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SERPIN G1 is a member of the serpin family, The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. SERPIN G1 is involved in the inhibition of the complement system to prevent spontaneous activation. SERPIN G1 may play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SERPIN G1 prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. SERPIN G1 is a very efficient physiological inhibitor of FXIIa, plasma kallikrein and fXIa, and could inhibit chymotrypsin and kallikrein. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases in the C1 complex of classical pathway of complement. Activation of the C1 complex is under control of the C1-inhibitor.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
10 μg | $184 | 7-10 days | |
50 μg | $545 | 7-10 days | |
500 μg | $1,900 | 7-10 days | |
1 mg | $2,970 | 7-10 days |
Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | SERPIN G1 is a member of the serpin family, The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. SERPIN G1 is involved in the inhibition of the complement system to prevent spontaneous activation. SERPIN G1 may play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SERPIN G1 prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. SERPIN G1 is a very efficient physiological inhibitor of FXIIa, plasma kallikrein and fXIa, and could inhibit chymotrypsin and kallikrein. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases in the C1 complex of classical pathway of complement. Activation of the C1 complex is under control of the C1-inhibitor. |
Species | Mouse |
Expression System | HEK293 Cells |
Tag | C-6xHis |
Accession Number | P97290 |
Synonyms | Serping1,SERPIN G1,Plasma protease C1 inhibitor,C1nh,C1-inhibiting factor,C1 Inh,C1 esterase inhibitor |
Amino Acid | Ala20-Gly504 |
Construction | Ala20-Gly504 |
Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
Molecular Weight | 90 KDa (reducing condition) |
Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris-HCl, 150 mM NaCl, pH 8.0. |
Reconstitution | Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing. |
Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
Research Background | SERPIN G1 is a member of the serpin family, The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. SERPIN G1 is involved in the inhibition of the complement system to prevent spontaneous activation. SERPIN G1 may play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SERPIN G1 prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. SERPIN G1 is a very efficient physiological inhibitor of FXIIa, plasma kallikrein and fXIa, and could inhibit chymotrypsin and kallikrein. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases in the C1 complex of classical pathway of complement. Activation of the C1 complex is under control of the C1-inhibitor. |
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