Recombinant Nipah virus Glycoprotein G(G)

Code CSB-CF862323NDT
Size US$3865Purchase it in Cusabio online store
(only available for customers from the US)
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names G
Uniprot No. Q9IH62
Research Area others
Alternative Names GGlycoprotein G
Species Nipah virus
Source in vitro E.coli expression system
Expression Region 1-602aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 72.0kDa
Protein Length Full Length
Tag Info N-terminal 10xHis-tagged and C-terminal Myc-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.
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.

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Target Data

Function Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.
Gene References into Functions
  1. G and the fusion protein F are both crucial glycoproteins located on the surface of the virus envelope. [review] PMID: 29963835
  2. the binding of the viral attachment protein G to its host receptor ephrinB2 was studied and showed monomeric and dimeric receptors activate distinct conformational changes in G. PMID: 28974687
  3. Data suggest that fusion of Nipah viruses with host cells is facilitated by two of viral membrane proteins, the G protein and the F protein; G head domain binds to human ephrins B2 and B3 altering conformational density of entire G head domain. PMID: 24615845
  4. Authors identified a G stalk C-terminal region (amino acids 159 to 163) that is important for multiple G functions, including G tetramerization, conformational integrity, G-F interactions, receptor-induced conformational changes in G, and F triggering. PMID: 25428863
  5. Cysteine cluster in the G protein is involved in stabilizing a unique microdomain critical for triggering fusion. PMID: 22496210
  6. Results indicated that the G-H loop of ephrin-B2 was indeed critical for the interaction between ephrin-B2 and Nipah virus-G. PMID: 21632558
  7. the G protein appeared to be constitutively internalized with the bulk flow during membrane turnover PMID: 15731282
  8. sNiV-G binds to ephrinB3 with a 30-fold higher affinity than that of sHeV-G. PMID: 17652392
  9. report the crystal structures of the NiV-G both in its receptor-unbound state and in complex with ephrin-B3, providing, to our knowledge, the first view of a paramyxovirus attachment complex in which a cellular protein is used as the virus receptor PMID: 18632560

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Subcellular Location Virion membrane, Single-pass type II membrane protein, Host cell membrane, Single-pass type II membrane protein
Protein Families Paramyxoviruses hemagglutinin-neuraminidase family
Database Links

KEGG: vg:920955

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  Email: [email protected]
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