Recombinant Human BMP-1/PCP Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (7)
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Recombinant Human BMP-1/PCP Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
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
Predicted Molecular Mass
70.5 kDa
84 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Supplied as a 0.2 μm filtered solution in HEPES and Ammonium Sulfate.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

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
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


Background: BMP-1/PCP

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.
Long Name
Bone Morphogenetic Protein 1
Entrez Gene IDs
649 (Human); 12153 (Mouse); 83470 (Rat)
Alternate Names
BMP1; BMP-1; bone morphogenetic protein 1; EC 3.4.24; EC; FLJ44432; Mammalian tolloid protein; mTld; PCOLC; PCP; PCP2; procollagen C-endopeptidase; Procollagen C-proteinase; TLD

Citations for Recombinant Human BMP-1/PCP Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

7 Citations: Showing 1 - 7
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  1. Novel myostatin-specific antibody enhances muscle strength in muscle disease models
    Authors: H Muramatsu, T Kuramochi, H Katada, A Ueyama, Y Ruike, K Ohmine, M Shida-Kawa, R Miyano-Nis, Y Shimizu, M Okuda, Y Hori, M Hayashi, K Haraya, N Ban, T Nonaka, M Honda, H Kitamura, K Hattori, T Kitazawa, T Igawa, Y Kawabe, J Nezu
    Scientific Reports, 2021;11(1):2160.
    Species: Cynomolgus Monkey
    Sample Types: Protein
    Applications: Bioassay
  2. LncRNA-Safe contributes to cardiac fibrosis through Safe-Sfrp2-HuR complex in mouse myocardial infarction
    Authors: K Hao, W Lei, H Wu, J Wu, Z Yang, S Yan, XA Lu, J Li, X Xia, X Han, W Deng, G Zhong, ZA Zhao, S Hu
    Theranostics, 2019;9(24):7282-7297.
    Species: Mouse
    Sample Types: Cells
    Applications: enzyme activity
  3. Intracellular retention of mutant lysyl oxidase leads to aortic dilation in response to increased hemodynamic stress
    Authors: VS Lee, CM Halabi, TJ Broekelman, PC Trackman, NO Stitziel, RP Mecham
    JCI Insight, 2019;5(0):.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Bioassay
  4. Maltose binding protein-fusion enhances the bioactivity of truncated forms of pig myostatin propeptide produced in E. coli
    Authors: SB Lee, SK Park, YS Kim
    PLoS ONE, 2017;12(4):e0174956.
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  5. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
    Nature, 2012;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp).
    Authors: Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y
    J. Bone Miner. Res., 2010;26(0):220.
    Species: Human
    Sample Types:
    Applications: Bioassay
  7. Dentin matrix protein-1 isoforms promote differential cell attachment and migration.
    Authors: Von Marschall Z, Fisher LW
    J. Biol. Chem., 2008;283(47):32730-40.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay


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