| Reactivity | HuSpecies Glossary |
| Applications | Enzyme Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002). The specific activity is >700 pmol/min/µg, as measured under the described conditions. |
| Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Coagulation Factor X protein Leu24-Lys488 with a C-terminal 10-His tag Proform Factor X was expressed, purified, activated and further purified to yield Factor Xa. |
| Accession # | |
| N-terminal Sequence | Tyr84, Phe124 & Ile235 |
| Structure / Form | Active form |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | F10 |
| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 12 kDa & 30 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 13-14 kDa and 33-36 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in MES, NaCl and CaCl2. |
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| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile 25 mM MES, 150 mM NaCl and 5 mM CaCl2, pH 6.0. |
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| Assay Procedure |
*Adjusted for Substrate Blank
|
As the only known physiological activator of thrombin, Factor X is a vitamin K-dependent plasma protease that plays a pivotal role in blood coagulation. Human Factor X is initially synthesized in the liver as a single-chain precursor of 488 amino acid residues with a signal peptide and a pro region (residues 1‑40). Both the intrinsic and extrinsic pathways activate Factor X to Xa, which consists of light (residues 41‑179) and heavy (residues 235‑488) chains linked by a disulfide bond. The light chain contains a Gla and two EGF-like domains and the heavy chain corresponds to the serine protease domain. The full-length human Factor X was expressed and the pro enzyme was purified and activated. The active protease (rhXa) was further purified and analyzed for its activity towards either peptides or proteins containing a Xa cleavage site. In addition to the activity described in the Activity Assay Protocol, rhFX also be used to cleave fusion proteins containing a Factor Xa cleavage site. The conditions for the optimal cleavage of a particular fusion protein, such as the molar ratio between rhFX and the protein and time and temperature of incubation, are protein-dependent and need to be individually determined.
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