Large envelope protein (S) Recombinant Protein | S recombinant protein

Recombinant Duck hepatitis B virus Large envelope protein (S)

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Large envelope protein (S); Recombinant Duck hepatitis B virus Large envelope protein (S); Recombinant Large envelope protein (S); Large envelope protein; L glycoprotein L-HBsAg; LHB Large S protein Large surface protein Major surface antigen Cleaved into the following chain: 1. Truncated S protein; 2. St; S recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 164-240
• Sequence: MAGTFGGILAGLIGLLVGFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYAGFCPWGCPGFLWTYL
• Sequence Length: 330

• Species: Duck hepatitis B virus (isolate white Shanghai duck S31) (DHBV)
• Preparation and Storage: Store at -20 degree C. For extended storage, store at -20 or -80 degree C.

NCBI and Uniprot Product Information

• NCBI GI #: 172045836
• UniProt Accession #: P17195
• Molecular Weight: 36,787 Da
• NCBI Official Full Name: Large envelope protein
• UniProt Protein Name: Large envelope protein
• UniProt Gene Name: S
• UniProt Synonym Gene Names: LHB; St
• UniProt Entry Name: HBSAG_HPBDW

Uniprot Description

Function: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. The large envelope protein probably also assumes fusion between virion and host membranes. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein

By similarity.Truncated S protein may be involved in translocation of pre-S domain through the virion membrane

By similarity.

Subunit structure: Large internal envelope protein interacts with capsid protein

By similarity.

Subcellular location: Virion membrane.

Domain: The large envelope protein is synthesized with the pre-S region at the cytosolic side of the endoplasmic reticulum and, hence will be within the virion after budding. Therefore the pre-S region is not N-glycosylated. Later a post-translational translocation of N-terminal pre-S and TM1 domains occur in about 50% of proteins at the virion surface. These molecules change their topology by an unknown mechanism, resulting in exposure of pre-S region at virion surface.

Post-translational modification: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles.Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg).

Sequence similarities: Belongs to the avihepadnavirus major surface antigen family.

Sequence caution: The sequence AAA45752.1 differs from that shown. Reason: Erroneous initiation.