Lot # Check on the product label
Clone # E6
Product Form Liquid
Purification & Buffer
Protein A or G purified and supplied in 0.01 M PBS (pH7.4) without preservative.
Purity >95% by HPLC & SDS-PAGE
Concentration 7 mg/ml
A synthetic peptide corresponding to the N-terminal of HBV-PreS1.
Specificity It specifically recognize N-terminal epitope of HBV-PreS1, and does not cross react with BSA, HBV-PreS2 and HBV-S antigens.
Other applications have not been tested.
The optimal dilutions should be determined by end user.
Matched antibody pair
Capture Ab: HBV-PreS1 mAb (clone # E6) & HBV-PreS1 mAb (clone # D8)
Recommended detection Ab: Goat anti-HBsAg pAb
Note: E6 & D8 mAbs should be combined used as the capture Ab.
Aliquot and store at -20°C for long term (at least one year).
Avoid repeated freeze and thaw cycles.
Hepatitis B virus (HBV), is a species of the genus Orthohepadnavirus, which is likewise a part of the Hepadnaviridae family of viruses. This virus causes the disease hepatitis B which is an infectious inflammatory illness of the liver and affects hominoidea, including humans. There are four known genes encoded by the genome called C, X, P, and S. Gene S is the gene that codes for the surface antigen (HBsAg). And HBsAg gene is one long open reading frame but contains three in frame "start" (ATG) codons that divide the gene into three sections, pre-S1, pre-S2, and S. The double interaction between the HBV capside and both S and pre-S1 domains may be required for virion morphogenesis.
1. Hunt, Richard (2007-11-21). "Hepatitis viruses". University of Southern California, Department of Pathology and Microbiology. Retrieved 2008-03-13.
2. Hassan MM, Li D, El-Deeb AS, et al. (October 2008). "Association between hepatitis B virus and pancreatic cancer". J. Clin. Oncol. 26 (28): 4557–62.
3. Francis poisson, Anne severac, Christophe hourioux, Alain goudeau, Philippe roingeard. Both Pre-S1 and S Domains of Hepatitis B Virus Envelope Proteins Interact with the Core Particle. Virology. Volume 228, Issue 1, 3 February 1997, Pages 115–120.