Domain Structure of Protein Z
The domain structure of protein Z is represented , where GLA = the region containing γ-carboxyglutamic acid residues; EGF = the region containing sequences homologous to human epidermal growth factor; pseudo catalytic domain = region homologous to the catalytic chain of serine proteases which lacks the active site His and Ser residues normally conserved in the catalytic triad.

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  • Human Protein Z



    SKU: HCPZ-0220 Category:
    Price:$2,550.00/1 mg, $293.00/100 µg
    Size 1 mg, 100 µg
    Formulation 50% glycerol/water (v/v)
    Storage -20°C
    Shelf Life 12 months
    Purity >95% by SDS-PAGE
    Activity Determination N/A

Human protein Z (PZ) is a single chain, vitamin K-dependant plasma protein (1,2). Analogous with the majority of the coagulation proteins, protein Z is synthesized in the liver. The mature protein contains 360 amino acids (4). Based on amino acid sequence homology the domain structure is similar to that of other vitamin K-dependant zymogens which include; factor VII, factor IX, factor X, and protein C (3,4). The N-terminal region contains a carboxyglutamic acid (Gla) domain important in its phospholipid membrane binding ability (5). Following the N-terminal Gla domain are two EGF domains and a region which connects to a catalytic-like domain (3,4). The C-terminal region has been shown to lack the “typical” serine protease activation site as well as the His and Ser residues from the catalytic triad (3,4). Protease activity has not been detected in either the full-length protein or cleavage products of protein Z (2). Functionally protein Z has been shown to be a direct requirement for the binding of thrombin to endothelial phospholipids (6,7). Protein Z also serves as a cofactor for the inhibition of coagulation factor Xa by a plasma serpin called protein Z-dependant protease inhibitor (ZPI) (8). Inhibition is dependant upon complex formation between factor Xa-PZ-ZPI on the phospholipid surface (8).

The physiological function of protein Z is still rather ill defined. As is the case with other coagulation proteins and inhibitors, protein Z is consumed during disseminated intravascular coagulation (DIC) (9). Furthermore, patients diagnosed with a protein Z deficiency present with abnormal bleeding diathesis during and after surgical events (10). These findings provide direct evidence as to the importance of protein Z in blood coagulation.

Human protein Z is prepared from fresh frozen plasma similar to the procedure described by Broze and Miletich (2). The purified protein Z is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20oC. Purity is assessed by SDS-PAGE analysis.

Sample gel image
LoadHuman Protein Z, 1 µg per lane
StandardSeeBluePlus 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)
Plasma concentration2.7 µg/ml (11)
Mode of actionRequired for the binding of thrombin to phospholipid surfaces and for PZ dependant inhibition of factor Xa.
Molecular weight62,000 (2)
Extinction coefficient
1 %
1 c m, 280 nm
= 12.0 (2)
StructureSingle chain, (Mr=62,000), displays structural similarity to other vitamin K-dependant coagulation factors based on sequence homology, most notably factor X (3,4)
  1. Prowse, C.V. and Esnouf, M.P., Biochem. Soc. Trans., 5, 255 (1973).
  2. Broze, G.J. and Miletech, J.P., J. Clin. Invest.,73, 933, (1984).
  3. Ichinose, A. et al., Biochem. Biophysics Res. Comm., 173, 1139 (1990).
  4. Sejima, H. et al., Biochem. Biophysics Res. Comm., 171, 661 (1990). McDonald, J.F. et al., Biochem., 36, 5120 (1997).
  5. Hogg, P.J. and Stenflo, J., J. Biol. Chem., 266, 10953 (1991).
  6. Hogg, P.J. and Stenflo, J., Biochem. Biophysics Res. Comm., 17, 801 (1991).
  7. Han, X. et al., Biochem., 38, 11073 (1999).
  8. Kemkes-Matthes, B. et al., Onkologie, 18, 195 (1995).
  9. Kemkes-Matthes, B. and Matthes, K.J., Thromb. Res., 79, 49 (1995).
  10. Kemkes-Matthes, B. and Matthes, K.J., Biomed Progress, 13, 51 (2000).
  1. Rezaie, A., et al., J Biol Chem. 2005 September 23; 280(38): 32722–32728. (Binding to HSV1)

This publication list is not all encompassing, and is only meant to provide limited examples of how Prolytix 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.

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