Human protein Z (PZ) is a single chain, vitamin K-dependent plasma protein.
Analogous with the majority of the coagulation proteins, protein Z is synthesized in the liver.
The mature protein contains 360 amino acids.
Based on amino acid sequence homology the domain structure is similar to that of other vitamin K-dependent zymogens which include factor VII, factor IX, factor X, and protein C.
The N-terminal region contains a carboxyglutamic acid (Gla) domain important in its phospholipid membrane binding ability.
Following the N-terminal Gla domain are two EGF domains and a region which connects to a catalytic-like domain.
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.
Protease activity has not been detected in either the full-length protein or cleavage products of protein Z.
Functionally protein Z has been shown to be a direct requirement for the binding of thrombin to endothelial phospholipids.
Protein Z also serves as a cofactor for the inhibition of coagulation factor Xa by a plasma serpin called protein Z-dependent protease inhibitor (ZPI).
Inhibition is dependent upon complex formation between factor Xa-PZ-ZPI on the phospholipid surface.
Applications:Suitable for use in ELISA and Western Blot.
Other applications not tested.
Recommended Dilutions:ELISA: 10ug/mlWestern Blot: 10ug/mlOptimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：1mg
Host：sheep
Source Antibody：human
Grade：Purified
Purity：Purified by salt fractionation followed by anion exchange. ≥95% by SDS-PAGE
Form：Supplied as a liquid in HEPES, 150mM sodium chloride, pH 7.4, 50% glycerol.
