Search results for: MOUSE & RAT CLOTTING FACTORS Rat Factor IXa
#31320079 2019/06/27 To Up
Highly purified fucosylated chondroitin sulfate oligomers with selective intrinsic factor Xase complex inhibition.
Fucosylated chondroitin sulfate (FCS) oligosaccharides of specific molecular weight have shown potent anticoagulant activities with selectivity towards intrinsic factor Xase complex. However, the preparation of FCS oligosaccharides by traditional methods requires multiple purification steps consuming large amounts of time and significant resources. The current study focuses on developing a method for the rapid preparation of FCS oligomers from sea cucumber Pearsonothuria graeffei having 6-18 saccharide residues. The key steps controlling molecular weight (Mw) and purity of these FCS oligomers were evaluated. Structural analysis showed the resulting FCS oligomers were primarily l-Fuc3,4diS-α1,3-d-GlcA-β1,3-(d-GalNAc4,6diS-β1,4-[l-Fuc3,4diS-α1,3-]d-GlcA-β1,3-)d-anTal-ol4,6diS (n = 1˜5) accompanied by partial de-fucosylation and/or de-sulfation. In vitro and in vivo experiments demonstrate that these FCS oligomers selectively inhibit intrinsic factor Xase complex and exhibit remarkable antithrombotic activity without hemorrhagic and hypotension side effects. This method is suitable for large-scale preparation of FCS oligosaccharides as clinical anticoagulants.Lufeng Yan, Danli Wang, Mengshan Zhu, Yanlei Yu, Fuming Zhang, Xingqian Ye, Robert J Linhardt, Shiguo Chen
2443 related Products with: Highly purified fucosylated chondroitin sulfate oligomers with selective intrinsic factor Xase complex inhibition.
100ug Lyophilized100ug Lyophilized1mg1mg1. KU100ug Lyophilized0.1 ml100ug Lyophilized100ug Lyophilized10 100ug Lyophilized0.1 mlRelated Pathways
#10595635 // To Up
An inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis.
An inhibitory anti-factor IX/IXa antibody (BC2) has been investigated as an anti-thrombotic agent in a rat venous thrombosis model. The treatment of rats post-injury with a single bolus dose of BC2 (3 mg/kg, i.v.) resulted in an approximately 4 fold reduction in venous thrombus mass (P = 0.043). This efficacy was matched by a minimal (<2.5 fold) prolongation of the aPTT and had no effect on the prothrombin time (PT). Heparin by comparison, given as a bolus followed by continuous infusion, at doses comparable in efficacy at reducing thrombus formation, prolonged the aPTT >50 fold. These results demonstrate that the anti-factor IX/IXa antibody (BC2), when compared to heparin, can effectively reduce venous thrombosis with less disruptive consequences on blood clotting.G Z Feuerstein, J R Toomey, R Valocik, P Koster, A Patel, M N Blackburn
2299 related Products with: An inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis.
100.00 ug100ul 100 UG100ug100ug100ug100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug100ug LyophilizedRelated Pathways
#9493581 // To Up
Cloning, expression, and characterization of mouse tissue factor pathway inhibitor (TFPI).
Tissue factor pathway inhibitor (TFPI) acts to regulate the initiation of coagulation by first inhibiting factor Xa. The complex of factor Xa/TFPI then inhibits the factor VIIa/tissue factor complex. The cDNA sequences of TFPI from several different species have been previously reported. A high level of similarity is present among TFPIs at the molecular level (DNA and protein sequences) as well as in biochemical function (inhibition of factor Xa, VIIa/tissue factor). In this report, we used a PCR-based screening method to clone cDNA for full length TFPI from a mouse macrophage cDNA library. Both cDNA and predicted protein sequences show significant homology to the other reported TFPI sequences, especially to that of rat. Mouse TFPI has a signal peptide of 28 amino acid residues followed by the mature protein (in which the signal peptide is removed) which has 278 amino acid residues. Mouse TFPI, like that of other species, consists of three tandem Kunitz type domains. Recombinant mouse TFPI was expressed in the human kidney cell line 293 and purified for functional assays. When using human clotting factors to investigate the inhibition spectrum of mouse TFPI, it was shown that, in addition to human factor Xa, mouse TFPI inhibits human factors VIIa, IXa, as well as factor XIa. Cloning and expression of the mouse TFPI gene will offer useful information and material for coagulation studies performed in a mouse model system.J Y Chang, D M Monroe, J A Oliver, D K Liles, H R Roberts
2740 related Products with: Cloning, expression, and characterization of mouse tissue factor pathway inhibitor (TFPI).
100 μg100.00 ug100.00 ug100ug1 mg1 kit(96 Wells)1 mL2ug1 kit(96 Wells)1mgRelated Pathways
#6974212 // To Up
Thrombogenicity of antihemophiliac preparations with factor VIII inhibitor bypassing activity.
D J Melewski, J Huebschmann, K Tourbaf, C M Ambrus, J L Ambrus
2808 related Products with: Thrombogenicity of antihemophiliac preparations with factor VIII inhibitor bypassing activity.
100ug100ug100ug250IU100ug1 ml60 IU5 100ug Lyophilized100ug Lyophilized100ugRelated Pathways
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