NATURAL PROTEASE INHIBITORS
| Cat Num. | Product | Activity | PM (g/mol) | Formulation | Size |
|---|---|---|---|---|---|
| 9-HCII-0190 | Heparin Cofactor IIInhibits thrombin, alpha-chymotrypsin, Cathepsin G, protease B, Streptomyces griseus | 700 to 1 800 units/mg | 65 600 | 50/50 (v/v) glycerol/H₂O; 5 mM calcium chloride | 100 µg |
| 9-HCATIII-0120 | Human AntithrombinInactivates several serine proteinases | 0.7 to 1.0 mole thrombin / mole AT | 58 000 | 50/50 (v/v) glycerol/H₂O; 5 mM calcium chloride | 1 mg |
| 6-ATIII-10 | Human AntithrombinInactivates several serine proteinases | 10 UI | 58 000 | tampon/NaCl | 1.5 mg |
| 9-MCATIII-5120 | Mouse AntithrombinInactivates several serine proteinases | 0.6 to 1.0 mole thrombin / mole AT | 58 000 | 50/50 (v/v) glycerol/H₂O; 5 mM calcium chloride | 100 µg |
| 9-CTI-01 | Corn Trypsin InhibitorCTI is extracted from ground kernels of corn into a physiologic buffer. Preparations of CTI are tested for the ability to prolong the aPTT assay without affecting the PT assay. The specific activity of each lot of CTI is determined, and one unit is defined as the amount of CTI required to double the aPTT of normal human plasma. CTI inhibits FXIIa and trypsin. | 12 500 | 20 mM Tris; 150 mM NaCl; pH 7.4, < -70° C | 1 mg | |
| 9-TAFI-01 | Thrombin Activatable Fibrinolysis InhibitorAfter thrombin activation, the mature protein downregulates fibrinolysis. | 2.0 to 9.2 units/mg | 60 000 | 20 mM HEPES; 150 mM NaCl; pH 7.4 | 50 µg |
| 9-ANG-01 | Human AngiostatinInhibits the proliferation of endothelial cells | ≈ 50 000 | 20 mM HEPES; 0.15 M NaCl ; pH 7.4 | 500 µg | |
| 9-HA2AP-0230 | α2-Plasmin InhibitorPhysiological inhibitor of plasmin, forming an irreversible complex in its catalytic site; prevents binding of plasmin to fibrin. | 67 000 | 50 mM phosphate potassium; 7.5 mM KCl; 7.575 mM EDTA; pH 7.4 | 100 µg | |
| 8-800277 | AprotininAprotinin is a polyvalent reversible inhibitor of serine proteinases. Aprotinin Pentapharm can be used for the isolation of proteins as well as for biopharmaceutical downstream purification to inhibit undesired proteolytic activity of serine proteases such as trypsin, plasmin, trypsinogen, urokinase, chymotrypsin, kallikrein, elastase and others. It can also be used during immunodiffusion, radioimmunoassay or enzyme-linked immuno assay procedures. Aprotinin is used in chromogenic assays for the determination of antithrombin III, heparin, α2-macroglobulin, factor Xa and thrombin to inhibit disturbing kallikrein or plasmin activities. | Aprotinine lyophilized (1g/vial) | 6 512 | ≈ 6 M KIU/vial | 1 g |
| 8-073-70 | Aprotinin | Aprotinine solution (≈ 200 000 KIU/ml) | 6512 | M KIU | |
| 8-126-05 | R-HirudinThis recombinant protein is the most potent and specific thrombin inhibitor known. | 6963.5 | 2 000 ATU | ||
| 6-H7035-P01 | TFPI recombinantInhibits the factor VIIa and tissue factor in the complexe Xa/TFPI/FVIIa/TF, pH 8,0 | 0.04 µg/µl | 53 350 | 50 mM Tris-HCl; 10 mM glutathion | 50 µg |
| 9-HCPZ-0220 | Human Protein ZThe main role of protein Z appears to be the degradation of factor Xa. This is done by protein Z-related protease inhibitor (ZPI), but the reaction is accelerated 1000-fold by the presence of protein Z, phospholipids and Ca²+. | 62 000 | 50/50 (v/v) glycerol/H₂O; 5 mM CaCl₂ | 100 µg |
Inhibition constants Ki in μM of Pefabloc inhibitors
for serine proteinases
Description
Detection and determination of proteinases, studies on their interactions with substrates and effectors and the investigation of their physiological role are greatly facilitated by the use of proteinase inhibitors.
In this context, especially synthetic, low-molecular weight inhibitors of different selectivity are very useful. They are widely applied during purification and characterization of proteinases.
Furthermore, synthetic inhibitors are useful tools for suppression of undesired proteolytic activity. Depending upon the manner in which the inhibitor is attached to the enzyme, one distinguishes reversible and irreversible inhibitors.
Characteristics
Pentapharm offers a selection of inhibitors derived from benzamidine. They can help in the characterization of trypsin-like enzymes.
Most Pefablocs® exhibit a selective inhibitory activity on certain trypsin-like proteinases of physiological relevance. However, each inhibitor will of course display a characteristic action on other serine proteinases (see table on Ki-values page 47).
Advantages
Supplied lyophilized or frozen
Expiry date > 1 year
Glass vial or plastic tubes
Discount according to quantities
Notice
 | 8-126-05 |
PDF Catalogue
 |
INHIBITORS |
