C1-INH C1 Esterase Inhibitor Antibodies
Affinity Biologicals, Inc. manufactures a broad range of C1-INH C1 Esterase Inhibitor Antibodies which can be found in the listing below. Further information about each individual C1-INH C1 Esterase Inhibitor Antibody is available by following the associated links. Our C1-INH C1 Esterase Inhibitor Antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays. These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins. Affinity’s C1-INH C1 Esterase Inhibitor Antibodies are manufactured for use in research applications.
Listing of C1-INH C1 Esterase Inhibitor Antibodies
GACINH-IG – Goat anti human C1 Inhibitor, purified IgG (5mg vial)
GACINH-HRP – Goat anti human C1 Inhibitor, peroxidase conjugated IgG (0.2 mg vial)
GACINH-AP – Goat anti human C1 Inhibitor, affinity purified IgG (0.5 mg vial)
Description – C1-INH C1 Esterase Inhibitor
C1-INH is part of the serpin family of proteases, along with Alpha 1 Antitrypsin (A1AT) and Antithrombin III (AT-III). These proteins inactivate their target proteases by forming stable complexes with the protein that is inhibited. Synthesized primarily by hepatocytes, C1-INH is also synthesized by monocytes. The regulation of the protein production is not completely understood since patients respond clinically to androgen therapy serum levels of C1-INH increase. It is believed that androgens may stimulate C1-INH synthesis.
C1-INH deficient patients are heterozygous – half the normal level of C1-INH is insufficient to prevent attacks. C1 Esterase Inhibitor is named for its action on the first component of complement (C1 esterase) C1-INH also inhibits components of the fibrinolytic, clotting and kinin pathways. C1-INH inactivates plasmin-activated Factor XII, Factor XIa and kallikrein. Within the complement system C1-INH blocks the activation of C1 and the rest of the classic complement pathway by binding to C1r and C1s. Without C1-INH, unchecked activation of C1, C2, and C4 occur before other inhibitors (C4-binding protein and factor I) can halt the cascade. The actual factor or factors responsible for the edema formation remain somewhat controversial. Researchers have demonstrated activation of the kinin system and increased bradykinin concentration associated with clinical flares. Bradykinin is an important inflammatory mediator that causes neutrophil chemotaxis, capillary dilation, and smooth muscle relaxation, and it has been linked to other forms of angioedema. In an animal model of C1-INH deficiency, bradykinin antagonists prevent capillary leakage. Others implicate C2 kinin, a metabolite of C2b, as the active agent in the presence of plasmin.