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Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation. Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesised in the liver and circulates as an inactive precursor. Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds. Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease.
Catalog Number: BOSSBS-9500R-A680
UOM: 1 * 100 µl
Supplier: Bioss


Description: Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD26 (ankyrin repeat domain-containing protein 26) is a 1709 amino acid protein that contains five ANK repeats. Expressed at high level in many tissues, including brain, liver, kidney and heart, ANKRD26 may be phosphorylated upon DNA damage by Atm or ATR. ANKRD26 is also expressed in the arcuate and ventromedial nuclei within the hypothalamus and in the ependyma and the circumventricular organs that act as an interface between the peripheral circulation and the brain. It is suggested that alterations in the gene encoding ANKRD26 may lead to obesity. Three isoforms of ANKRD26 exists due to alternative splicing events.
Catalog Number: BOSSBS-9755R-A680
UOM: 1 * 100 µl
Supplier: Bioss


Description: Fc (Ig constant fragment) receptors ensure protection of the host against foreign antigens, such as microorganisms and pathogens, by removing Ig-coated antigen complexes from circulation. Fc receptors are present on lymphoid and myeloid derivatives, where they mediate endocytosis of Ig-antigen complexes, antibody production in B cells through T cell antigen presentation, cytotoxicity and the release of cytokines and reactive oxygen species. The Fc γ-binding protein (FCGBP) interacts with the Fc portion of IgG and MUC2 to mediate the maintenance of the mucosal structure. FCGBP is a 5,405 amino acid protein that contains twelve TIL (trypsin inhibitory-like) domains and thirteen VWFD domains. It is predominantly expressed in placenta and colon epithelium as well as in thyroid and serum. Patients with various autoimmune diseases seemingly have higher levels of FCGBP protein present in their serum.
Catalog Number: BOSSBS-13168R-A488
UOM: 1 * 100 µl
Supplier: Bioss


Description: The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Lewis blood group antigens are carbohydrate moieties structurally integrated in mucous secretions. Lewis antigen system alterations have been described in gastric carcinoma and associated lesions. Anomalous expression of Lewis B antigen has been found in some non-secretory gastric carcinomas and colorectal cancers.
Catalog Number: BNC401008-500
UOM: 1 * 500 µl
Supplier: Biotium


Description: The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Lewis blood group antigens are carbohydrate moieties structurally integrated in mucous secretions. Lewis antigen system alterations have been described in gastric carcinoma and associated lesions. Anomalous expression of Lewis B antigen has been found in some non-secretory gastric carcinomas and colorectal cancers.
Catalog Number: BNC041008-100
UOM: 1 * 100 µl
Supplier: Biotium


Description: Lipin 1 is a member of the Lipin family of nuclear proteins. This family contains three members: Lipin 1, Lipin 2 and Lipin 3, all of which contain a nuclear signal sequence, a highly conserved amino-terminal (NLIP) domain and a carboxy-terminal (CLIP) domain. LPIN1 (Lipin 1) is crucial for normal adipose tissue development and metabolism. LPIN1 selectively activates a subset of PGC1 alpha target pathways, including fatty acid oxidation and mitochondrial oxidative phosphorylation by inducing expression of the nuclear receptor PPARalpha. LPIN1 also inactivates the lipogenic program and suppresses circulating lipid levels. An abundance of LPIN1 promotes fat accumulation and insulin sensitivity, whereas a deficiency in LPIN1 may deter normal adipose tissue development, resulting in insulin resistance and lipodystrophy, a heterogeneous group of disorders characterized by loss of body fat, fatty liver, hypertriglyceridemia and insulin resistance.
Catalog Number: BOSSBS-7533R-CY5.5
UOM: 1 * 100 µl
Supplier: Bioss


Description: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.
Catalog Number: BOSSBS-7547R
UOM: 1 * 100 µl
Supplier: Bioss


