| Catalog# |
CJ07 |
| Source |
Human cells |
| Description |
Recombinant mouse SERPIN G1 is produced with our mammalian expression system in human cells. The target protein is expressed with sequence (Ala20-Gly504) of mouse SERPIN G1 fused with a polyhistidine tag at the C-terminus. |
| Names |
SERPIN G1/Plasma protease C1 inhibitor/C1 Inh/C1Inh/C1 esterase inhibitor/C1-inhibiting factor/Serping1/C1nh |
| Accession # |
P97290 |
| Formulation |
Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl,pH8.0 |
| Shipping |
The product is shipped at ambient temperature. |
| Reconstitution |
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 3X PBS.
Please aliquot the reconstituted solution |
| Storage |
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 5 months. |
| Purity |
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
| Endotoxin |
Less than 0.1 ng/µg (1 IEU/µg). |
| Amino Acid Sequence |
AFSDPEATSHSTQDPLEAQAKSRESFPERDDSWSPPEPTVLPSTWPTTSVAITITNDTMGKVANE SFSQHSQPAAQLPTDSPGQPPLNSSSQPSTASDLPTQATTEPFCPEPLAQCSDSDRDSSEAKLSE ALTDFSVKLYHAFSATKMAKTNMAFSPFSIASLLTQVLLGAGDSTKSNLESILSYPKDFACVHQA LKGFSSKGVTSVSQIFHSPDLAIRDTYVNASQSLYGSSPRVLGPDSAANLELINTWVAENTNHKI RKLLDSLPSDTCLVLLNAVYLSAKWKITFEPKKMMAPFFYKNSMIKVPMMSSVKYPVAQFDDHTL KAKVGQLQLSHNLSFVIVVPVFPKHQLKDVEKALNPTVFKAIMKKLELSKFLPTYLTMPHIKVKS SQDMLSVMEKLEFFDFTYDLNLCGLTEDPDLQVSAMKHETVLELTESGVEAAAASAISFGRSLPI FEVQRPFLFLLWDQQHRFPVFMGRVYDPRGVDHHHHHH
|
| 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. |
