Recombinant Nipah virus Glycoprotein G(G)-VLPs

Code CSB-MP862323NDT
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Product Details

Target Names G
Uniprot No. Q9IH62
Research Area Others
Alternative Names G; Glycoprotein G
Species Nipah virus
Source Mammalian cell
Expression Region 1-602aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info C-terminal 10xHis-tagged
If you have specified tag type, please tell us and we will check if it’s possible to develop.
Form Lyophilized powder
Note: We will default ship it in lyophilized form with normal bule ice packs. However, if you request to ship in liquid form, it needs to be shipped with dry ice, please communicate with us in advance and extra fees for dry ice and dry ice box will be charged.
Buffer Lyophilized from PBS, 6% Trehalose, pH 7.4
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°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.
Note: 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 the protein at -20°C/-80°C upon receiving it, and ensure to avoid repeated freezing and thawing, otherwise, it will affect the protein activity.
Datasheet & COA Please contact us to get it.

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Target Background

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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