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Recombinant Hepatitis孭 Virus嘭2C-P3A Mosaic?/h1> Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HAV-230

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. . 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. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.

Description :

The protein contains the HAV core proteins P2C-P3A immunodominant regions, amino acids: (1392-1521),(1492-1606). HAV core proteins are purified by proprietary chromatographic techniques.

Purification method:

Purified by proprietary chromatographic technique.

Purity:

Recombinant HAV P2C-P3A is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

Formulation:

1mg/ml in 10mM CBB, pH9.6, 0.1% SDS and 50% glycerol

Storage:

Recombinant HAV is shipped at ambient temperature. Upon arrival, Store at -20C.

Stability:

Recombinant HAV is stable 5 years frozen, One month in solution at room temperature.

Specificity:

Immunoreactive with sera of HAV-infected individuals

Application:

Recombinant HAV Antigen may be used in ELISA and Western blots, excellent for detection of HAV with minimal specificity problems.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.


Protein synonyms/aliases:

Genome polyprotein

Precursor's functional components:

Coat protein VP4 (P1A)
Coat protein VP2(P1B)
Coat protein VP3 (P1C)
Coat protein VP1 (P1D)
Picornain 2A(EC 3.4.22.29)
    (Core protein P2A)
Core protein P2B
Core protein P2C;Probable protein P3A
Probable protein P3B
Picornain 3C(EC 3.4.22.28)
    (Protease 3C)
    (P3C)
RNA-directed RNA polymerase(EC 2.7.7.48)
    (P3D) .

Protein Family:


Protein Domains:


Domains:
IPR001676   Picornavirus capsid
IPR000605   RNA helicase
IPR000199   Peptidase C3A and C3B, picornaviral
IPR007095   RNA-directed RNA polymerase, double-strand and positive-strand RNA virus
IPR001205   RNA-directed RNA polymerase, P3D protein

Protein links:

Recombinant Hepatitis孭 Virus嘭2C-P3A Mosaic?protein domain

Recombinant Hepatitis孭 Virus嘭2C-P3A Mosaic?protein family


Precursor- Protein structure and amino acid sequence:


Latest Publications:

1. [Genomic sequence of hepatitis A virus L-A-1 vaccine strain]
Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 2004 Dec;18(4):360-2
2. Hepatitis A virus VP3 may activate serum response element associated transcription.
Scand J Gastroenterol 2003 Mar;38(3):307-13
3. [Expression of the 3a and 3d fusion protein of hepatitis A virus in prokaryotic cell and antigenicity analysis]
Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi 2002 Sep;16(3):215-8
4. Mutational characteristics in consecutive passage of rapidly replicating variants of hepatitis A virus strain H2 during cell culture adaptation.
World J Gastroenterol 2002 Oct;8(5):872-8
5. Mapping of protein domains of hepatitis A virus 3AB essential for interaction with 3CD and viral RNA.
Virology 1999 Nov 25;264(2):410-21
6. Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC.
J Virol 1999 Dec;73(12):9867-78

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中華民國95年06月06日更新