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Recombinant Human Active Coagulation Factor XIV/ProteinC, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Active Coagulation Factor XIV/ProteinC, CF Summary

Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate Boc-VPR-AMC (Catalog # ES011). The specific activity is >275 pmol/min/µg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived human Coagulation Factor XIV/Protein C protein
Ala43-Pro461, with a C-terminal 10-His tag
The isolated protein was activated by thrombin/thrombomodulin complex and further purified.
Accession #
N-terminal Sequence
Ala43 (light chain) & Leu212 (heavy chain)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Enzymes
Gene
PROC
Purity
>95%, 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.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
19 kDa (light chain), 29 kDa (heavy chain).
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.
SDS-PAGE
22-25 kDa and 40-50 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl and CaCl2.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Assay Buffer: 50 mM Tris, 0.15 M NaCl, 10 mM CaCl2, 0.01% (w/v) Brij 35, pH 8.5
  • Recombinant Human Active Coagulation Factor XIV/Protein C (rhPROC) (Catalog # 4998-SE)
  • Substrate: Boc-Val-Pro-Arg-AMC (Catalog # ES011)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhPROC to 2 ng/µL in Assay Buffer.
  2. Dilute Substrate to 1 mM in Assay Buffer.
  3. Load into plate 50 µL of 2 ng/µL rhPROC, and start the reaction by adding 50 µL of 1 mM Substrate. As a Substrate Blank combine 50 µL of 1 mM Substrate and 50 µL of Assay Buffer.
  4. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

 Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard 7-Amino, 4-Methyl Coumarin (AMC) (Sigma, Catalog # A-9891).

Per Well:
  • rhPROC: 0.1 µg
  • Substrate: 500 μM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Active Coagulation Factor XIV/ProteinC, CF

  • Anticoagulant protein C
  • APC
  • Autoprothrombin IIA
  • Blood coagulation factor XIV
  • Coagulation Factor XIV
  • EC 3.4.21
  • EC 3.4.21.69
  • PC
  • PROC
  • PROC1
  • protein C (inactivator of coagulation factors Va and VIIIa)
  • Protein C
  • vitamin K-dependent protein C

Background

Protein C (PROC) is a vitamin K-dependent serine protease synthesized in liver as a single-chain precursor (1). The N-terminus consists of a signal peptide (aa 1-32) and a propeptide (aa 33-42). The mature chain (aa 43-461) is converted to two disulfide-linked chains (light: aa 43-199 and heavy: 200‑461) and both forms are inactive. The light chain consists of Gla (gamma-carboxy-glutamate) domain and two EGF-like domains. The heavy chain consists of an activation peptide (aa 200‑211) and serine protease domain (aa 212-450). Present in plasma at 3 to 5 mg/L, PROC plays a key role in anticoagulation. Physiologically, the inactive forms of PROC are converted to the active form by thrombin, which releases the activation peptide. The active PROC cleaves factors VIIIa and Va to inactivate them. This anticoagulation activity can be enhanced by a presence of a cofactor such as Protein S. In hereditary thrombophilia, PROC deficiency is caused by a genetic mutation which affects PROC activity. A severe recessive form may result in massive thrombosis fatal to patient.

  1. Shen, L. and Dahlbäck, B. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds. pp. 1673.

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Bioinformatics

Gene Symbol PROC
Uniprot