GeneBio Systems
Recombinant Human SerpinG1/C1IN Protein (His Tag)
Recombinant Human SerpinG1/C1IN Protein (His Tag)
SKU:PKSH033043
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Size: 50μg
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Exp date: 12 months
Category ID_II: Recombinant Proteins
Category ID_III: Others
Abbreviation: SerpinG1;C1IN
Target Synonym: C1 Esterase Inhibitor;C1 Inh;C1-Inhibiting Factor;C1IN;C1Inh;C1NH;HAE1;HAE2;Plasma Protease C1 Inhibitor;SERPING1;Serpin G1
Research Areas: Cardiovascular;immunology
Conjugation:
Target Species: Human
Expression Host: HEK293 Cells
Application:
Fusion tag: C-His
UNIProt ID: P05155
Accession: AAH11171.1
Background: As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. Serpin G1 is a serine protease inhibitor protein. It is the largest member among the serpin class of proteins. Remarkably, Serpin G1 has a 2-domain structure, unlike most family members. The C-terminal serpin domain is similar to other serpins, and this part of Serpin G1 provides the inhibitory activity. The N-terminal domain is not essential for Serpin G1 to inhibit proteinases and has no similarity to other proteins. The main function of Serpin G1 is the inhibition of the complement system to prevent spontaneous activation. Serpin G1 is an acute phase protein and circulates in blood at levels of around 0.25g/L, whose levels rise 2-fold during inflammation. Although named after its complement inhibitory activity, Serpin G1 also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Most notably, Serpin G1 play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. It is also the most important physiological inhibitor of fXIIa, chymotrypsin and plasma kallikrein.
Concentration:
Activity: Not validated for activity
Sequence: Asn23-Ala500
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 53.9 kDa
ObservedMW: 102 kDa