Description: Follicular dendritic cells are cells that facilitate antigen recognition by B cells in follicles. This kind of dendritic cell is not bone marrow derived and is not a kind of blood cell. It is purely a resident of the follicles of secondary lymphoid organs. B cells form germinal centers around follicular dendritic cells in lymphoid organs. Dendritic cells form from monocytes, white blood cells which circulate in the body and, depending on the right signal, can turn into dendritic cells or macrophages. The monocytes in turn are formed from stem cells in the bone marrow.In normal tissue this antibody identifies dendritic cells and a proportion of B lymphocytes. Evidence in pathological tissue and functional studies suggests it binds to an epitope expressed by antigen presenting cells. Within the macrophage/dendritic cell populations the epitope seen by RFD1 is coexpressed with RFD7 by a subset of cells that exhibit suppressive activity on T cell stimulation.
Catalog Number: BOSSBS-1766R-A350
UOM: 1 * 100 µl
Supplier: Bioss


Description: Follicular dendritic cells are cells that facilitate antigen recognition by B cells in follicles. This kind of dendritic cell is not bone marrow derived and is not a kind of blood cell. It is purely a resident of the follicles of secondary lymphoid organs. B cells form germinal centers around follicular dendritic cells in lymphoid organs. Dendritic cells form from monocytes, white blood cells which circulate in the body and, depending on the right signal, can turn into dendritic cells or macrophages. The monocytes in turn are formed from stem cells in the bone marrow.In normal tissue this antibody identifies dendritic cells and a proportion of B lymphocytes. Evidence in pathological tissue and functional studies suggests it binds to an epitope expressed by antigen presenting cells. Within the macrophage/dendritic cell populations the epitope seen by RFD1 is coexpressed with RFD7 by a subset of cells that exhibit suppressive activity on T cell stimulation.
Catalog Number: BOSSBS-1766R-CY3
UOM: 1 * 100 µl
Supplier: Bioss


Description: Immunodensity isolation of untouched circulating tumor cells.
Catalog Number: STMC15137
UOM: 1 * 1 KIT
Supplier: STEMCELL Technologies


Description: 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.
Catalog Number: PRSI91-483
UOM: 1 * 50 µG
Supplier: ProSci Inc.


Description: The complement pathway is an important host defense system that contributes to both innate and acquired immunity. There are three pathways of complement activation: the classical pathway, lectin pathway and alternative pathway. Complement protein Factor I is a key serine protease that modulates the complement cascade by regulating the levels of C3 convertases. It circulates in plasma as a heavily N-glycosylated heterodimer made up of two disulfide linked chains, each carrying three N-linked oligosaccharide chains that may have both structural and functional roles in the interactions with the natural substrate and the cofactor during catalysis. Factor I is a serine protease with a high degree of specificity for C3b and C4b. It requires protein cofactors for cleavage of these complement proteins; Factor H, CR1 or MCP are required for C3b cleavage, and C4bp or CR1 are required for C4b cleavage.
Catalog Number: BOSSBS-13131R-A680
UOM: 1 * 100 µl
Supplier: Bioss


Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).
Catalog Number: BOSSBS-9500R-A488
UOM: 1 * 100 µl
Supplier: Bioss


Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).
Catalog Number: BOSSBS-9500R-A647
UOM: 1 * 100 µl
Supplier: Bioss


Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation. Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesised in the liver and circulates as an inactive precursor. Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds. Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease.
Catalog Number: BOSSBS-9500R-A750
UOM: 1 * 100 µl
Supplier: Bioss


Description: Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD26 (ankyrin repeat domain-containing protein 26) is a 1709 amino acid protein that contains five ANK repeats. Expressed at high level in many tissues, including brain, liver, kidney and heart, ANKRD26 may be phosphorylated upon DNA damage by Atm or ATR. ANKRD26 is also expressed in the arcuate and ventromedial nuclei within the hypothalamus and in the ependyma and the circumventricular organs that act as an interface between the peripheral circulation and the brain. It is suggested that alterations in the gene encoding ANKRD26 may lead to obesity. Three isoforms of ANKRD26 exists due to alternative splicing events.
Catalog Number: BOSSBS-9755R-A750
UOM: 1 * 100 µl
Supplier: Bioss


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