mCherry-encoding Oncolytic Herpes Simplex Virus 1 (ΔICP6, ΔΔICP34.5), hTERT-mCherry(Cat#: RepOV-0048XY)

This product is a mCherry encoding oncolytic herpes simplex virus, which is based on HSV-1 with ICP6 and two copies of ICP34.5 deleted. ICP6 encodes a viral ribonucleotide reductase (vRR) function that allows replication of wild-type HSV to occur even in quiescent cells, such as the neurons. ICP34.5 protein, is important for viral replication, viral exit from infected cells, prevention of the premature shut-off of protein synthesis in the infected host, and neurovirulence. This product can be used in oncolytic virotherapy research and further recombinant HSV construction.

Specifications

Family Herpesviridae
Species Herpes simplex virus
Serotype Herpes simplex virus 1
Backbone HSV-1 (ΔICP6, ΔΔICP34.5)
Backbone Background Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), also known as human herpesvirus 1 and 2 (HHV-1 and HHV-2), are two members of the human Herpesviridae family, a set of viruses that produce viral infections in the majority of humans. Modified Herpes simplex virus is considered as a potential therapy for cancer and has been extensively clinically tested to assess its oncolytic ability.
Gene Modification ΔICP6, ΔΔICP34.5
Promoter hTERT
Transgene mCherry
Type of Transgene Reporter gene
Related Target/Protein mCherry Fluorescence Protein
Capsid Modification None
Titer >1*10^8 PFU
Related Diseases Glioma

Transgene

Alternative Names mCherry
UniProt ID X5DSL3

Information

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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