Recombinant Influenza A virus Matrix protein 2(M) Reference: CSB-CF389902ILU_100 Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation (By similarity).
Recombinant Influenza A virus Matrix protein 2(M) Reference: CSB-CF389902ILU_20 Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation (By similarity).
Recombinant Eisenia fetida Lysenin Reference: CSB-CF515723EJV_100 Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.
Recombinant Eisenia fetida Lysenin Reference: CSB-CF515723EJV_20 Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.
Recombinant Bombyx mori Cecropin-D(CECD) Reference: CSB-CF524922BTT_100 Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
Recombinant Bombyx mori Cecropin-D(CECD) Reference: CSB-CF524922BTT_20 Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
Recombinant Halobacterium salinarum Cobalamin import system permease protein... Reference: CSB-CF532244HTL(A4)_100 Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably involved in the translocation of the substrate across the membrane
Recombinant Halobacterium salinarum Cobalamin import system permease protein... Reference: CSB-CF532244HTL(A4)_20 Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably involved in the translocation of the substrate across the membrane