Cobra venom factor, partial, Naja kaouthia, recombinant

Organism: Naja kaouthia (Monocled cobra) (Naja siamensis). Source: E.coli. Expression Region: 733-984aa. Protein Length: Partial. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: DDNEDGFIAD SDIISRSDFP KSWLWLTKDL TEEPNSQGIS SKTMSFYLRD SITTWVVLAV SFTPTKGICV AEPYEIRVMK VFFIDLQMPY SVVKNEQVEI RAILHNYVNE DIYVRVELLY NPAFCSASTK GQRYRQQFPI KALSSRAVPF VIVPLEQGLH DVEIKASVQE ALWSDGVRKK LKVVPEGVQK SIVTIVKLDP RAKGVGGTQL EVIKARKLDD RVPDTEIETK IIIQGDPVAQ IIENSIDGSK LN. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity. Reference: "Molecular cloning and derived primary structure of cobra venom factor."Fritzinger D.C., Bredehorst R., Vogel C.-W.Proc. Natl. Acad. Sci. U.S.A. 91:12775-12779(1994). Function: Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.