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Antithrombin III

DOMAIN STRUCTURE OF ANTITHROMBIN III Antithrombin III contains three intra-chain disulfide bonds (-S-S-), a carbohydrate rich domain (CHO), an NH₂-terminal heparin binding domain, and a COOH-terminal serine protease binding domain.

PURCHASING AND PRODUCT INFORMATION

Catalog Number HCATIII-0120 MCATIII-5120*	Description Human Antithrombin III Mouse Antithrombin III	Size 1 mg 100 µg	Formulation 50% (vol/vol) glycerol/H2O 50% (vol/vol) glycerol/H2O
Storage -20oC	Purity >95% by SDS-PAGE	Activity Determination Thrombin inhibition	Shelf Life (properly stored) 12 months
	Sample Gel Information: Gel: Novex 4-12% Bis-Tris Load: Human ATIII, 1 µg per lane Buffer: MOPS Standard: SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)
U.S. Pricing	Product inquiry	SAMPLE DATA SHEET	ORDER NOW!

*Due to mouse plasma quality issues our mouse proteins are not being sold until further notice.  At the present time we cannot give a completion date.  Thank you.

Overview of Antithrombin III

Antithrombin III (ATIII) is a single chain glycoprotein with a molecular weight of 58,000. It is a member of the serpin (serine protease inhibitor) super family and is considered to be the most important inhibitor in the coagulation cascade (1,2). ATIII inhibits a wide spectrum of serine proteases including thrombin, factors IXa, Xa and XIa, kallikrein, plasmin, urokinase, C1-esterase, and trypsin. The mechanism of inhibition involves the formation of a stable 1:1 complex between the active site of the protease and the scissile bond (Arg 385-Ser 386) of ATIII. The active site serine of thrombin has been shown to form a covalent intermediate with the P1 amino acid (Arg 385) of ATIII. The rate of inhibition of serine proteases by ATIII is increased to varying degrees by heparin. In the case of being a thrombin inhibitor or factor Xa inhibitor, the interaction with ATIII is enhanced 3 orders of magnitude in the presence of heparin. The interaction between ATIII and heparin involves a unique sequence of sulfated and non-sulfated monosaccharide units on heparin, and critical lysine residues on ATIII. The binding of ATIII to heparinoid structures on vascular endothelium has been demonstrated and shown to enhance the inhibition of factors IXa, Xa, and thrombin. 

ATIII may also function in the complement cascade. The binding of ATIII to fluid phase complement attack-complexes in sera has been demonstrated. In addition, the S protein of complement (an inhibitor of the membrane attack-complex) interferes with the ATIII/thrombin interaction. 

ATIII is prepared from fresh frozen plasma by heparin-agarose affinity chromatography (3). The purified protein is supplied in 50% (vol/vol) glycerol/H₂O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis. 

Properties of Antithrombin III (thrombin inhibitor)

PURCHASING AND PRODUCT INFORMATION

References 

1. Griffith, M.J., In Blood Coagulation, ed. R.F.P. Zwaal, H.C. Hemker, pp. 259-283, Amersterdam: Elsevier, 1986. 
2. Rosenberg, R.D., et al., J. Clin. Invest., 74, 1 (1984). 
3. Damus, P.S. and Rosenberg, R.D., Methods Enzymol., 45, 653-69 (1976). 
4. Petersen, T.E., et al., In The Physiological Inhibitors of Coagulation and Fibrinolysis, ed. D. Collen, M. Verstrate, pp. 43-54, 5. Amsterdam: Elsevier, 1979. 
5. Nordenman, B., et al., J. Biochem., 78, 195 (1977). 
6. Conrad, J., et al., Hemostasis, 13, 363 (1983). 
7. Kurachi, W., et al., Biochemistry, 15, 368 (1976).