Recombinant human BMP2 protein (Qk007)


Recombinant human BMP2 protein is a 26 kDa disulfidelinkebioactive dimer comprised of the mature domain of human BMP2 protein. Our recombinant human BMP2 protein has been optimized for expression in E. coli and purified to homogeneity, offering a highly reliable and cost-effective option for the regulation of stem cell differentiation.

Qk007 Recombinant human BMP2 protein

Bone morphogenetic protein 2 (BMP2) is a member of the BMP subgroup of the transforming growth factor beta (TGF-β) superfamily. It plays numerous roles in the developing embryo, such as embryonic patterning along the dorso-ventral axis, organogenesis, limb bud formation, and bone and cartilage growth. BMP2 protein is a potent differentiation factor and directs human pluripotent stem cells towards extra-embryonic endoderm, mesenchymal and neural lineages, and chondrocytes1.  Recombinant BMP2 protein induces bone and cartilage formation in vitro and chondrogenesis in human adult mesenchymal stem cells2.

Human bone morphogenetic protein 2 (BMP2) is synthesized as a preproprotein consisting of N-terminal signal peptide, 259 amino acid residue pro-domain and 114 residue mature domain. Proteolytic removal of the propeptide enables mature BMP2 protein to form active disulfide-linked homodimers, and heterodimers with BMP7.

Mature human BMP2 protein shares 100% amino acid sequence identity with mouse and rat BMP2. It also shares 85% amino acid sequence identity with the related protein, BMP4, and less than 51% identity with other BMPs.

Summary: Qk007 mature domain of human bone morphogenetic protein 2 (BMP2) expressed in E. coli and purified to homogeneity (Uniprot: P12643). Mature active protein is a disulfide-linked dimer.

Molecular mass: ~26 kDa (for the dimer)

Form: protein is provided lyophilized from a fully volatile solution without carrier protein. Animal-derived component and carrier protein-free.

Purity and bioactivity

For peace of mind that our recombinant human BMP2 protein will work exactly the same way every day, from batch to batch and at any scale you need, we conduct extensive purity and bioactivity analysis. This includes SDS-PAGE, mass spectrometry, reversed-phase chromatography, UV spectroscopy and endotoxin level testing.

To confirm the biochemical identity of our recombinant human BMP2 protein and ensure that its purity meets our rigorous standards, we conduct SDS-PAGE on every protein batch. As BMP2 is a disulfide-linked dimer, we use both reduced and non-reduced conditions, as well as appropriate stains, for our SDS-PAGE analysis.

We also check the final refolded protein is bioactive using a BMP-responsive firefly luciferase reporter assay in HEK293T cells. By knowing what the expected activity of the protein is and measuring calibrant alongside each batch of protein, we can use this bioassay to define a complete dose-response curve. In addition, we use it to check the EC50 value of each preparation of our recombinant human BMP2 protein.

Find out more about our extensive purity testing in the next tab.

Example data

Protein purity: SDS-PAGE in reduced and non-reduced conditions

Recombinant human BMP2 protein purity in SDS-PAGE

Bioactivity: BMP-responsive luciferase reporter assay

Recombinant human BMP2 protein bioactivity in a BMP-responsive luciferase reporter assay

Research applications

iPSC/ESC differentiation

All our proteins are produced in our Cambridge, UK labs.  We provide detailed quality data for each batch because we believe reliable, high-quality cytokines and growth factors are critical for successful stem cell and organoid culture.  Please contact us with questions any time by email at or phone +44 (0) 1223 491486 / US toll free 1-866 877 2185.

Order online and upload your PO or pay by credit card,  or email your PO to

We provide bulk orders and stock reservation for sensitive applications, please email us.

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

For final purity and activity tests on our proteins, we choose a vial at random and reconstitute as recommended. Biochemical identity and purity is determined using SDS-PAGE, mass spectrometry and analytical reversed-phase chromatography. Bioactivity is quantified using an appropriate cell-based assay. As stem cells are sensitive to endotoxin levels, we use a high-resolution test to ensure endotoxin levels are at industry-leading low levels (<0.01 EU per µg protein). We also check that the correct amount of protein is recovered from the vial - it might sound basic, but if you order 100 µg, we believe you should receive 100 µg, so you can rely on your calculated dilution.

Purity: SDS-PAGE

Result: BMP2 migrates as a single band at 26 kDa in non-reducing (NR) conditions and 13 kDa as a single monomeric species upon reduction (R). No contaminating protein bands are visible.

Recombinant human BMP2 protein purity in SDS-PAGE

Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.

