Immobilized Nipah Virus Glycoprotein G Protein, His Tag at 5 μg/mL (100 μL/well) can bind Human Ephrin-B2 / EFNB2 Protein, Fc tag (MALS verified) with EC50 of 7.4-9.6 ng/ml.
Nipah Virus Glycoprotein G His Tag Protein
Nipah Virus Glycoprotein G His Tag Protein
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Product Details
Product Details
Product Specification
| Synonyms | Glycoprotein G |
| Accession | Q9IH62 |
| Amino Acid Sequence | Protein sequence (Q9IH62, Gln71-Thr602, with N-His Tag) QNYTRSTDNQAVIKDALQGIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINENVNEKCKFTLPPLKIHECNISCPNPLPFREYRPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLERIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYHCSAVYNNEFYYVLCAVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDGENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPLVVNWRNNTVISRPGQSQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEILYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT |
| Expression System | HEK293 |
| Molecular Weight | Predicted MW: 61 kDaObserved MW: 70-90 kDa |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <1EU/μg |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized powder |
| Storage Buffer | Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4 with 3% trehalose. |
| Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. |
Background
The Nipah virus Glycoprotein G (NiV-G) is a surface attachment protein essential for viral entry. It forms tetramers that recognize and bind to cellular receptors ephrin-B2 and ephrin-B3, which are highly conserved in mammals. Following receptor binding, the fusion protein (F) is triggered to mediate membrane fusion. NiV-G is a primary target for neutralizing antibodies, making it a key component of vaccine and antiviral research. Due to Nipah virus's high pathogenicity and biosafety level 4 classification, studies of G protein structure and function are critical for developing countermeasures against this deadly paramyxovirus.
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Bioactivity
SDS-PAGE
2μg（R: reducing conditions）
