Recombinant Leiurus hebraeus Alpha-like toxin Lqh6 Reference: CSB-BP348580LDS_100 Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is highly toxic to insects and mice, and inhibits the binding of alpha-toxin to cockroach neuronal membranes.
Recombinant Leiurus hebraeus Alpha-like toxin Lqh6 Reference: CSB-BP348580LDS_20 Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is highly toxic to insects and mice, and inhibits the binding of alpha-toxin to cockroach neuronal membranes.
Recombinant Leiurus hebraeus Alpha-like toxin Lqh7 Reference: CSB-BP348581LDS_500 Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is highly toxic to insects and mice, and inhibits the binding of alpha-toxin to cockroach neuronal membranes.
Recombinant Leiurus hebraeus Alpha-like toxin Lqh7 Reference: CSB-BP348581LDS_100 Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is highly toxic to insects and mice, and inhibits the binding of alpha-toxin to cockroach neuronal membranes.
Recombinant Leiurus hebraeus Alpha-like toxin Lqh7 Reference: CSB-BP348581LDS_20 Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is highly toxic to insects and mice, and inhibits the binding of alpha-toxin to cockroach neuronal membranes.
Recombinant Tityus bahiensis Toxin Tb2-II Reference: CSB-BP350784TEQ_500 Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing . This toxin is active against both mammals and insects.
Recombinant Tityus bahiensis Toxin Tb2-II Reference: CSB-BP350784TEQ_100 Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing . This toxin is active against both mammals and insects.
Recombinant Tityus bahiensis Toxin Tb2-II Reference: CSB-BP350784TEQ_20 Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing . This toxin is active against both mammals and insects.
Recombinant Hamster polyomavirus Major capsid protein VP1 Reference: CSB-BP355947HBZ_500 Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Recombinant Hamster polyomavirus Major capsid protein VP1 Reference: CSB-BP355947HBZ_100 Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Recombinant Hamster polyomavirus Major capsid protein VP1 Reference: CSB-BP355947HBZ_20 Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.