DENV2 Envelope Protein (HEK293, His)
Based on 1 publication(s) in Google Scholar
NS1 Protein, essential in virus budding, binds the cell membrane, forming a nucleocapsid that becomes the virus core. During entry, NS1 facilitates viral genome penetration post-hemifusion. NS1 migrates to the nucleus, influencing host functions, and counteracts host EXOC1's antiviral effects by sequestering and degrading EXOC1 via the proteasome pathway. Additionally, NS1 impedes RNA silencing by interfering with the host Dicer enzyme. DENV2 Envelope Protein (HEK293, His) is the recombinant DENV2 Envelope protein, expressed by HEK293, with N-His labeled tag.
- Species: Virus
- Source: HEK293
-
Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
NS1 Protein, essential in virus budding, binds the cell membrane, forming a nucleocapsid that becomes the virus core. During entry, NS1 facilitates viral genome penetration post-hemifusion. NS1 migrates to the nucleus, influencing host functions, and counteracts host EXOC1's antiviral effects by sequestering and degrading EXOC1 via the proteasome pathway. Additionally, NS1 impedes RNA silencing by interfering with the host Dicer enzyme. DENV2 Envelope Protein (HEK293, His) is the recombinant DENV2 Envelope protein, expressed by HEK293, with N-His labeled tag.
The NS1 protein plays a vital role in virus budding, as it binds to the cell membrane and assembles the viral RNA into a nucleocapsid, which becomes the core of a fully developed virus particle. In the process of virus entry, NS1 may facilitate the penetration of the viral genome into the host cytoplasm following hemifusion triggered by surface proteins. NS1 has the ability to migrate to the cell nucleus, where it exerts its influence on host functions. It can counteract the antiviral effects of host EXOC1 by sequestering and degrading EXOC1 through the proteasome degradation pathway. Furthermore, NS1 hinders RNA silencing by interfering with the host Dicer enzyme.
Publications (1)
-
Journal Impact Factor
-
Most Recent
-
J Immunol Methods
Development of a sensitive sandwich ELISA for the envelope domain III protein of dengue virus type 2. [Abstract]2025 Dec:545:114000. PMID: 41183705
Technical Parameters
-
Species Virus
-
Source HEK293
-
Tag N-His
-
Accession
P29990 (M281-S677)
-
Gene ID/
-
Molecular Construction
-
N-term
-
DENV2 (M281-S677)
Accession # P29990 -
C-term
-
-
Protein Length
Partial
-
Synonyms
Genome polyprotein; Protein prM; Peptide pr; Small envelope protein M; Matrix protein; Envelope protein E; Envelope Protein/E Protein (DENV); LGenome polyprotein; L
-
AA Sequence
MRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFRCKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSS
-
Predicted Molecular Mass
46.2 kDa
-
Molecular Weight
Approximately 55-60 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
-
Glycosylation
Yes
-
Structure/Form
Monomer
-
Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)