Anti-HBsAg Polyclonal Antibody is a Goat antibody targeting HBsAg. Anti-HBsAg Polyclonal Antibody can be used in WB,IHC-P,IHC-Fr,IF,ELISA.

IgG

Human,HBV (predicted:Bee,Hepatitis B virus)

1. Paraformaldehyde-fixed, paraffin embedded (Hepatitis B virus infected human hepatocellular carcinoma); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15 min; Blocking buffer (normal goat serum) at 37°C for 30 min; Antibody incubation with (HBSAg) Polyclonal Antibody, Unconjugated (TMAB-00835) at 1:200 overnight at 4°C, followed by A594 conjugated Rabbit Anti-Goat IgG H&L secondary antibody incubation and staining.
2. Measured by its binding ability in a indirect ELISA. Immobilized recombinant HBSAg protein at 2 μg/mL (100 μL/well) can bind  Goat Anti-Human HBSAg Antibody, the EC50 is 29.14 ng/mL.
3. Sample:
Lane 1: Recombinant HBSAg protein
Primary: Anti-HBSAg (TMAB-00835) at 1/1000 dilution
Secondary: IRDye800CW Donkey anti-Goat IgG at 1/20000 dilution
Predicted band size: 44 kDa
Observed band size: 20 kDa

WB: 1:500-2000; IHC-P: 1:100-500; IHC-Fr: 1:100-500; IF: 1:100-500; ELISA: 1:5000-10000

Polyclonal

Recombinant Protein: HBsAg protein

S

Large envelope protein

Hepatitis B

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. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein.
The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid.