Recombinant Human BMP-1/PCP Protein, CF Summary
Ala121-Gln730, with a C-terminal 6-His tag
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.
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.
- 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
- Dilute rhBMP-1 to 20 ng/µL in Assay Buffer.
- Dilute substrate to 20 µM in Assay Buffer.
- 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.
- Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in kinetic mode for 5 minutes.
- 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).
- rhBMP-1: 1 µg
- Substrate: 10 µM
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).
- Wozney, J.M. et al. (1988) Science 242:1528.
- Bond, J.S. and R.J. Beynon (1995) Protein Sci. 4:1247.
- Steiglitz, B.M. et al. (2004) J. Biol. Chem. 279:980.
- Leighton, M. and K.E. Kadler (2003) J. Biol. Chem. 278:18478.
- Hartigan, N. et al. (2003) J. Biol. Chem. 278:18045.
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.
Citations: Showing 1 - 7
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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
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
Sample Types: Cells
Applications: enzyme activity
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):.
Sample Types: Cell Lysates
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.
Sample Types: Recombinant Protein
Applications: Enzyme Assay
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
Sample Types: Whole Cells
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.
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.
Sample Types: Recombinant Protein
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Fluorogenic Peptide Substrates
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