Recombinant Glycoprotein G (G), partial

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

Purity

>85% (SDS-PAGE)

Target Names

Uniprot NO.

Q9IH62

Species

Nipah virus

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

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.

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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

G and the fusion protein F are both crucial glycoproteins located on the surface of the virus envelope. [review] PMID:29963835
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
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
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
Cysteine cluster in the G protein is involved in stabilizing a unique microdomain critical for triggering fusion. PMID:22496210
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
the G protein appeared to be constitutively internalized with the bulk flow during membrane turnover PMID:15731282
sNiV-G binds to ephrinB3 with a 30-fold higher affinity than that of sHeV-G. PMID:17652392
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