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HAV-VP1-P2A (residues 722-830), Hepatitis A Virus Coat Protein VP1- Core Protein P2A, recombinant, E. coli

Research Use Only
PR-1113
Jena Bioscience
ApplicationsWestern Blot, ELISA
Product group Proteins / Signaling Molecules
€ 391,00
100 ug
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Overview

  • Supplier
    Jena Bioscience
  • Product Name
    HAV-VP1-P2A (residues 722-830), Hepatitis A Virus Coat Protein VP1- Core Protein P2A, recombinant, E. coli
  • Delivery Days Customer
    5
  • Applications
    Western Blot, ELISA
  • Certification
    Research Use Only
  • Estimated Purity
    >90%
  • Scientific Description
    The protein contains the HAV Coat protein VP1 and core protein P2A immunodominant regions, amino acids 722-830. HAV core proteins are purified by proprietary chromatographic techniques. Background: 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 HAVinfected 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.
  • Storage Instruction
    -20°C
  • UNSPSC
    12352202