Reporter-encoding Oncolytic Vaccinia Virus Western Reserve (ΔE3L,ΔK3), pSE/L-(mCherry) (RepOV-0084WQ)

This product is a mCherry encoding oncolytic vaccinia virus, which is based on VACV-WR with E3L and K3L double deleted.Protein E3 plays a role in the inhibition of multiple cellular antiviral responses activated by dsRNA, such as inhibition of PKR activation, apoptosis, and IFN-mediated antiviral activities. Protein K3 acts as a pseudosubstrate for EIF2AK2/PKR kinase. Inhibits therefore eIF-2-alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff.The double deletion of E3L and K3L with oncolytic-rendered modifications could enhance an immune response to a poxvirus vaccine.This product can be used in oncolytic virotherapy research and vaccinie application.

Family Poxviridae
Species Vaccinia virus
Serotype Western Reserve
Backbone VACV-WR(ΔE3L,ΔK3)
Backbone Background VACV-WR strain derived from Wyeth through passaging in mice and shown high tumor selectivity and strong oncolytic effect in mouse models.The engineered VACV-WR could further enhance the immune activity and the efficacy of cancer therapies.
Gene Modification ΔE3L,ΔK3
Promoter pSE/L
Transgene mCherry
Type of Transgene Reporter gene
Related Target/Protein mCherry Fluorescence Protein
Capsid Modification None
Titer >1*10^8 PFU
Related Diseases Breast cancer, Prostate cancer, Colon cancer, Cancer vaccine
Alternative Names mCherry
Introduction mCherry is a member of the mFruits family of monomeric red fluorescent proteins (mRFPs). As a RFP, mCherry was derived from DsRed of Discosoma sea anemones. mCherry absorbs light between 540-590 nm and emits light in the range of 550-650 nm. mCherry belongs to the group of fluorescent protein chromophores used as vital instruments to visualize genes and analyze their functions in experiments. Genome editing has been improved greatly through the precise insertion of these fluorescent protein tags into the genetic material of many diverse organisms. Most comparisons between the brightness and photostability of different fluorescent proteins have been made in vitro, removed from biological variables that affect protein performance in cells or organisms. It is hard to perfectly simulate cellular environments in vitro, and the difference in environment could have an effect on the brightness and photostability.
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