Large envelope Protein, HBV-C (P.pastoris, 180a.a, His)
The large envelope protein is crucial in its two conformations, "outside" (Le-HBsAg) and "inside" (Li-HBsAg). Externally, it binds the virus to cellular receptors, initiates infection, determines species specificity, and promotes viral particle internalization via caveolin-mediated endocytosis. Large envelope Protein, HBV-C (P.pastoris, 180a.a, His) is the recombinant Virus-derived Large envelope protein, expressed by P. pastoris , with N-6*His labeled tag.
- Species: Virus
- Source: P. pastoris
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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.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- Help & FAQs
Biological Activity
Description
The large envelope protein is crucial in its two conformations, "outside" (Le-HBsAg) and "inside" (Li-HBsAg). Externally, it binds the virus to cellular receptors, initiates infection, determines species specificity, and promotes viral particle internalization via caveolin-mediated endocytosis. Large envelope Protein, HBV-C (P.pastoris, 180a.a, His) is the recombinant Virus-derived Large envelope protein, expressed by P. pastoris , with N-6*His labeled tag.
Background
The Large Envelope Protein exists in two topological conformations, namely 'external' or Le-HBsAg, and 'internal' or Li-HBsAg. In its external conformation, the protein acts as a critical agent, binding the virus to cell receptors and initiating infection. This pivotal interaction not only establishes species specificity and liver tropism but also triggers virion internalization, predominantly through caveolin-mediated endocytosis. The Large Envelope Protein further facilitates fusion between the virion membrane and the endosomal membrane. In its internal conformation, the protein plays a crucial role in virion morphogenesis, functioning akin to a matrix protein and mediating contact with the nucleocapsid. Simultaneously, the middle envelope protein plays a vital role in virion budding, inducing a nucleocapsid-independent process. This budding mechanism leads to the formation of subviral lipoprotein particles, with a diameter of 22 nm, devoid of a nucleocapsid.
Technical Parameters
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Species Virus
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Source P. pastoris
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Tag N-6*His
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Accession
P31868 (G2-G181)
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Gene ID/
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Molecular Construction
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N-term
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6*His
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HBV-C L (G2-G181)
Accession # P31868 -
C-term
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Protein Length
Topological domain
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Synonyms
S; Large envelope protein; L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen
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AA Sequence
GGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDHWPEANQVGVGTFGPGFTPPHGGLLGWSPQAQGILTTVPAAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRTGDPAPNMENTTSG
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Predicted Molecular Mass
20.9 kDa
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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.
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)
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