Bioactivity: luciferase reporter assay

Result: BMP2 activity is determined using a BMP2-responsive luciferase reporter assay in stably transfected HEK293T cells. EC50 = 0.30 nM.

Recombinant human BMP2 bioactivity in a BMP2-responsive luciferase reporter assay

Bioactivity is determined using a BMP2-responsive firefly luciferase reporter in stably transfected HEK293T cells. Cells are treated (in triplicate) with a serial dilution of BMP2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data are from QK007 batch #010.

Purity: mass spec analysis

Result: calculated molecular mass of the BMP2 dimer is 26058 Da. Result of the analysis: 26057.5 Da which is consistent with the calculated mass. No significant heterogeneity is present.

Recombinant human BMP2 protein shows the expected molecular mass in MALDI mass spectrometry analysis

MALDI mass spectrometric analysis is used to confirm the molecular mass of the intact protein and to reveal any heterogeneity that would not be evident in SDS-PAGE analysis. The results are compared with calculated mass of the protein with the assumption that all the cysteines are disulfide-linked. The different peaks represent different charge states of the protein.

Purity: analytical reversed-phase chromatography

Result: Reversed-phase chromatogram shows single sharp peak showing that the protein is pure and homogeneous.

Recovery of recombinant human BMP2 protein

Protein purity and structural homogeneity is analyzed by reversed-phase chromatography. 50 µg of protein, at 0.1 mg/ml in 10 mM HCl is analyzed in ACE C4 4.6 x 250 mm column eluted using a 10 – 90 % acetonitrile gradient in 0.1 % trifluoroacetic acid. Homogeneity is judged by the absence of multiple peaks and by the symmetry of the main peak. Blue line shows absorbance at 280 nm and the green line the acetonitrile gradient.

Purity: endotoxin level determination

Result: Endotoxin level <0.005 EU/ug protein (below level of detection)

Stem cell cultures are sensitive to endotoxins1, which can be present in media, serum and as a contaminant on plasticware.  We optimize our protein production processes to ensure the lowest possible levels of endotoxin contamination. Our endotoxin pass criteria are set at the industry-leading <0.1 EU per ug protein and we aim for <0.01 EU per ug protein.  Endotoxin levels in our proteins are determined by an external expert microbiological testing services provider.  Example data from QK007 batch #010.

1. A biological study establishing the endotoxin limit for in vitro proliferation of human mesenchymal stem cells (2017). Yusuke Nomura, Chie Fukui, Yuki Morishita, Yuji Haishima. Regenerative Therapy, 7, 45-51.

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Pure recombinant BMP2 protein may be poorly soluble in physiological solutions. Please follow our handling guidance for lyophilized cytokines below to minimize loss of protein due to precipitation or adsorption to plastic. We advise storing our recombinant human BMP2 protein at very low pH before dilution in cell culture media or your final working solution. Low pH will also assist in maintaining the correct disulfide structure of the protein by minimizing disulfide bond exchange reactions.

  • Resuspension in physiological buffers may cause precipitation of stock solutions, hence we recommend dissolving our lyophilized cytokines in 10 mM HCl (1:1000 dilution of concentrated HCl) while keeping the protein concentration at 50 µg/ml or above, in order to avoid loss by adsorption to plasticware.
  • To ensure you recover all of the protein, let the sample sit for a few minutes with the solubilization buffer at room temperature and pipette gently up and down (avoid foaming).
  • Rinse the tube with some more 10 mM HCl and pool with the rest.
  • The protein is tolerant of some freeze and thaw cycles, but as always with proteins, it is better to aliquot and store frozen.
  • Our proteins are supplied carrier protein-free. If compatible with your work, add carrier protein of your choice, such as BSA, HSA or gelatin, to further minimize loss by adsorption.
  • Store at -80°C for long-term storage or at -20°C for short-term storage.

We check that the correct amount of protein is recovered from the vial – it might sound basic but if you order 100 µg, we believe you should receive 100 µg, so when you use the proteins you can rely on your calculated dilution.

Recovery: protein quantitation

Result: UV spectrum shows full recovery of protein following aliquoting and lyophilization.

Absorbance at 280 nm: average 0.136

Recovered concentration: 0.136 cm-1 x 10 / 1.46 cm-1 mg ml-1 = 0.93 mg / ml
Recovery: 93%

Recovery of recombinant human BMP2 protein

The sample was reconstituted in 10 mM HCl to a theoretical concentration of 1 mg/ml following instructions above. Concentration was calculated using extinction coefficient at 280 nm.

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