coli expression system. Expression Region: 807-1245aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-SUMO-tagged. Target Protein Sequence: YEHATTVPNV PQIPYKALVE RAGYAPLNLE ITVMSSEVLP STNQEYITCK FTTVVPSPKI KCCGSLECQP AAHADYTCKV FGGVYPFMWG GAQCFCDSEN SQMSEAYVEL SADCASDHAQ AIKVHTAAMK VGLRIVYGNT TSFLDVYVNG VTPGTSKDLK VIAGPISASF TPFDHKVVIH RGLVYNYDFP EYGAMKPGAF GDIQATSLTS KDLIASTDIR LLKPSAKNVH VPYTQASSGF EMWKNNSGRP LQETAPFGCK IAVNPLRAVD CSYGNIPISI DIPNAAFIRT SDAPLVSTVK CEVSECTYSA DFGGMATLQY VSDREGQCPV HSHSSTATLQ ESTVHVLEKG AVTVHFSTAS PQANFIVSLC GKKTTCNAEC KPPADHIVST PHKNDQEFQA AISKTSWSWL FALFGGASSL LIIGLMIFAC SMMLTSTRR. 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: Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Reference: "Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins." Rice C.M., Strauss J.H. Proc. Natl. Acad. Sci. U.S.A. 78:2062-2066(1981). Function: Capsid protein