Recombinant Human/Mouse/Rat BMP-2 Protein


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Product Details

Reactivity Hu, Mu, RtSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Human/Mouse/Rat BMP-2 Protein Summary

Details of Functionality
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Binnerts, M.E. et al. (2004) Biochem. Biophys. Res. Commun. 315(2):272. The ED50 for this effect is 40-200 ng/mL.
The specific activity of Recombinant Human BMP-2 is approximately 781 U/μg, which is calibrated against human BMP-2 WHO International Standard (NIBSC code: 93/574).
Chinese Hamster Ovary cell line, CHO-derived BMP-2 protein
Accession #
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
13 kDa (monomer).
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.
15-16 kDa, reducing conditions
Read Publications using
355-BM in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in Glycine, Sucrose, Tween® 80 and Glutamic Acid with BSA as a carrier protein. *1 mg pack size (01M) is supplied as a 0.2 µm filtered solution in Glycine, Sucrose, Tween® 80 and Glutamic Acid with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100-200 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Human/Mouse/Rat BMP-2 Protein

  • BMP2
  • BMP-2
  • BMP-2A
  • BMP2ABone morphogenetic protein 2A
  • bone morphogenetic protein 2


Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsal-ventral patterning, organogenesis, limb bud formation, and bone formation and regeneration (1, 2). Human BMP‑2 is synthesized as a 396 amino acid (aa) preproprotein that contains a 23 aa signal sequence, a 259 aa prosegment, and a 114 aa mature region (3). Proteolytic removal of the propeptide enables mature BMP-2 to form active disulfide linked homodimers and heterodimers with BMP-7 (2). Mature monomeric BMP-2 is an 18 kDa glycosylated peptide with seven conserved cysteines that form a cystine knot structure (4). Mature human BMP-2 shares 100% aa sequence identity with mouse and rat BMP-2. It shares 85% aa sequence identity with human BMP-4 and less than 51% with other BMPs. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMPR‑IA, or BMPR‑IB) and a type II receptor (BMP RII or Activin RIIB) (2, 5). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth, and bone and cartilage repair (6, 7). It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells, and vascular smooth muscle cells (2, 8‑10). BMP-2/BMP-7 heterodimers are significantly more potent than BMP-2 homodimers at inducing bone formation in vivo (11). BMP-2 also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells, and is required for cardiac contractility (12‑15).
  1. Kishigami, S. and Y. Mishina (2005) Cytokine Growth Factor Rev. 16:265.
  2. Chen, D. et al. (2004) Growth Factors 22:233.
  3. Wozney, J. et al. (1988) Science 242:1528.
  4. Sun, P.D. and D.R. Davies (1995) Annu. Rev. Biophys. Biomol. Struct. 24:269. 
  5. Sebald, W. et al. (2004) Biol. Chem. 385:697.
  6. De Luca, F. et al. (2001) Endocrinology 142:430.
  7. Davidson, E.N.B., et al. (2007) Arthritis Res. Ther. 9:R102.
  8. Ryoo, H.-M. et al. (2006) Gene 366:51.
  9. Kramer, J. et al. (2000) Mech. Dev. 92:193.
  10. Li, X. et al. (2008) Atherosclerosis January 5 epub.
  11. Zhu, W. et al. (2004) J. Bone Miner. Res. 19:2021.
  12. Peiris, D. et al. (2007) Am. J. Physiol. Gastrointest. Liver Physiol. 292:G753.
  13. Kano, Y. et al. (2005) Endocrinology 146:5332.
  14. Hallahan, A.R. et al. (2003) Nat. Med. 9:1033.
  15. Wang, Y.-X. et al. (2007) Cardiovasc. Res. 74:290.

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Publications for BMP-2 (355-BM)(121)

We have publications tested in 11 confirmed species: Human, Mouse, Rat, Bovine, Canine, Chicken, Equine, Rabbit, Transgenic Mouse, Xenopus, Zebrafish.

We have publications tested in 9 applications: Binding Assay, Bioassay, ELISA capture, In Ovo, In Vivo, In Vivo grafting, Organogenesis, Surface Plasmon Resonance, complex formation.

