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Catalog Number: (BOSSBS-15458R-A350)
Supplier: Bioss
Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1914R-CY7)
Supplier: Bioss
Description: Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1914R-CY3)
Supplier: Bioss
Description: Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10339R)
Supplier: Bioss
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.
UOM: 1 * 100 µl


Supplier: DWK Life Sciences
Description: The DURAN® borosilicate glass 3.3, double-walled, wide mouth bottles GLS 80® incorporate an integral jacket that isolates the contents from the external environment. Heated or cooled liquids can be circulated through the jacket to control the temperature within a screw topped bottle. Double-walled bottles offer a sealable and more flexible alternative to open topped jacketed beakers.

Catalog Number: (BOSSBS-9500R-CY7)
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).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9501R-A488)
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 X (Stuart Prower factor, FX, F10) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor. The mature form of Factor X (Factor X A) is generated by Factor IX A- or Factor VII A-mediated cleavage at the tripeptide sequence, Arg-Lys-Arg, to yield a disulfide linked dimer. Together with the cofactor Factor V A and Ca2+ on the surface of platelets or endothelial cells, Factor X A coordinates as part of the prothrombinase complex, which mediates proteolysis of Prothrombin into active Thrombin. Mutations at the Factor X locus resulting in Factor X deficiencies can contribute to hemorrhagic diathesis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9501R-A555)
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 X (Stuart Prower factor, FX, F10) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor. The mature form of Factor X (Factor X A) is generated by Factor IX A- or Factor VII A-mediated cleavage at the tripeptide sequence, Arg-Lys-Arg, to yield a disulfide linked dimer. Together with the cofactor Factor V A and Ca2+ on the surface of platelets or endothelial cells, Factor X A coordinates as part of the prothrombinase complex, which mediates proteolysis of Prothrombin into active Thrombin. Mutations at the Factor X locus resulting in Factor X deficiencies can contribute to hemorrhagic diathesis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9500R-A350)
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).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9500R-A555)
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).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13168R-CY7)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13168R-A555)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1914R-A750)
Supplier: Bioss
Description: Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognise a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.
UOM: 1 * 100 µl


Supplier: Biotium
Description: This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.

Supplier: Biotium
Description: This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.

Supplier: Biotium
Description: This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.

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