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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: (BOSSBS-15458R-CY7)
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-11621R-HRP)
Supplier: Bioss
Description: The family of guanylin regulatory peptides, including guanylin and uroguanylin, are strongly expressed in intestinal mucosa and regulate intestinal fluid secretion during digestion. Guanylins are also involved in acid neutralization and the regulation of membrane-bound guanylate cyclase signaling molecules. Guanylin and uroguanylin are secreted primarily in the stomach, intestine, and colon. Guanylin is also detected in plasma. Guanylin is an endogenous activator of intestinal guanylate cyclase. It stimulates intestinal guanylate cyclase through the same receptor binding region as the heat-stable enterotoxins. Gut enterochromaffin cells synthesize guanylin to be a prohormone of 115 amino acids which is then is processed to the molecular form of 94 amino acids. This 10kDa form is found circulating in the blood.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11621R-FITC)
Supplier: Bioss
Description: The family of guanylin regulatory peptides, including guanylin and uroguanylin, are strongly expressed in intestinal mucosa and regulate intestinal fluid secretion during digestion. Guanylins are also involved in acid neutralization and the regulation of membrane-bound guanylate cyclase signaling molecules. Guanylin and uroguanylin are secreted primarily in the stomach, intestine, and colon. Guanylin is also detected in plasma. Guanylin is an endogenous activator of intestinal guanylate cyclase. It stimulates intestinal guanylate cyclase through the same receptor binding region as the heat-stable enterotoxins. Gut enterochromaffin cells synthesize guanylin to be a prohormone of 115 amino acids which is then is processed to the molecular form of 94 amino acids. This 10kDa form is found circulating in the blood.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7533R-CY5)
Supplier: Bioss
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.
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-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-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-9501R-A680)
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 synthesised 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: (70-0621-U100)
Supplier: Tonbo Biosciences
Description: The MEL-14 antibody is specific for mouse CD62L, also known as L-Selectin, a cell adhesion molecule which facilitates lymphocyte “rolling” on activated vascular endothelium and homing to high endothelial venules (HEV) as immune cells transmigrate from blood into peripheral tissues. L-Selectin is a member of a family of Selectin molecules which act together with the integrin family of adhesion molecules to mediate leukocyte-endothelial interactions. L-Selectin is characteristically expressed by neutrophils, and is also found on B cells, monocytes, granulocytes, and at varying levels on naive, effector and memory T cells. It is rapidly shed upon cell activation, releasing into the circulation a soluble form whose biological role is of particular interest in cancer biology research.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-15458R-A555)
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


Supplier: Tonbo Biosciences
Description: The MEL-14 antibody is specific for mouse CD62L, also known as L-Selectin, a cell adhesion molecule which facilitates lymphocyte “rolling” on activated vascular endothelium and homing to high endothelial venules (HEV) as immune cells transmigrate from blood into peripheral tissues. L-Selectin is a member of a family of Selectin molecules which act together with the integrin family of adhesion molecules to mediate leukocyte-endothelial interactions. L-Selectin is characteristically expressed by neutrophils, and is also found on B cells, monocytes, granulocytes, and at varying levels on naive, effector and memory T cells. It is rapidly shed upon cell activation, releasing into the circulation a soluble form whose biological role is of particular interest in cancer biology research.

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