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.
| 説明 |
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 Host |
Human Cells
|
| Tag |
C-6His
|
| Accession Number |
P97290
|
| 別名 |
Serping1, Plasma protease C1 inhibitor, C1 Inh, C1 esterase inhibitor, C1-inhibiting factor, SERPIN G1, C1nh
|
| Amino Acid |
Ala20-Gly504
|
| Construction |
Recombinant Mouse Serine Protease Inhibitor-clade G1 is produced by our Mammalian expression system and the target gene encoding Ala20-Gly504 is expressed with a 6His tag at the C-terminus.
|
| Protein Purity |
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
|
| 分子量 |
90 KDa, reducing conditions
|
| Endotoxin |
Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
|
| Formulation |
Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
|
| Reconstitution |
Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
|
| Stability & Storage |
Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
|
| Shipping |
The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below.
|
| 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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