Thermo Fisher Scientific Human Protein Z Native Protein

Applications

Tested Dilution

Publications

Control (Ctrl)

Assay-dependent

-

Product Specifications

Species

Human

Molecular weight

62 kDa

Class

Native

Type

Protein

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Purification

SDS-PAGE

Storage buffer

50% water with 50% glycerol

Contains

no preservative

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

Product Specific Information

RP-43134 contains native human Protein Z protein.

RP-43134 may be used as a positive control in many immunological assays.

The product is of human blood/plasma origin. Although the starting material was tested prior to initiation of the manufacturing process, and was found negative or nonreactive for anti-HIV-1/2, HIV-1 antigen(s), HBsAg, STS, anti-HCV, anti-HBcore and anti-HTLV I & II, extreme caution should be used when handling this material as there is a margin of error in all tests.

This product is to be used for IN VITRO research purposes only, and is not intended for clinical or diagnostic use!

Target Information

PROZ protein Z, vitamin K-dependent plasma glycoprotein. It is 62 kDa large and 396 amino acids long. It has four domains: a gla-rich region, two EGF-like domains and a trypsin-like domain. It lacks the serine residue that would make it catalytically active as a serine protease. It is a member of the coagulation cascade, the group of blood proteins that leads to the formation of blood clots. It is vitamin K-dependent, and its functionality is therefore impaired in warfarin therapy. It is a glycoprotein. Although it is not enzymatically active, it is structurally related to several serine proteases of the coagulation cascade: factors VII, IX, X and protein C. The carboxyglutamate residues (which require vitamin K) bind protein Z to phospholipid surfaces. The main role of protein Z appears to be the degradation of factor Xa. This is done by protein Z-related protease inhibitor (ZPI), but the reaction is accelerated 1000-fold by the presence of protein Z. Oddly, ZPI also degrades factor XI, but this reaction does not require the presence of protein Z. In some studies, deficiency states have been associated with a propensity to thrombosis. Others, however, link it to bleeding tendency; there is no clear explanation for this, as it acts physiologically as an inhibitor, and deficiency would logically have led to a predisposition for thrombosis.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.