Recombinant human BMP-2 protein (Qk007)

Human recombinant BMP-2 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. BMP-2 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 BMP-2 protein, animal origin-free (AOF) and carrier protein-free.

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1000µg will be despatched as 2 x 500µg

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Summary

  • High purity human bone morphogenetic protein 2, BMP-2 (Uniprot: P12643).

  • >98%, by SDS-PAGE quantitative densitometry

  • 26 kDa (dimer)

  • Expressed in E. coli

  • Animal origin-free (AOF) and carrier protein-free.

  • Manufactured in our Cambridge, UK laboratories

  • Lyophilized from acetonitrile, TFA

  • Resuspend in 10 mM HCl at >100 µg/ml (provided with protein and free of charge), prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C

Featured applications

  • Differentiation of human pluripotent stem cells towards extra-embryonic endoderm, mesenchymal, neural lineages, and chondrocytes

Bone morphogenetic protein 2,BDA2, SSFSC, BMP-2A, BMP-2, Bone morphogenetic protein 2A

human

species similarity:
mouse – 100%
rat – 100%
porcine – 100%
bovine – 100%

Bioactivity

Human BMP2 Qk007 protein bioactivity lot #010

BMP-2 activity is determined using the BMP-2 responsive firefly luciferase reporter assay in stably transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of BMP-2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 0.3 nM (7.8 ng/mL). Data from Qk007 lot #10.

Purity

Human BMP2 Qk007 protein purity SDS-PAGE lot #010

BMP-2 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)

  • Recovery from stock vial:  >95%

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.

Qkine BMP-2 is more biologically active than a comparable alternative supplier protein

Qkine BMP-2 has higher bioactivity than an alternative supplier BMP-2

Bioactivity was determined using a BMP-2-responsive firefly luciferase reporter assay in stably transfected HEK293T cells. Cells were treated with a serial dilution of Qkine BMP-2 (Qk007, green) or alternative BMP-2 (supplier B, black). Firefly luciferase activity was measured and normalized to the control Renilla luciferase activity. Data from Qk007 lot #204510.

Protein background

Bone morphogenetic protein 2 (BMP-2) 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. BMP-2 protein is a potent differentiation factor and directs human pluripotent stem cells towards extra-embryonic endoderm, mesenchymal and neural lineages, and chondrocytes [1] .  Recombinant BMP-2 protein induces bone and cartilage formation in vitro and chondrogenesis in human adult mesenchymal stem cells [2].

Human bone morphogenetic protein 2 (BMP-2) 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 BMP-2 protein to form active disulfide-linked homodimers, and heterodimers with BMP7.

Mature human BMP-2 protein shares 100% amino acid sequence identity with mouse and rat BMP-2. It also shares 85% amino acid sequence identity with the related protein, BMP-4, and less than 51% identity with other BMPs.

[1] Pera, M. F. et al. Regulation of human embryonic stem cell differentiation by BMP-2 and its antagonist noggin. J. Cell Sci. 117, 1269–80 (2004). doi.org/10.1242/jcs.00970

[2] Schmitt, B. et al. BMP2 initiates chondrogenic lineage development of adult human mesenchymal stem cells in high-density culture. Differentiation. 71, 567–77 (2003). doi.org/10.1111/j.1432-0436.2003.07109003.x

Additional resources

Publications using recombinant human BMP-2 protein (Qk007)

Sex-Specific Chromatin Remodelling Safeguards Transcription in Germ Cells.
In Nature on 8 December 2021 by Huang, T et al.

Hydrostatic Pressure Promotes Chondrogenic Differentiation and Microvesicle Release from Human Embryonic and Bone Marrow Stem Cells.
In Biotechnology Journal on 18 December 2021 by Luo, L, et al.

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

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