| + |
Factor Va-Xa | up-regulates activity 
cleavage
|
F2 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263546 |
|
|
|
|
| pmid |
sentence |
| 11983337 |
This activation is accomplished at a physiologically relevant rate by the prothrombinase complex, a macromolecular association of the serine protease factor Xa (fXa) with its cognate cofactor, factor Va (fVa), and substrate, prothrombin|Factor Va Increases the Affinity of Factor Xa for Prothrombin |
|
| Publications: |
1 |
| + |
F10 | form complex 
binding
|
Factor Va-Xa |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263557 |
|
|
in vitro |
|
| pmid |
sentence |
| 2026608 |
The binding of factor Xa to factor Va in the presence of Ca2+ ions and phospholipid is fundamental for the activation of prothrombin to thrombin. |Regardless of which protein was labeled, a factor Xa-Va complex (s20,w = 9.8) was formed. The interaction is specific and reversible. I |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
F5 | form complex
binding
|
Factor Va-Xa |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263558 |
|
|
in vitro |
|
| pmid |
sentence |
| 2026608 |
The binding of factor Xa to factor Va in the presence of Ca2+ ions and phospholipid is fundamental for the activation of prothrombin to thrombin. |Regardless of which protein was labeled, a factor Xa-Va complex (s20,w = 9.8) was formed. The interaction is specific and reversible. I |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
Factor Va-Xa
CPX-6221