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Binding Assay
ELISA capture
In Ovo
In Vivo
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Surface Plasmon Resonance
complex formation
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Showing Publications 1 - 10 of 121. Show All 121 Publications.
Publications using 355-BM Applications Species
K Sasa, K Yoshimura, A Yamada, D Suzuki, Y Miyamoto, H Imai, K Nagayama, K Maki, M Yamamoto, R Kamijo Monocarboxylate transporter-1 promotes osteoblast differentiation via suppression of p53, a negative regulator of osteoblast differentiation Sci Rep, 2018;8(1):10579. 2018 [PMID: 30002387] (Bioassay, Mouse) Bioassay Mouse
K Koefoed, J Skat-Rørda, P Andersen, CB Warzecha, M Pye, TA Andersen, KD Ajbro, E Bendsen, M Narimatsu, F Vilhardt, LB Pedersen, JL Wrana, RH Anderson, K Møllgård, ST Christense, LA Larsen The E3 ubiquitin ligase SMURF1 regulates cell-fate specification and outflow tract septation during mammalian heart development Sci Rep, 2018;8(1):9542. 2018 [PMID: 29934521] (Bioassay, Human) Bioassay Human
YH Chung, YH Huang, TH Chu, CL Chen, PR Lin, SC Huang, DC Wu, CC Huang, TH Hu, YH Kao, MH Tai BMP-2 restoration aids in recovery from liver fibrosis by attenuating TGF-?1 signaling Lab. Invest., 2018;0(0):. 2018 [PMID: 29789683] (Bioassay, Rat) Bioassay Rat
P Jongwattan, M Terajima, PA Miguez, W Querido, H Nagaoka, N Sumida, EG Gurysh, KM Ainslie, N Pleshko, L Perera, M Yamauchi Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function Sci Rep, 2018;8(1):7022. 2018 [PMID: 29728612] (Bioassay, Mouse) Bioassay Mouse
H Kang, S Jha, Z Deng, N Fratzl-Zel, WA Cabral, A Ivovic, F Meylan, EP Hanson, E Lange, J Katz, P Roschger, K Klaushofer, EW Cowen, RM Siegel, JC Marini, T Bhattachar Somatic activating mutations in MAP2K1 cause melorheostosis Nat Commun, 2018;9(1):1390. 2018 [PMID: 29643386] (Bioassay, Human) Bioassay Human
M Desancé, R Contentin, L Bertoni, T Gomez-Ledu, T Branly, S Jacquet, JM Betsch, A Batho, F Legendre, F Audigié, P Galéra, M Demoor Chondrogenic Differentiation of Defined Equine Mesenchymal Stem Cells Derived from Umbilical Cord Blood for Use in Cartilage Repair Therapy Int J Mol Sci, 2018;19(2):. 2018 [PMID: 29439436] (Bioassay, Equine) Bioassay Equine
S Kokabu, V Rosen BMP3 expression by osteoblast lineage cells is regulated by canonical Wnt signaling FEBS Open Bio, 2018;8(2):168-176. 2018 [PMID: 29435407] (Bioassay, Mouse) Bioassay Mouse
JB Lees-Shepa, M Yamamoto, AA Biswas, SJ Stoessel, SE Nicholas, CA Cogswell, PM Devarakond, MJ Schneider, SM Cummins, NP Legendre, S Yamamoto, V Kaartinen, JW Hunter, DJ Goldhamer Activin-dependent signaling in fibro/adipogenic progenitors causes fibrodysplasia ossificans progressiva Nat Commun, 2018;9(1):471. 2018 [PMID: 29396429] (In Vivo, Mouse) In Vivo Mouse
WS Fagg, N Liu, MJ Yang, K Cheng, E Chung, JS Kim, G Wu, J Fair Magnetic Targeting of Stem Cell Derivatives Enhances Hepatic Engraftment into Structurally Normal Liver Cell Transplant, 2017;26(12):1868-1877. 2017 [PMID: 29390880] (Bioassay, Mouse) Bioassay Mouse
MG Perino, S Yamanaka, DR Riordon, Y Tarasova, KR Boheler Ascorbic acid promotes cardiomyogenesis through SMAD1 signaling in differentiating mouse embryonic stem cells PLoS ONE, 2017;12(12):e0188569. 2017 [PMID: 29232368] (Bioassay, Mouse) Bioassay Mouse
Show All 121 Publications.

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FAQs for BMP-2 (355-BM). (Showing 1 - 1 of 1 FAQs).

  1. I am interested in Bone Morphogenic Protein 2 (BMP-2) for clinical trial in humans. I am using this protein in stem cells culture for future use in humans. Do you have BMP-2 in pharma grade that I can use for humans?
    • Our antibodies are for research purposes only unfortunately. I am sorry we cannot be of further help.

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Gene Symbol BMP2