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Human BMP2 protein (bone morphogenetic protein 2) protein is member of the TGFβ family and a key regulator of embryogenesis and potent differentiation factor of embryonic stem cells (ESC) and induced pluripotent stem cells (iPSC) towards endoderm fates. BMP2 plays roles in the differentiation of mesenchymal cells to adipocytes, epithelial cancer EMT, chondrogenesis and regulation of neuronal and glial cell development.
26 kDa disulfide–linked bioactive highly pure dimer comprised of the mature domain of human BMP2 protein (animal-free and carrier protein-free). Our recombinant human BMP2 protein has been optimized for expression in E. coli and purified to homogeneity, offering a highly reliable and cost-effective reagent for the regulation of stem cell differentiation.
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1mg may be despatched as 2 x 500µg
high purity human bone morphogenetic protein 2, BMP2 (Uniprot: P12643).
26 kDa (dimer)
expressed in E. coli
animal-free (AOF) and carrier protein-free.
manufactured in our Cambridge, UK laboratories
lyophilized from acetonitrile, TFA
resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired and store frozen at -20 oC or -80 oC
differentiation of human pluripotent stem cells towards extra-embryonic endoderm, mesenchymal, neural lineages, and chondrocytes
BMP2 activity 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. EC50 = 0.30 nM. Data from QK007 batch #010.
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.
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. Data from Qk007 lot #010
further quality assays
mass spectrometry: single species with expected mass
analytical reversed-phase: single sharp peak
endotoxin: <0.005 EU/μg protein (below level of detection)
We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine. All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.
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.
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.
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 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.
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.
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.
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.
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.
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.
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.
Our products are for research use only and not for diagnostic or therapeutic use. Products are not for resale.
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