mCherry-encoding Oncolytic Herpes Simplex Virus 1 (ΔICP27), CMV-mCherry(Cat#: RepOV-0006XY)
DatasheetThis product is a mCherry encoding oncolytic herpes simplex virus, which is based on HSV-1 with ICP27 deleted. ICP27 is highly cytotoxic probably due to its secondary role of preventing the splicing of pre-mRNAs in favour of translation from the mainly unspliced hepes RNAs. Deletion of ICP27 might produce a safer and less cytotoxic system when combined with other oncolytic-rendered modifications. 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 (ΔICP27) |
| 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 | ΔICP27 |
| Promoter | CMV |
| Transgene | mCherry |
| Type of Transgene | Reporter gene |
| Related Target/Protein | mCherry Fluorescence Protein |
| Capsid Modification | None |
| Titer | >1*10^8 PFU |
| Related Diseases | Tumor |
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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