Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF

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Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF Summary

Product Specifications

>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA.

When Recombinant Mouse GDF-9 (Catalog # 739-G9) is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human/Mouse BMPR‑II Fc Chimera that produces 50% of the optimal binding response is found to be approximately 0.1 ‑ 0.5 μg/mL.

Mouse myeloma cell line, NS0-derived BMPR-II protein
(Ala26 - Ile151, with an N-terminal Met)
Accession # Q13873
(Pro100 - Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Met & Ser27
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass

41.5 kDa (monomer)

65-75 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 Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: BMPR-II

Like other members of the TGF-beta superfamily, cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the binding to heteromeric complex of type I and type II serine-threonine kinase receptors. Both receptor types are required for the signl transduction. BMP receptor II (BMPR-II) is one of the five mammalian type II receptors (including TGF-beta R-II, ActR-II, ActR-IIB, BMPR-II and MISR-II) for the TGF-beta superfamily ligands. The type II receptors for TGF-beta and activin bind ligands with high affinity by itself. In contrast, BMPR-II binds BMP-2, BMP-4 and BMP-7 weakly in the absence of type I receptor, and the binding can be facilitated by the presence of the type I receptor. BMPR-II mRNA is widely expressed in fetal and adult tissues. Human and mouse BMPR-II are highly conserved sharing 97% sequence identity.

  1. Rosenzweig, B.L. et al. (1995) Proc. Natl. Acad. Sci. USA 92:7632.
  2. Beppu, H. et al. (1997) Biochem. Biophys. Res. Commun. 235:499.
  3. Kawabata, M. et al. (1998) Cytokine and Growth Factor Reviews 9:49.
Long Name
Bone Morphogenetic Protein Receptor II
Entrez Gene IDs
659 (Human); 12168 (Mouse)
Alternate Names
BMP type II receptor; BMP type-2 receptor; BMPR2; BMPR-2; BMPR3; BMPRII; BMPR-II; BMPR-IIprimary pulmonary hypertension 1; Bone morphogenetic protein receptor type II; bone morphogenetic protein receptor type-2; bone morphogenetic protein receptor, type II (serine/threonine kinase); BRK-3; EC 2.7.11; EC; FLJ41585; FLJ76945; PPH1BMR2; T-ALK; type II activin receptor-like kinase; type II receptor for bone morphogenetic protein-4

Citations for Recombinant Human/Mouse BMPR-II Fc Chimera 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.

9 Citations: Showing 1 - 9
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  1. Crystal structures of BMPRII extracellular domain in binary and ternary receptor complexes with BMP10
    Authors: J Guo, B Liu, M Thorikay, M Yu, X Li, Z Tong, RM Salmon, RJ Read, P Ten Dijke, NW Morrell, W Li
    Nature Communications, 2022;13(1):2395.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: Surface Plasmon Resonance
  2. The anti-M�llerian hormone prodomain is displaced from the hormone/prodomain complex upon bivalent binding to the hormone receptor
    Authors: RL Cate, N di Clement, C Racine, NP Groome, RB Pepinsky, A Whitty
    The Journal of Biological Chemistry, 2021;0(0):101429.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: ELISA Capture
  3. BMPR1A is necessary for chondrogenesis and osteogenesis while BMPR1B prevents hypertrophic differentiation
    Authors: T Mang, K Kleinschmi, F Ploeger, A Schoeneman, S Lindemann, A Gigout
    J. Cell. Sci., 2020;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  4. Facilitated receptor-recognition and enhanced bioactivity of bone morphogenetic protein-2 on magnesium-substituted hydroxyapatite surface
    Authors: B Huang, Y Yuan, T Li, S Ding, W Zhang, Y Gu, C Liu
    Sci Rep, 2016;6(0):24323.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains
    Authors: Y Kienast, U Jucknischk, S Scheiblich, M Thier, M de Wouters, A Haas, C Lehmann, V Brand, D Bernicke, K Honold, S Lorenz
    J. Biol. Chem, 2016;291(7):3395-410.
    Species: Human
    Sample Types:
    Applications: Bioassay
  6. Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor Growth.
    Authors: Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV
    J. Biol. Chem., 2011;286(34):30034-46.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  7. A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7.
    Authors: Sengle G, Ono RN, Lyons KM, Bachinger HP, Sakai LY
    J. Mol. Biol., 2008;381(4):1025-39.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ELISA (Capture)
  8. The BMP-binding protein Crossveinless 2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling in Drosophila.
    Authors: Serpe M, Umulis D, Ralston A, Chen J, Olson DJ, Avanesov A, Othmer H, O'Connor MB, Blair SS
    Dev. Cell, 2008;14(6):940-53.
    Species: Drosophila
    Sample Types: Recombinant Protein
    Applications: Binding Assay
  9. Regulation of ADMP and BMP2/4/7 at opposite embryonic poles generates a self-regulating morphogenetic field.
    Authors: Reversade B, De Robertis EM
    Cell, 2005;123(6):1147-60.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Receptor Binding Assay


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Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF
By Anonymous on 02/18/2021
Application: In vitro bioactivity in cell culture