Recombinant Sindbis virus Structural polyprotein,partial

Code CSB-CF361018SHZb2
Size US$3606
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 85% as determined by SDS-PAGE.
Uniprot No. P03316
Research Area others
Alternative Names Structural polyprotein; p130) [Cleaved into: Capsid protein; EC 3.4.21.90; Coat protein; C); Precursor of protein E3/E2; p62; pE2); Assembly protein E3; Spike glycoprotein E2; E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1; E1 envelope glycoprotein)]
Species Sindbis virus (SINV)
Source in vitro E.coli expression system
Expression Region 807-1245aa
Target Protein Sequence YEHATTVPNVPQIPYKALVERAGYAPLNLEITVMSSEVLPSTNQEYITCKFTTVVPSPKIKCCGSLECQPAAHADYTCKVFGGVYPFMWGGAQCFCDSENSQMSEAYVELSADCASDHAQAIKVHTAAMKVGLRIVYGNTTSFLDVYVNGVTPGTSKDLKVIAGPISASFTPFDHKVVIHRGLVYNYDFPEYGAMKPGAFGDIQATSLTSKDLIASTDIRLLKPSAKNVHVPYTQASSGFEMWKNNSGRPLQETAPFGCKIAVNPLRAVDCSYGNIPISIDIPNAAFIRTSDAPLVSTVKCEVSECTYSADFGGMATLQYVSDREGQCPVHSHSSTATLQESTVHVLEKGAVTVHFSTASPQANFIVSLCGKKTTCNAECKPPADHIVSTPHKNDQEFQAAISKTSWSWLFALFGGASSLLIIGLMIFACSMMLTSTRR
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 65.9kDa
Protein Length Partial
Tag Info N-terminal 10xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
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.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life 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.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Capsid protein
Gene References into Functions
  1. The authors conclude that H230 of E1 protein is essential for the assembly of complete infectious Sindbis virus virions and that the presence of an amino acid at E2 position 209 is required for complete budding of Sindbis virus particles although several different amino acids can be at this location without affecting the titer. PMID: 27412592
  2. Mutating conserved cysteines in the e2 glycoprotein causes virus-specific assembly defects. PMID: 22238319
  3. Interactions of the cytoplasmic domain of E2 with nucleocapsid cores promote alphavirus budding. PMID: 22190727
  4. analysis of molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus PMID: 22001018
  5. Interaction of E2 glycoprotein with heparan sulfate is crucial for cellular infection of Sindbis virus PMID: 20300181
  6. Xray structure of spike, representing an intermediate in fusion process and clarifying maturation process; trimer of E2-E1 is similar to spikes in the neutral pH virus; amino- and carboxy-terminal domains of E2 form immunoglobulin-like folds PMID: 21124457
  7. specific amino acids within the region comprising amino acids 81 to 113 responsible for the encapsidation of the genomic RNA have been identified. PMID: 18305029
  8. The data indicate that the role of the cysteine residues in E3 is not primarily structural: it is hypothesized that E3 has an enzymatic or functional role in virus assembly, and these possibilities are further discussed. PMID: 19109378

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Subcellular Location Capsid protein: Virion, Host cytoplasm, Host cell membrane, SUBCELLULAR LOCATION: Precursor of protein E2: Virion membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein, SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein, SUBCELLULAR LOCATION: Protein 6K: Host cell membrane, Multi-pass membrane protein, Virion membrane, Multi-pass membrane protein, SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein
Protein Families Alphavirus structural polyprotein family
Database Links

KEGG: vg:1502155

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