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Serpin G1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00502
Synonyms: 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.

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Serpin G1 Protein, Human, Recombinant (His)
Pack Size Availability Price/USD Quantity
10 μg 5 days $ 129.00
50 μg 5 days $ 390.00
500 μg 5 days $ 1,900.00
1 mg 5 days $ 2,730.00
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Biological Description
Technical Params
Product Properties
Description 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 System Human Cells
Tag C-6His
Accession Number AAH11171.1
Synonyms C1-Inhibiting Factor, Serpin G1, SERPING1, C1 Esterase Inhibitor, C1 Inh, Plasma Protease C1 Inhibitor, C1Inh, C1NH, C1IN
Amino Acid Asn23-Ala500
Construction Recombinant Human Serine Protease Inhibitor-clade G1 is produced by our Mammalian expression system and the target gene encoding Asn23-Ala500 is expressed with a 6His tag at the C-terminus.
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight 102 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 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

 

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