The purity of recombinant hBMP-2 was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant hBMP-2 and staining overnight with Coomassie Blue.
ATDC-5 cells were cultured with 0 to 1000 ng/mL of hBMP-2. Alkaline phosphatase activity was measured after 67 hours by measuring the OD405.
Western blot analysis of extracts from serum-starved HT-1080 cells, untreated and treated for 30 minutes with various concentrations of Human BMP-2, using Phospho-Smad1/5 (Ser463/465) (41D10) Rabbit mAb #9516 (upper) and Smad1 Antibody #9743 (lower).
The working concentration of BMP-2 generally ranges from 20-50 ng/ml.
Lyophilized product is very stable at -20°C. It is recommended to reconstitute with 10 mM HCl at a concentration of 0.1 mg/ml, which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
The ED50 as determined by the cytolysis of MC3T3-E1 cells is less than 50 ng/ml.
Recombinant human BMP-2 was expressed in E. coli and is supplied in a lyophilized form. A greater than 95% purity was determined by reverse-phase HPLC and SDS-PAGE.
Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs are synthesized as precursor proteins that are processed by cleavage to produce mature proteins. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5 and 8), resulting in the translocation of Smad to the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).
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