Parvovirus B19 VP1/VP2 Virus-like Particles (B19 VP1/VP2 VLPs)-SF9 (CAT#: VLP-025YF)

Datasheet

Recombinant Parvovirus B19 Virus-like Particles (B19 VLPs) are produced in Insect cell expression system, assembled with VP1 and VP2 structure protein. VLP is mimicking the native 3D structure of viruses which can elicit strong immune responses. However, VLPs lack viral genomic material which makes them non-infectious, unable to replicate and enhance the safety during manufacture and administration. B19 VLPs can be used in the development of B19 diagnostics and in vaccine development and R&D (including use as an immunogen).

Product Specifications

Structural Proteins
Capsid proteins VP1 and VP2

Expression Systems
Insect cell (Sf9) expression system

Buffer
16 mM sodium phosphate, 120 mM NaCl, pH 7.4 containing 20% glycerol

Form
Liquid

Alternative Names
Parvovirus B19 VP1/VP2 Virus-like Particles; B19 VP1/VP2 VLPs; VLPs; Virus-like Particles; erythrovirus B19 virus; Parvovirus B19 Virus; B19 Virus; B19 Virus-like Particles

Storage
Store at 4°C short term (2-4 weeks). Store at -80 °C long term. Avoid repeated freeze/thaw cycles.

Virus Background

Virus Family
Parvoviridae

Virus Species
Primate erythroparvovirus 1

Virus Overview
Erythroviruses belong to the Parvoviridae family of small DNA viruses. It is a non-enveloped, icosahedral virus that contains a single-stranded linear DNA genome of approximately 5,600 base pairs in length. The infectious particles may contain either positive or negative strands of DNA. The icosahedral capsid consists of 60 capsomeres, consisting of two structural proteins, VP1 (83 kDa) and VP2 (58 kDa), which are identical except for 227 amino acids at the amino-terminal of the VP1-protein, the so-called VP1-unique region. VP2 is the major capsid protein, and comprises approximately 95% of the total virus particle. VP1-proteins are incorporated into the capsid structure in a non-stoichiometrical relation (based on antibody-binding analysis and X-ray structural analysis the VP1-unique region is assumed to be exposed at the surface of the virus particle. At each end of the DNA molecule there are palindromic sequences which form "hairpin" loops. The hairpin at the 3' end serves as a primer for the DNA polymerase. It is classified as an erythrovirus because of its capability to invade red blood cell precursors in the bone marrow. Three genotypes (with subtypes) have been recognised.

Virus Structure
Non-enveloped, single-stranded linear DNA

Related Disease
Fifth disease, AIDS, Arthritis and arthralgias, Aplastic crisis, Hydrops fetalis

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Customer Review

Stable expression in the host

Stable expression and antibody production in mice.
2022-12-24

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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