Recombinant Human BMP-1/PCP Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Enzyme Activity

Order Details

Recombinant Human BMP-1/PCP Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007). The specific activity is >4 pmol/min/µg, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived human BMP-1/PCP protein
Ala121-Gln730, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Enzymes
>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.


Theoretical MW
70.5 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.
84 kDa, reducing conditions
Read Publications using
1927-ZN in the following applications:

Packaging, Storage & Formulations

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.
Supplied as a 0.2 μm filtered solution in HEPES and Ammonium Sulfate.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Assay Buffer: 25 mM HEPES, 0.1% Brij-35 (w/v), pH 7.5
  • Recombinant Human BMP‑1/PCP (rhBMP-1) (Catalog # 1927-ZN)
  • Fluorogenic Peptide Substrate: MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH (Catalog # ES007)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhBMP-1 to 20 ng/µL in Assay Buffer.
  2. Dilute substrate to 20 µM in Assay Buffer.
  3. Load into a black well plate 50 µL of 20 ng/µL rhBMP-1 and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing Assay Buffer in place of rhBMP-1.
  4. Read at excitation and emission wavelengths of 320 nm and 405 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 MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhBMP-1: 1 µg
  • Substrate: 10 µM


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

Alternate Names for Recombinant Human BMP-1/PCP Protein, CF

  • BMP1
  • BMP-1
  • bone morphogenetic protein 1
  • EC 3.4.24
  • EC
  • FLJ44432
  • Mammalian tolloid protein
  • mTld
  • PCP
  • PCP2
  • procollagen C-endopeptidase
  • Procollagen C-proteinase
  • TLD


Bone morphogenetic protein 1 (BMP‑1), also known as procollagen C‑proteinase (PCP), is a zinc protease of the astacin family (1, 2). BMP‑1/PCP plays a key role in formation of extracellular matrix (ECM) by converting precursor proteins into their mature and functional forms. The precursor proteins identified as substrates for BMP‑1/PCP include collagens, biglycan, laminin 5, dentin matrix protein‑1, and lysyl oxidase (3). There are six alternatively spliced forms known to be derived from the BMP‑1 gene, and isoform 1 consisting of residues 1 to 730 was expressed. The secreted and purified protein does not contain the signal peptide (amino acid residues 1‑22) and pro domain (residues 23‑120), but contain protease (residues 121‑321), CUB I (residues 322‑434), CUB II (residues 435‑546), EGF‑like (residues 547‑588) and CUB III (residues 591‑703) domains. The pro domain is apparently cleaved by a furin‑like proprotein convertase (4). The purified BMP‑1/PCP is an active protease and its peptidase activity can be determined as described above. The purified BMP‑1/PCP is predicted to possess procollagen C‑proteinase activity because it contains the minimal domain structure required (5).

  1. Wozney, J.M. et al. (1988) Science 242:1528.
  2. Bond, J.S. and R.J. Beynon (1995) Protein Sci. 4:1247.
  3. Steiglitz, B.M. et al. (2004) J. Biol. Chem. 279:980.
  4. Leighton, M. and K.E. Kadler (2003) J. Biol. Chem. 278:18478.
  5. Hartigan, N. et al. (2003) J. Biol. Chem. 278:18045.

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Gene Symbol BMP1