Large envelope Protein, HBV-A (Cell-Free, P03141, His)

The large envelope protein exhibits two topological conformations: “external” (Le-HBsAg) and “internal” (Li-HBsAg). In the external state, it attaches the virus to cellular receptors, initiating infection and determining liver tropism. Large envelope Protein, HBV-A (Cell-Free, P03141, 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, P03141, His) is 399 a.a., with molecular weight of 45.1 kDa.

The Large Envelope Protein exhibits two distinct topological conformations, referred to as 'external' or Le-HBsAg, and 'internal' or Li-HBsAg. In its external conformation, the protein facilitates the attachment of the virus to cell receptors, initiating infection and determining species specificity and liver tropism. This interaction leads to virion internalization, primarily through caveolin-mediated endocytosis. Additionally, the large envelope protein ensures fusion between the virion membrane and endosomal membrane. In its internal conformation, the protein plays a crucial role in virion morphogenesis, acting as a matrix protein during contact with the nucleocapsid. Simultaneously, the middle envelope protein is pivotal in virion budding, inducing budding in a nucleocapsid-independent manner. Throughout this process, the majority of envelope proteins bud to form subviral lipoprotein particles with a diameter of 22 nm, devoid of a nucleocapsid.

Virus

E. coli Cell-free

N-10*His

P03141 (G2-I400)

/

GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI

45.1 kDa

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

<1 EU/μg, determined by LAL method.