site map  

 

 

 

 

 

 

 


QUESTIONS?

+1 (802) 878-1777

hti@haemtech.com


 

 

 

 

 

 

 

 

ORDERING

Human Proteins

Bovine Proteins

Mouse Proteins

Other Species

Inhibitors

Substrates

Antibodies

Sample Collection Tubes

Deficient Plasmas

Assay Kits

Pricing

HOME PAGE

 

 

 

 

 

 

 

 

QUESTIONS?

+1 (802) 878-1777

hti@haemtech.com

 

 Coagulation Factor X

DOMAIN STRUCTURE OF FACTOR X The domain structure of factor X is represented, where: GLA = region containing γ-carboxyglutamic acid residues, EGF = region containing sequences homologous to human epidermal growth factor, AP = activation peptide released upon conversion of the zymogen to the active serine protease, CATALYTIC DOMAIN = region containing the serine protease catalytic triad. The arrow indicates the site which is proteolytically cleaved by factor Xase during activation of the zymogen.

 

PURCHASING AND PRODUCT INFORMATION

 

Catalog Number

HCX-0050

HCX-GD

BCX-1050

MCX-5050

Description

Human Factor X

Human gla-domainless X

Bovine Factor X

Mouse Factor X

Size

100 g

100 g

100 g

100 g

Formulation

50% (vol/vol) glycerol/H2O

same

same

same

Storage

-20oC

Purity

>95% by SDS-PAGE

NOT tissue/cell culture grade

Activity Determination

Clotting assay

Shelf Life (properly stored)

12 months

Sample Gel Information:

Gel: Novex 4-12% Bis-Tris

Load: Human Factor X, 1 g 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)

 

Sample publications referencing our Factor X:

  1. Livingston, J., et al., Biochem. J. (2006) 393, 529535 (Binding to HSV1)

  2. Yang, Y., et al., J Immunol. 2006 December 1; 177(11): 8219 8225. (Used as capture antigen in ELISA)

  3. Zaiss A.K., Lawrence R., Elashoff D., Esko J.D., and Herschman H.R. (2011). Differential effects of murine and human Factor X on adenovirus transduction via cell surface heparan sulfate. Journal of Biological Chemistry Jul 15;286(28):24535-43. 

This publication list is not all encompassing, and is only meant to provide limited examples of how Haematologic Technologies' products are used.  We encourage you to search the literature for other examples pertinent to your experimentation, and to contact us with any technical questions.

U.S. Pricing

Product inquiry

SAMPLE DATA SHEET

ORDER NOW!

Overview of Factor X

Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond (1,2). Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, factor VIIIa, cellular surface and calcium ions) or the extrinsic factor Xase complex (factor VIIa, tissue factor, cellular surface and calcium ions). Activation of human factor X by either complex results in cleavage at Arg52-Ile53 of the COOH-terminal heavy chain and subsequent release of a 52 amino acid activation glycopeptide. Factor Xa then serves as the enzyme component of the prothrombinase complex which is responsible for the rapid conversion of prothrombin to thrombin. The gla residues enable factor X/Xa to bind phospholipid (i.e. cell surfaces) in a calcium dependent manner; a requirement for assembly of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other (12). This region of the molecule is involved in the recognition of cellular binding domains. 


Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques (3) and immunoaffinity chromatography (4). In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. (5,6). The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20oC. Purity is determined by SDS-PAGE analysis and activity is measured in a factor X clotting assay. 

Properties of Factor X

Localization: Plasma
Plasma concentration: 10 g/ml
Mode of action: Zymogen; precursor to the serine protease factor Xa
Molecular weight: 58,900 (human) (7)
55,100 (bovine) (8)
Extinction coefficient:
E
1 %
1 c m, 280 nm
= 11.6 (human) (9)
= 12.4 (bovine) (10)
Isoelectric point: 4.9-5.2 (human) (9)
4.8-5.2 (bovine) (9)
Structure: two subunits, Mr=16,200 and 42,000 (human), Mr=16,500 and 39,300 (bovine), NH2-terminal gla domain, and two EGF domains
Percent carbohydrate: 15 % (human) (7)
10 % (bovine) (8)
Post-translational modifications: eleven gla residues (7,8)
one β-hydroxyaspartate

References 
1. Davie, E.W., et al., Adv. Enzymol., 48, 277 (1979). 
2. Jackson, C.M., Ann. Rev. Biochem., 49, 765 (1980). 
3. Bajaj, S.P., et al., Prep. Biochem., 11, 397 (1981). 
4. Church, W.R., et al., Thrombosis Res., 38, 417 (1985). 
5. Bajaj, S.P., et al., J. Biol. Chem., 248, 7729 (1973). 
6. Krishnaswamy, S., et al., J. Biol. Chem., 261, 8997 (1986). 
7. Fujikawa, K., et al., Biochemistry, 11, 4882 (1972). 


 

PRODUCTS ORDERING SERVICES ABOUT US TECH NOTES CONTACT

 

© 2009 Haematologic Technologies, Inc. All Rights Reservedspacer