MMP9-expressing Oncolytic Herpes Simplex Virus 1 (ΔΔICP34.5, ΔΔICP47), CMV-MMP9(Cat#: CyOV-0063XY)

This product is a MMP9 expressing oncolytic herpes simplex virus, which is based on HSV-1 with two copies of both ICP34.5 and ICP47 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. ICP47 usually functions to block antigen presentation in HSV-infected cells so its disruption leads to a virus that does not confer on infected tumour cells properties that might protect them from the host's immune system when infected with HSV. 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 (ΔΔICP34.5, ΔΔICP47)
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 ΔΔICP34.5, ΔΔICP47
Promoter CMV
Transgene MMP9
Type of Transgene Cytokine
Related Target/Protein Matrix metallopeptidase 9
Capsid Modification None
Titer >1*10^8 PFU
Related Diseases Glioma

Transgene

Alternative Names MMP9, GELB, CLG4B, MMP-9, MANDP2, matrix metallopeptidase 9
Gene ID 4318

Information

Introduction 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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