Human BMP-2

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Cat-Nr.200-002S
Size10 µg
Price160 €
SourceE. coli
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]115
Molecular Weight26.0 kDa
N Terminal SequenceMQAKHKQ
Endotoxin Levels< 0.1 ng per µg of BMP-2
Biological ActivityMeasured by the ability of BMP-2 to induce alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 0.3-0.8 µg/ml.
Species ReactivityHuman
Buffer50 mM acetic acid
ReconstitutionThe lyophilized BMP-2 is best soluble in 50 mM acetic acid at a concentration of 0.1mg/ml but should be also soluble in most aqueous buffers when the pH is below 6.0.
Stability and StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted BMP-2 should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles!
Synonymsbone morphogenetic protein 2; BDA2; BMP2A; bone morphogenetic protein 4; ZYME; BMP2B; OFC11; BMP2B1; MCOPS6
DescriptionHuman Bone Morphogenetic Protein-2 (BMP-2) is a disulfide-bonded homodimeric protein with an apparent molecular weight of 26 kDa. BMP-2 regulates similarly to its nearest homologue BMP-4 diverse fundamental processes during embryonic development: BMP-2 and other BMP proteins have great potential for medical therapeutic applications, in particular because they allow or at least accelerate the ossification of extensive bone lesions. The amino acid sequence of recombinant human BMP-2 starts with MQAKHKQ (position 283) containing the Met from the E. coli expression vector. BMP-2 is a heparin binding protein.
Protein SequenceMQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Uniprot IDP12643
Protein RefSeqNP_001191
mRNA RefSeqNM_001200

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Reference

  1. Osteogenic differentiation and proliferation of bone marrow-derived mesenchymal stromal cells on PDLLA + BMP-2-coated titanium alloy surfaces. M. Haversath et al., J Biomed Mater Res A. 2016 Jan;104(1):145-54.
  2. Functionalization of titanium implants using a modular system for binding and release of VEGF enhances bone-implant contact in a rodent model. H. Schliephake et al., J Clin Periodontol. 2015 Mar;42(3):302-10.
  3. Hollow hydroxyapatite microspheres/chitosan composite as a sustained delivery vehicle for rhBMP-2 in the treatment of bone defects. A.H. Yao et al., J Mater Sci Mater Med. 2015 Jan;26(1):5336.
  4. Release and bioactivity of bone morphogenetic protein-2 are affected by scaffold binding techniques in vitro and in vivo. S. Suliman et al., J Control Release. 2015 Jan 10;197:148-57.
  5. Improved Anchorage of Ti6Al4V Orthopaedic Bone Implants through Oligonucleotide Mediated Immobilization of BMP-2 in Osteoporotic Rats. J. V. Wölfle et al., PLoS One. 2014; 9(1): e86151.
  6. Efficacy Evaluation of a New Hyaluronan Derivative HYADD® 4-G to Maintain Cartilage Integrity in a Rabbit Model of Osteoarthritis. P. Mainil-Varlet et al., Cartilage. 2013 Jan; 4(1): 28–41.
  7. Functionalisation of PLLA nanofiber scaffolds using a possible cooperative effect between collagen type I and BMP-2: impact on colonization and bone formation in vivo. M. D. Schofer et al., J Mater Sci Mater Med. 2012 Sep; 23(9): 2227–2233.
  8. Functionalisation of PLLA nanofiber scaffolds using a possible cooperative effect between collagen type I and BMP-2: impact on growth and osteogenic differentiation of human mesenchymal stem cells. M. D. Schofer et al., J Mater Sci Mater Med. 2011 Jul; 22(7): 1753–1762.
  9. Electrospun PLLA Nanofiber Scaffolds and Their Use in Combination with BMP-2 for Reconstruction of Bone Defects. M. D. Schofer et al., PLoS One. 2011; 6(9): e25462.

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