Hepatitis A Virus VP3 Capsid Protein
recombinant, E. coli
For in vitro use only!
Shipping: shipped on blue ice
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 38 kDa
Purity: > 95 % (SDS-PAGE, RP-HPLC)
Form: liquid (Supplied as 1 mg/ml solution in 10 mM CBB pH 9.6, 0.1% SDS and 50% glycerol)
The protein contains the HAV VP3 immunodominant regions, amino acids: 304-415. Hepatitis A Virus VP1 protein is purified by proprietary chromatographic techniques.
Background: HAV, the prototype of the genus Hepatovirus, belongs to the family Picornaviridae. Its 7.5-kb single-stranded RNA genome bears different distinct regions: the 5' and 3' noncoding regions (NCR), the P1 region, which encodes the structural proteins VP1, VP2, VP3, and a putative VP4, and the P2 and P3 regions encoding nonstructural proteins associated with replication. Hepatitis A virus (HAV) encodes a single polyprotein which is posttranslationally processed into the functional structural and nonstructural proteins. Only one protease, viral protease 3C, has been implicated in the nine protein scissions.
Recombinant HAV-VP3 may be used in ELISA and Western blots, excellent for detection of HAV with minimal specificity problems.
Specificity: Immunoreactive with sera of HAV-infected individuals.
Sanchez et al. (2004) A novel CD4+ T-helper lymphocyte epitope in the VP3 protein of hepatitis A virus. J. Med. Virol. 72:525.
Kanda et al. (2004) Hepatitis A virus VP3 may activate serum response element associated transcription. Scand. J. Gastroenterol. 38:307.
Haro et al. (2003) Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: a robust method for vaccine design. FEBS Lett. 540:133.
Chavez et al. (2001) Membrane fusion induced by a lipopeptidic epitope from VP3 capside protein of hepatitis A virus. Luminescence. 16:135.
Sospedra et al. (2001) Interaction study of peptide from VP3 capsid protein of hepatitis A virus through monolayers and fluorescence spectroscopy. Luminescence. 16:103.
Chavez et al. (2001) Membrane fusion by an RGD-containing sequence from the core protein VP3 of hepatitis A virus and the RGA-analogue: implications for viral infection. Biopolymers. 58:63.