Product Overview
Recombinant norovirus-like particles. Particles are formed by expression of VP1 (AlbertaSG005/CA/2015) in HEK293 cells, and are purified from the cytoplasm using a proprietary series of density gradients.
Alternative Names
Norovirus; NoV; Norovirus GII.17 VLP; Norovirus GII.17 VLP; Norovirus GII.17; Norovirus VLP
Purity
Greater than 50% purity by SDS-PAGE.
Buffer
Proprietary buffer
Introduction
Norovirus VP1 protein is the capsid protein of Norovirus. It is a 59kD glycoprotein with three key domains. The shell domain (S domain) contains elements essential for the formation of the icosahedron. The Protruding domain (P domain) is divided into sub-domains P1 and P2. P domain interacts in dimeric contacts that increase the stability of the capsid and form the protrusions on the virion. A hypervariable region in P2 is thought to play an important role in receptor binding and immune reactivity.
Keywords
Norovirus; NoV; Norovirus GII.17 VLP; Norovirus GII.17 VLP; Norovirus GII.17; Norovirus VLP
Citations
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Q & A
Q: Could you please provide the strain information for the Norovirus GII.17 VLP?
A: The VLP is derived from the strain Human calicivirus NLV/Erfurt/546/00/DE.
Customer Reviews
USHIJIMA, H; MUKOYAMA, A; et al. SEROTYPING OF HUMAN ROTAVIRUSES IN THE TOKYO AREA (1990-1993) BY ENZYME-IMMUNOASSAY WITH MONOCLONAL-ANTIBODIES AND BY REVERSE TRANSCRIPTION AND POLYMERASE CHAIN-REACTION AMPLIFICATION. JOURNAL OF MEDICAL VIROLOGY 44:162-165(1994).
KOBAYASHI, N; et al. EFFECT OF THE SELECTION PRESSURE WITH ANTI-VP7 AND ANTI-VP4 NEUTRALIZING MONOCLONAL-ANTIBODIES ON REASSORTANT FORMATION BETWEEN 2 HUMAN ROTAVIRUSES (VOL 135, PG 383, 1992). ARCHIVES OF VIROLOGY 137:411-411(1994).
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COA
Certificate of Analysis
