|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the mature form of human BMP2 (NP_001191.1) (Gln283-Arg396) was expressed. The mature form sequences of human, mouse, rat, rhesus and canine BMP2 are identical.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 95 % as determined by SDS-PAGE|
|Measured by its ability to induce alkaline phosphatase production by MC3T3-E1 mouse osteoblastic cells. The ED50 for this effect is typically 0.5-2 μg/ml.|
|Please contact us for more information.|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human BMP2 monomer consists of 115 amino acids and has a predicted molecular mass of 13 kDa.|
|Lyophilized from sterile 30 % CAN, 0.1 % TFA, pH 2.9.|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
BMP-2 protein, like other bone morphogenetic proteins, plays an important role in the development of bone and cartilage. BMP-2 protein is involved in the hedgehog pathway, TGF beta signaling pathway, and cytokine-cytokine receptor interaction. BMP-2 and BMP-7 are osteogenic BMPs that have been demonstrated to potently induce osteoblast differentiation in a variety of cell types. BMP-2, BMP-4 and BMP-7 are known to be of major importance in bone formation and repair. In cancerous tissues BMP-2 protein may play an important role in the progression of glioma.