Large envelope Protein, HBV-A (Cell-Free, P17101, His)

Large envelope proteins exist in two topological conformations: “external” (Le-HBsAg) and “internal” (Li-HBsAg). In its external state, it mediates viral attachment to cellular receptors, initiates infection, determines species specificity, and promotes viral particle internalization via caveolin-mediated endocytosis. Large envelope Protein, HBV-A (Cell-Free, P17101, His) is the recombinant Virus-derived Large envelope protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of Large envelope Protein, HBV-A (Cell-Free, P17101, His) is 399 a.a., with molecular weight of 45.1 kDa.

The Large Envelope Protein exhibits two distinct topological conformations, termed 'external' or Le-HBsAg, and 'internal' or Li-HBsAg. In its external conformation, the protein serves as a crucial mediator for attaching the virus to cell receptors, initiating infection, and determining species specificity and liver tropism. This interaction prompts virion internalization primarily through caveolin-mediated endocytosis, while also facilitating fusion between the virion membrane and the endosomal membrane. In its internal conformation, the protein plays a pivotal role in virion morphogenesis and functions as a matrix protein, establishing contact with the nucleocapsid. Simultaneously, the middle envelope protein contributes significantly to virion budding, inducing a nucleocapsid-independent process. This budding process leads to the formation of subviral lipoprotein particles with a diameter of 22 nm, lacking a nucleocapsid.

Virus

E. coli Cell-free

N-10*His

P17101 (G2-I400)

/

GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPVFGANSNNPDWDFNPIKDHWPAANQVGVGAFGPGFTPPHGGVLGWSPQAQGMLTPVSTIPPPASANRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQALQDPRVRGLYFPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLPVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSRSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLILGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSSFIPLLPIFFCLWVYI

45.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.