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Serpin G1 Protein, Human, Recombinant (His)

カタログ番号 TMPJ-00502
別名: C1-Inhibiting Factor, Serpin G1, SERPING1, C1 Esterase Inhibitor, C1 Inh, Plasma Protease C1 Inhibitor, C1Inh, C1NH, C1IN

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
Serpin G1 Protein, Human, Recombinant (His)
パッケージサイズ 在庫状況 単価(税別)
10 μg 約5 days ¥ 30,000
50 μg 約5 days ¥ 89,500
500 μg 約5 days ¥ 436,000
1 mg 約5 days ¥ 626,500
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生物学的特性に関する説明
Technical Params
Product Properties
説明 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.
Species Human
Expression Host HEK293 Cells
Tag C-6xHis
Accession Number AAH11171.1
別名 C1-Inhibiting Factor, Serpin G1, SERPING1, C1 Esterase Inhibitor, C1 Inh, Plasma Protease C1 Inhibitor, C1Inh, C1NH, C1IN
Amino Acid Asn23-Ala500
Construction Asn23-Ala500
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
分子量 102 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℃. For reconstituted proteinsolutions, 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 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.

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Keywords

Serpin G1 Protein, Human, Recombinant (His) C1-Inhibiting Factor Serpin G1 SERPING 1 SERPING1 C1 Esterase Inhibitor C1 Inh Plasma Protease C1 Inhibitor C1Inh SERPING-1 C1NH C1IN recombinant recombinant-proteins proteins protein