antibody

Sheep anti-human Prothrombin (F.II), Affinity-Purified IgG

MBS512142

0.5 mg

365 USD

polyclonal

sheep

nonconjugated

Antibody

Sheep anti-human Prothrombin (F.II), Affinity-Purified IgG

Prothrombin

Prothrombin, human

Prothrombin; Prothrombin; prothrombin; serine protease; OTTHUMP00000197117; OTTHUMP00000233661; prothrombin B-chain; coagulation factor II (thrombin); Coagulation factor II

F2; F2; PT

THRB_HUMAN

Polyclonal

Sheep

This antibody is specific for prothrombin as demonstrated by immunoelectrophoresis and ELISA.

Affinity purified IgG. Vial containing ml of IgG purified by affinitychromatography on immobilized F.II. Total protein is 0.5 mg.

Affinity-purified IgG (APIgG), clear liquid.

APIgG concentration is mg/ml, determined by absorbance using an extinction coefficient (E1%280) of 13.4.

Store between -10 and -20 degree C. Product will become viscous but will not freeze. Avoid storage in frost-free freezers. Keep vial tightly capped. Allow product to warm to room temperature and gently mix before use.

Suitable as a source of enriched antibodies to human prothrombin.

Immunogen: Human prothrombin purified from plasma.

Buffer: 10 mM HEPES, pH 7.4, 150 mM NaCl, 50% (v/v) glycerol. Neutralizing Activity: Not determined

Prothrombin (factor II, F.II) is a vitamin K-dependent glycoprotein produced in the liver. The concentration of prothrombin in plasma is ~100 ug/ml (~1.4 uM). Prothrombin is a single chain molecule with a molecular weight of 72 kDa. Prothrombin consists of a catalytic domain followed by two kringle structures and an amino-terminal domain containing 10 gamma-carboxy-glutamic acid (gla) residues. These gla residues allow prothrombin to bind to membranes that contain acidic phospholipids in a calcium dependent manner. The binding to membranes is required for effective presentation of prothrombin as a substrate for activation by the prothrombinase complex, which consists of activated factor X, activated cofactor V and calcium on phospholipid membrane. Activation by prothrombinase occurs by sequential cleavage after residue Arg320 then after Arg271 to produce the active protease alpha-thrombin (37 kDa) and the byproduct prothrombin fragment 1.2 (35 kDa). The product thrombin further cleaves prothrombin fragment 1.2 after residue Arg155 into individual prothrombin fragments 1 and 2. The activity of alpha-thrombin in plasma is inhibited primarily by antithrombin and the rate of inhibition is accelerated 1000-fold in the presence of optimal concentrations of heparin. Other physiological inhibitors of thrombin in the absence of heparin include alpha2macroglobulin and alpha1antitrypsin1-3.

1. Mann KG; Prothrombin and Thrombin; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 184-199, J.B. Lippincott Co., Philadelphia PA, USA, 1994. 2. Mann KG; Prothrombin; Methods in Enzymology 45, pp 123-156, 1976. 3. Downing MW, Bloom JW, Mann KG; Comparison of the Inhibition of Thrombin by Three Plasma Protease Inhibitors; Biochemistry 17, pp 2649-2653, 1978.

135807

P00734.2

P00734

P00734

70,037 Da

Angiopoietin Receptor Tie2-mediated Signaling Pathway (137917); Blood Clotting Cascade Pathway (198840); Cell Surface Interactions At The Vascular Wall Pathway (106062); Class A/1 (Rhodopsin-like Receptors) Pathway (106357); Common Pathway (106060); Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); Diabetes Pathways (105902); FOXA2 And FOXA3 Transcription Factor Networks Pathway (137911)

Coagulation factor II is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. F2 also plays a role in maintaining vascular integrity during development and postnatal life. Mutations in F2 leads to various forms of thrombosis and dysprothrombinemia. [provided by RefSeq]

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. Ref.12. Catalytic activity: Selective cleavage of Arg- -Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. Subcellular location: Secreted extracellular space. Tissue specificity: Expressed by the liver and secreted in plasma. Post-translational modification: 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. Involvement in disease: Defects in F2 are the cause of factor II deficiency (FA2D) [. MIM:613679]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Ref.2 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40Genetic variations in F2 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [. 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. Ref.43Defects in F2 are a cause of susceptibility to thrombosis (THR) [. MIM:188050]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Ref.32 Ref.41. Pharmaceutical use: The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues. 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.It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting.Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.The cleavage after Arg-198, observed in vitro, does not occur in plasma. Sequence similarities: Belongs to the peptidase S1 family.Contains 1 Gla (gamma-carboxy-glutamate) domain.Contains 2 kringle domains.Contains 1 peptidase S1 domain.

0.5 mg

365 USD