|
 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.
PURCHASING
AND PRODUCT INFORMATION
|
Catalog
Number
HCPZ-0220 |
Description
Human
Protein Z |
Size
100
µg
|
Formulation
50%
glycerol/H2O (v/v)
|
|
Storage
-20oC |
Purity
>95%
by SDS-PAGE |
Activity
Determination
N/A |
Shelf
Life (properly stored)
12
months |
 |
Sample Gel
Information:
Gel:
Novex 4-12% Bis-Tris
Load:
Human Protein Z, 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)
|
|
Sample
publications referencing our Protein Z:
-
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 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. |
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U.S.
Pricing |
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inquiry |
SAMPLE
DATA SHEET |
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NOW! |
Overview
of Protein Z
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.
Properties
of Protein Z
| Localization: |
Plasma |
| Plasma concentration: |
2.7 µg/ml (11) |
| Mode of action: |
Required for the binding of thrombin to phospholipid surfaces
and for PZ dependant inhibition of factor Xa. |
| Molecular weight: |
62,000 (2) |
| Extinction coefficient: |
|
| Structure: |
Single chain,
(Mr=62,000), displays structural similarity to
other vitamin K-dependant coagulation factors based on sequence
homology, most notably factor X (3,4) |
PURCHASING
AND PRODUCT INFORMATION
References
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).
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