serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 10 (SERPINA10) ELISA Kits

Human serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 10 (SERPINA10) interaction partners

1. PZ/ZPI polymorphisms do not appear to play an active role in the development of prosthesis heart valve thrombosis.

2. Data suggest oxidized lipid vesicles with phosphatidylserine/polyunsaturated fatty acids promote inactivation of ZPI-PZ complex or free ZPI; binding of PZ-complexed or free ZPI to oxidized vesicles mediates inactivation of ZPI (an inhibitor of FXa); blocking heparin- (anticoagulant-)binding site on ZPI interferes with binding to lipid or PZ. (ZPI = protein Z-dependent protease inhibitor; PZ = protein Z; FXa = factor Xa)

3. rs2232710 SNV showed no association with DVT in two Dutch replication cohorts the LETS study and the MEGA study, indicating that the rs2232710 variant is not a risk factor for DVT

4. Results show the energetic basis of the Z-dependent protease inhibitor (ZPI)-protein Z (PZ) interaction and suggest an important role for ZPI Lys-239 in PZ catalytic action.

5. The unbalance between PZ and ZPI in plasma samples from patients with Colorectal Cancer or Pancreatic Cancer is not only related to an inflammatory state but could also results from an ectopic synthesis of these proteins by the cancer cells.

6. Protein Z EGF2 subdomain constitutes an interactive-site for ZPI protein.

7. Protein Z/protein Z-dependent protease inhibitor and Fxa expression in human gastric cancer cells indicate that these proteins may play a role in anticoagulant events at the tumor tissue.

8. the PZ/ZPI complex may play some modulating role in hemophilia A

9. structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI.

10. The study shows by Ala-scanning mutagenesis of the ZPI-binding interface, together with native PAGE and kinetic analyses of PZ binding to ZPI, that Tyr240 and Asp293 of ZPI are crucial hot spots for PZ binding.

11. Report two missense mutations identified in venous thrombosis patients impair the inhibitory function of the ZPI were not convincingly associted with thrombosis risk.

12. heparin-binding site of ZPI was mapped: basic residues of both helices C and D of ZPI interact with heparin to modulate the inhibitory function of the serpin.

13. Plasma ZPI levels were unchanged in non-pregnant recurrent miscarriage women, while the plasma PZ level was slightly reduced, a finding consistent with existing reports.

14. Medium expression of ZPI(IRS=6.5), together with weak expression of PZ(IRS=4), was observed in cancer cells.

15. localization of PZ/ZPI and FX in colon cancer cells indicates that PZ/ZPI may contribute to anticoagulant events at the tumor site.

16. The results demonstrate that both ZPI R67X and W303X non-sense variants and specific ZPI haplotypes are significantly associated with recurrent spontaneous miscarriage.

17. heparin activates ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and pharmacologically important role in ZPI anticoagulant function.

18. present in loco in human breast cancer tissue

19. Data show that mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.

20. PROTEIN A AND PZI WERE FOUND IN KIDNEY TUBULES BY IMMUNOHISTOCHEMISTRY

Mouse (Murine) serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 10 (SERPINA10) interaction partners

1. Letter: ZPI is a typical acute phase reactant.

2. structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI.

3. PZ and ZPI deficiency would be associated with a modest thrombotic risk with ZPI deficiency producing a more severe phenotype.

Cow (Bovine) serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 10 (SERPINA10) interaction partners

1. structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI.