Recombinant human SERPING1 protein is a Human Fragment protein, in the 23 to 500 aa range, expressed in CHO, with >95% purity, < 1 EU/µg endotoxin level and suitable for HPLC, SDS-PAGE, FuncS.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes Migrates at an apparent molecular weight of approximately 80-90 kDa by SDS PAGE analysis under reducing conditions. |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein.
C1IN, C1NH, SERPING1, Plasma protease C1 inhibitor, C1 Inh, C1Inh, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1
Recombinant human SERPING1 protein is a Human Fragment protein, in the 23 to 500 aa range, expressed in CHO, with >95% purity, < 1 EU/µg endotoxin level and suitable for HPLC, SDS-PAGE, FuncS.
Constituents: 0.14% Sodium phosphate
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein.
Belongs to the serpin family.
Highly glycosylated (49%) with N- and O-glycosylation. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This product was previously labelled as C1 Inactivator
SERPING1 also known as C1 inhibitor or C1-inactivator is a protein that plays an important mechanical role in the regulation of the complement system. It is a member of the serpin superfamily and has a molecular mass of approximately 105-110 kDa. This protein is mainly expressed in the liver but also present in other tissues such as monocytes and epithelial cells. As an inhibitor SERPING1 effectively regulates the activity of the complement subcomponents C1r and C1s plasmin and kallikrein by inhibiting their protease activity preventing unwanted activation of the complement cascade.
The protein acts as a critical control point in the complement and contact activation system. It is part of the C1 complex which includes the proteins C1q C1r and C1s. The regulation extends to pathways that involve the breakdown of plasma proteins and prevention of spontaneous inflammatory reactions. By controlling these pathways the protein prevents excessive inflammation and tissue damage which can occur during immune responses. Its involvement extends to the regulation of the complement system and maintenance of vascular permeability.
SERPING1 interacts closely with mechanisms involved in the complement cascade and the kinin-kallikrein pathways. It associates with proteins like MASP-1 and MASP-2 important in the complement and lectin pathways. These pathways are important for innate immunity and influence factors like inflammation and blood pressure. SERPING1 modulates these pathways by inhibiting key enzymes and ensuring controlled responses therefore maintaining systemic balance within the immune system.
The malfunction or deficiency of SERPING1 has direct links to hereditary angioedema a condition marked by severe and rapid swelling episodes. The disorder results from inadequate inhibition of bradykinin emphasizing the protein's role in vascular regulation. Additionally the protein has implications in autoimmune diseases such as systemic lupus erythematosus where complement regulation is disrupted. The interplay between SERPING1 and other proteins such as bradykinin receptor B2 remains significant in understanding disease mechanisms and developing therapeutic interventions.
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