Recombinant Human BMP-1/PCP Protein, CF

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Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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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.
Source
Mouse myeloma cell line, NS0-derived human BMP-1/PCP protein
Ala121-Gln730, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ala121
Protein/Peptide Type
Recombinant Enzymes
Gene
BMP1
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

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.
SDS-PAGE
84 kDa, reducing conditions
Publications
Read Publications using
1927-ZN in the following applications:

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 HEPES and Ammonium Sulfate.
Purity
>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

Notes

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 3.4.24.19
  • FLJ44432
  • Mammalian tolloid protein
  • mTld
  • PCOLC
  • PCP
  • PCP2
  • procollagen C-endopeptidase
  • Procollagen C-proteinase
  • TLD

Background

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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Publications for BMP-1/PCP (1927-ZN)(4)

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Bioinformatics

Gene Symbol BMP1
Uniprot