The full-length genome of TYLCSV (1.8 copies) is cloned in the binary plasmid vector pBin19, allowing transformation into Agrobacterium and infection of plants
Unit: 1 microgram, allowing infection of plants following transformation into Agrobacterium
Plasmid contains the entire genome of HIV-1 with a specific mutation in the protease gene, which has been described as a polymorphic mutation. It is unclear, whether it can confer drug resistance to specific HIV-1 PR inhibitors directly. It has been shown in cell culture that the presence of the 63P change leads to higher "replicative fitness" of the virus. The respective mutations have been reported in viruses from HIV-infected individuals on PR inhibitors with virologic therapy failure.
Purified recombinant SARS-CoV-2 P.3 Spike protein (trimerisation domain and C-terminal hexa histidine-tag) expressed in mammalian HEK293F cells as secreted protein
Purified recombinant SARS-CoV-2 BA.2 (B.1.1.529.2) Spike protein (trimerisation domain and C-terminal hexa histidine-tag) expressed in mammalian HEK293F cells as secreted protein
Purified recombinant SARS-CoV-2 BA.2.75 (B.1.1.529.2.75) Spike protein (trimerisation domain and C-terminal hexa histidine-tag) expressed in mammalian HEK293F cells as secreted protein
Purified recombinant SARS-CoV-2 A.30 Spike protein (trimerisation domain and C-terminal hexa histidine-tag) expressed in mammalian HEK293F cells as secreted protein
Purified recombinant SARS-CoV-2 BA.4/BA.5 (B.1.1.529.4/5) Spike protein (trimerisation domain and C-terminal hexa histidine-tag) expressed in mammalian HEK293F cells as secreted protein
plasmid encoding the VSV antigenome, lacking the G gene, and encoding mCherry, for producing recombinant VSV lacking a glycoprotein for pseudotyping assays or for cloning and production of VSV encoding foreign glycoproteins.
plasmid encoding the VSV antigenome, lacking the G gene, and encoding eGFP, for producing recombinant VSV lacking a glycoprotein for pseudotyping assays or for cloning and production of VSV encoding foreign glycoproteins.