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Catalog Number: (BOSSBS-5918R-A750)
Supplier: Bioss
Description: Angiopoietin-like protein 3 (Angptl3) functions as a potent lipoprotein lipase inhibitor and is an important component of plasma triglyceride homeostasis. Angptl3 also plays a role in adipose formation and angiogenesis through its interaction with integrin ?v)beta(3). It is secreted by the liver and is functionally defined by the C-terminal fibrinogen (FBN)-like domain and an N-terminal coiled-coil domain. Angptl3 regulates circulating triglyceride levels during different nutritional states thereby mediating the feeding/fasting cycle. A deficiency of Angptl3 results in abnormally low lipid levels, and a repression of the protein may be protective against atherosclerosis. Angptl3 may also play an important role in hyperlipidemia in diabetes.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11621R-CY7)
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-15458R)
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-A680)
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 Signalling 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 10 kDa form is found circulating in the blood.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10397R)
Supplier: Bioss
Description: This gene encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15458R-A750)
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-10397R-A555)
Supplier: Bioss
Description: This gene encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10339R-A680)
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


Catalog Number: (BOSSBS-9501R-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. 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-CY3)
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-HRP)
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-9756R-A750)
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.
UOM: 1 * 100 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: (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


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