This product is a MMP9 expressing oncolytic herpes simplex virus, which is based on HSV-1 with ICP34.5 and UNG deleted. 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. Uracil DNA glycosylase (UNG, UDG) is the most abundant cellular enzyme encoded by the UL2 gene for removing uracil generated by hydrolytic deamination of cytosine or misincorporation of dUTP. The deletion of UDG may have contributed to lower rates of DNA repair during the passage or selection conditions. 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 (ΔICP34.5, ΔUNG)
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.
Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. In humans the MMP9 gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain.
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Datasheet