Cobra Venom Factor, Naja naja kaouthia

Native cobra venom factor from Naja naja kaouthia. Glycoprotein composed of three non-identical disulfide-bonded subunits with M.W. of 68 kDa (α), 48 kDa (β), and 30 kDa (γ). Cobra venom factor (CVF) is a structural and functional analog of cobra, as well as mammalian C3. Thus, in the presence of Factor B, Factor D, and Mg²⁺, CVF can form a stable CVF,Bb complex that is a C3/C5 convertase enzyme; however, the CVF,Bb complex is not susceptible to regulation by Factors H and I. Four to six µg of purified CVF are equal to 1.0 unit of functional activity as measured by the method of Cochrane, et al.

Native cobra venom factor from Naja naja kaouthia. Glycoprotein composed of three nonidentical disulfide-bound subunits with M.W. of 68,000 (α), 48,000 (β), and 30,000 (γ). Cobra Venom Factor (CVF) is a structural and functional analog of cobra, as well as mammalian C3. In the presence of Factor B, Factor D, and Mg²⁺, CVF can form a stable CVF, Bb complex which is a C3/C5 convertase enzyme; however, the CVF,Bb complex is not susceptible to regulation by Factors H and I. Four to six µg of purified CVF is equal to 1.0 unit of functional activity as measured by the method of Cochrane, et al.

Toxicity: Harmful (C)

Bogers, W.M., et al. 1993. Eur. J. Immunol.23, 433.
Fritzinger, D.C., et al. 1992. J. Immunol. 149, 3554.
Muller, B. and Muller-Ruchholtz, W. 1987. Leuk. Res.11, 461.
Vogel, C.W. and Muller-Eberhard, H.J. 1984. J. Immunol. Methods73, 203.
Cochrane, C.G., et al. 1970. J. Immunol. 105, 55.
Ballows, M. and Cochrane, C.G. 1969. J. Immunol.103, 944.

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