Alpha-2-antiplasmin, also called Serpin F2, is a serine protease inhibitor (serpin) responsible for inactivating plasmin, and an important enzyme participates in fibrinolysis and degradation of other proteins. In liver cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of plasmin and an increase in fibrinolysis. Serpin F2 is major expressed on liver and kidney. Some other tissues such as muscle, intestine, central nervous system, and placenta also express Serpin F2 mRNA at a moderate level indicated that it is a key regulator of plasmin-mediated proteolysis in these tissues.

Alpha 2 Antiplasmin/SerpinF2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 53.2 kDa and the accession number is P08697-1.

Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense. Ceruloplasmin Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 35.4 kDa and the accession number is P00450.

Plasminogen Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.0 kDa and the accession number is P00747.

Alpha 2 Antiplasmin/SerpinF2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 53.6 kDa and the accession number is Q5ND36.

Alpha 2 Antiplasmin/SerpinF2 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 53.6 kDa and the accession number is Q68FT8.

the lymphangiogenic factors vascular endothelial growth factor C (VEGFC) and VEGFD are cleaved by thrombin and plasmin, serine proteases generated during hemostasis and wound healing. Genetic studies reveal that platelet enhancement of lymphatic growth after wounding is dependent on the release of VEGFC, but not VEGFD, a finding consistent with high expression of VEGFC in both platelets and avian thrombocytes. VEGFC Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.1 kDa and the accession number is Q6FH59.

Kininogen-1 is a secreted protein which contains three cystatin domains. There are two alternatively spliced forms, designated as the high molecular weight (HMW) and low MW (LMW) forms. Kininogen-1 plays a critical role in blood coagulation and inflammatory response. Kininogens are inhibitors of thiol proteases. Kininogen-1 participates in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII, also inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. The active peptide bradykinin that is released from Kininogen-1 shows a variety of physiological effects: influence in smooth muscle contraction, induction of hypotension, natriuresis and diuresis, decrease in blood glucose level. It is a mediator of inflammation and causes increase in vascular permeability, stimulation of nociceptors release of other mediators of inflammation. It has a cardioprotective effect. LMW-kininogen inhibits the aggregation of thrombocytes and doesn’t involved in blood clotting.

Alpha-1-antitrypsin 1-5(SERPIN A1) is a secreted protein and belongs to the serpin family. Serpins bind the protease active site resulting in a major conformational rearrangement that traps the enzyme in a covalent acyl-enzyme intermediate. Mouse SERPIN A1 is a serine protease inhibitor whose targets include elastase,plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema orliver disease. Several transcript variants encoding the same protein have been found for this gene.

Tissue-type plasminogen activator (PLAT) is a protein that secreted into extracellular space. PLAT contains five domains: EGF-like domain, fibronectin type-I domain, 2 kringle domains and peptidase S1 domain. It belongs to the peptidase S1 family. The main function of this protein is to convert plasminogen into biologically active plasmin. As a protease, PLAT plays a crucial role in regulating blood fibrinolysis, maintaining the homeostasis of extracellular matrix and in modulating the post-translational activation of growth factors. PLAT is found not only in the blood, where its primary function is as a thrombolytic enzyme, but also in the central nervous system (CNS). It participates in a number of physiological and pathological events in the CNS, as well as the role of neuroserpin as the natural regulator of PLAT's activity in these processes. Increased or decreased activity of PLAT leads to hyperfibrinolysis or hypofibrinolysis, respectively. In addition, as a cytokine, PLAT plays a pivotal role in the pathogenesis of renal interstitial fibrosis through diverse mechanisms. Thus, as a fibrogenic cytokine, it promotes the progression of kidney diseases.

Serpin A1a is also known as alpha-1-antitrypsin, is a member of the serpin superfamily of serine proteinase inhibitors that are involved in the regulation of a number of proteolytic processes. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin.

the lymphangiogenic factors vascular endothelial growth factor C (VEGFC) and VEGFD are cleaved by thrombin and plasmin, serine proteases generated during hemostasis and wound healing. Genetic studies reveal that platelet enhancement of lymphatic growth after wounding is dependent on the release of VEGFC, but not VEGFD, a finding consistent with high expression of VEGFC in both platelets and avian thrombocytes. VEGFC Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.1 kDa and the accession number is Q6FH59.

Serpin E2 is a member of the Serpin superfamily. It is differentially expressed during neuronal differentiation and is able to transform human embryonic kidney cells into neuronlike cells. Its over-expression in mice leads to progressive neuronal and motor dysfunction in these animals. It is also over-expressed in the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples whereas it is weakly expressed in all normal pancreas and chronic pancreatitis tissue samples. Serpin E2 is a potent inhibitor of thrombin, trypsin, urokinase, plasmin and plasminogen activators. It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from the onset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction.

Serpin B12 is a member of the serpin family. Serpins are the largest and most diverse family of serine protease inhibitors. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Serpin B12 is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. Serpins are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.

Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. uPAR/PLAUR Protein, Rat, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 34.1 kDa and the accession number is P49616.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Mouse SerpinB12 is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. It is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.

Carboxypeptidase B2 (CPB2) is a secreted enzyme that belongs to the peptidase M14 family. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen by the liver and circulates in the plasma as a plasminogen-bound zymogen. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides, such as kinins or anaphylatoxins, in the circulation regulating their activities. CPB2 also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. CPB2 exhibits carboxypeptidase activity when it is activated by proteolysis at residue Arg92 of the thrombin/thrombomodulin complex. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.

Protein AMBP belongs to the calycin superfamily and Lipocalin family. AMBP can be cleaved into three chains: α-1-microglobulin, inter-α-trypsin inhibitor light chain and trypstatin. AMBP is expressed by the liver and secreted in plasma. α-1-microglobulin occurs in many physiological fluids including the plasma, urine, and cerebrospinal fluid. Inter-α-trypsin inhibitor is present in the plasma and urine. α-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin, Inter-α-trypsin inhibitor inhibits trypsin, plasmin and lysosomal granulocytic elastase. Trypstatin act as a trypsin inhibitor, exists in a monomer forms and also occurs as a complex with tryptase in mast cells.

C-Type Lectin Domain Family 3 Member B (CLEC3B) is a serum and tissue protein and it contais a C-type lectin which binds to Ca++. CLEC3B is originally found in plasma, the concentrations approximately 10mg/l. It can bind to kringle 4 of plasminogen and enhance the activation of plaminogen to plasmin, catalyzed by tissue plasminogen activator in the presence of poly-D-lysine. In addition, CLEC3B may be involved in the packaging of molecules destined for exocytosis. Also, CLEC3B is best known as a prognostic marker in ovarian cancer.

Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease.

Transforming growth factor beta 3(TGFB3) is a member of a TGF -β superfamily which is defined by theirstructural and functional similarities. TGFB3 is secreted as a complex with LAP. This latent form of TGFB3becomes active upon cleavage by plasmin, matrix metalloproteases, thrombospondin -1, and a subset ofintegrins. It binds with high affinity to TGF- β RII, a type II serine/threonine kinase receptor. TGFB3 is involved incell differentiation, embryogenesis and development.It is believed to regulate molecules involved in cellularadhesion and extracellular matrix (ECM) formation during the process of palate development. Without TGF-β3,mammals develop a deformity known as a cleft palate.