Hepatitis A Virus, P3C, Recombinant (HAV)

Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein and a panel of serum samples from acutely HAV-infected patients. The term "antigenic domain" is used in this study to define a protein region spanned with consecutive overlapping immunoreactive peptides. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 aa, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 aa, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. It is interesting to note that four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.\n\nRecombinant protein corresponding to aa1643-1743 containing the P3C immunodominant regions from the Hepatitis A Virus expressed in E. coli.\n\nApplications:\nSuitable for use in ELISA and Western Blot. Other applications not tested. \n\nRecommended Dilutions:\nOptimal dilutions to be detrmined by the researcher.\n\nSpecificity:\nImmunoreactive with sera of HAV-infected individuals\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1900-30A

Size

100ug

Form

Supplied as a liquid in 10mM CBB, pH 9.6, 0.1% SDS, 50% glycerol.

Purity

(same/more than)90% by 10% PAGE with coomassie staining. Chromatographically purified.

References

1. Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization. Peters H, Kusov YY, Benie AJ, Peters T, Biochem J 2005 Jan 15;385(Pt 2):363-70 2. Structural variations in keto-glutamines for improved inhibition against hepatitis A virus 3C proteinase. Jain RP, Vederas JC, Bioorg Med Chem Lett 2004 Jul 16;14(14):3655-8 3. Expression of hepatitis A virus procapsids in the insect cells infected by recombinant baculovirus] Dzagurov GK, Kusov IuIu, Vopr Virusol 2003 May-Jun;48(3):36-40 4. Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system. Losick VP, Schlax PE, Lawson TG, Virology 2003 May 10;309(2):306-19 5. Hepatitis A virus VP3 may activate serum response element associated transcription. Kanda T, Yokosuka O, Imazeki F, Omata M, Scand J Gastroen terol 2003 Mar;38(3):307-13 6. Mutational characteristics in consecutive passage of rapidly replicating variants of hepatitis A virus strain H2 during cell culture adaptation. Hu NZ, Hu YZ, Liu GD, World J Gastroenterol 2002 Oct;8(5):872-8.