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Cleaved Thrombin APII (Arg327) Cell-Based Colorimetric ELISA Kit

-KA3977C

Catalog: KA3977C
Size
Price
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96well
$330.00
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Main Information
Reactivity

Human

Applications

ELISA

Conjugate/Modification


Unmodified

Detailed Information
Storage
2-8°C/6 months
Modification
Unmodified
Detection Method
Colorimetric
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Antigen&Target Information
Gene Name:
F2
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Other Name:
Prothrombin ;
Coagulation factor II ;
[Cleaved into: Activation peptide fragment 1 ;
Activation peptide fragment 2 ;
Thrombin light chain ;
Thrombin heavy chain]
show all
Database Link:
Organism Gene ID SwissProt
Human 2147; P00734;
Mouse P19221;
Background:
catalytic activity:Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.,disease:Defects in F2 are the cause of various forms of dysprothrombinemia [MIM:176930].,disease:Genetic variations in F2 may be a cause of susceptibility to ischemic stroke [MIM:601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.,function:Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.,miscellaneous:It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting.,miscellaneous:Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.,miscellaneous:The cleavage after Arg-198, observed in vitro, does not occur in plasma.,miscellaneous:Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.,online information:Thrombin entry,pharmaceutical:The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.,PTM:The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.,similarity:Belongs to the peptidase S1 family.,similarity:Contains 1 Gla (gamma-carboxy-glutamate) domain.,similarity:Contains 1 peptidase S1 domain.,similarity:Contains 2 kringle domains.,tissue specificity:Expressed by the liver and secreted in plasma.,
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Function:
protein import into nucleus, translocation, cell activation, regulation of protein amino acid phosphorylation, positive regulation of protein amino acid phosphorylation, acute inflammatory response, protein amino acid phosphorylation,proteolysis, protein targeting, protein import into nucleus, phosphorus metabolic process, phosphate metabolic process, ion transport, cation transport, calcium ion transport, cellular ion homeostasis, cellular calcium ion homeostasis, cellular metal ion homeostasis, intracellular protein transport, nucleocytoplasmic transport, apoptosis,activation of caspase activity, defense response, acute-phase response, inflammatory response, cell surface receptor linked signal transduction, elevation of cytosolic calcium ion concentration, intracellular signaling cascade, protein kinase cascade, JAK-STAT cascade, tyrosine phosphorylation of STAT protein, STAT protein nuclear translocation, blood coagulation, hemostasis, protein localization, cell death, response to wounding, positive regulation of biosynthetic process, regulation of calcium ion transport into cytosol, positive regulation of calcium ion transport into cytosol,positive regulation of macromolecule biosynthetic process, positive regulation of phosphorus metabolic process,positive regulation of macromolecule metabolic process, regulation of collagen metabolic process, positive regulation of collagen metabolic process, regulation of cell death, positive regulation of peptidase activity, regulation of metal ion transport, programmed cell death, protein transport, di-, tri-valent inorganic cation transport, death, phosphorylation,protein import, peptidyl-tyrosine phosphorylation, peptidyl-tyrosine modification, regulation of phosphate metabolic process, cellular homeostasis, metal ion transport, cellular cation homeostasis, cellular di-, tri-valent inorganic cation homeostasis, platelet activation, regulation of blood coagulation, positive regulation of blood coagulation, negative regulation of blood coagulation, regulation of protein modification process, positive regulation of protein modification process, regulation of response to external stimulus, regulation of cellular protein metabolic process, positive regulation of cellular protein metabolic process, regulation of homeostatic process, positive regulation of homeostatic process, regulation of collagen biosynthetic process, positive regulation of collagen biosynthetic process, protein localization in organelle, protein localization in nucleus, cellular protein localization, wound healing, regulation of phosphorylation, positive regulation of phosphorylation, homeostatic process, fibrinolysis, regulation of apoptosis,regulation of programmed cell death, positive regulation of catalytic activity, regulation of ion transport, positive regulation of ion transport, positive regulation of caspase activity, regulation of caspase activity, positive regulation of molecular function, regulation of multicellular organismal metabolic process, positive regulation of multicellular organismal metabolic process, establishment of protein localization, positive regulation of phosphate metabolic process, intracellular transport, chemical homeostasis, ion homeostasis, coagulation, regulation of coagulation,negative regulation of coagulation, positive regulation of coagulation, regulation of body fluid levels, positive regulation of transport, nuclear transport, nuclear import, regulation of phosphorus metabolic process, release of sequestered calcium ion into cytosol, positive regulation of multicellular organismal process, negative regulation of multicellular organismal process, positive regulation of protein metabolic process, regulation of release of sequestered calcium ion into cytosol, positive regulation of release of sequestered calcium ion into cytosol, regulation of sequestering of calcium ion, negative regulation of sequestering of calcium ion, regulation of hydrolase activity,positive regulation of hydrolase activity, cytosolic calcium ion homeostasis, regulation of calcium ion transport, positive regulation of calcium ion transport, regulation of peptidase activity, regulation of endopeptidase activity, metal ion homeostasis, di-, tri-valent inorganic cation homeostasis, calcium ion homeostasis, cation homeostasis, cellular chemical homeostasis, cytosolic calcium ion transport, calcium ion transport into cytosol, cellular macromolecule localization,
show all
Cellular Localization:
Secreted, extracellular space.
show all
Tissue Expression:
Expressed by the liver and secreted in plasma.
show all
Catalog: KA3977C
Size
Price
Status
Qty.
96well
$330.00
In stock

0

Add to cart

Collected

Collect

Customized Service

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