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Recombinant Human Bone Morphogenetic Protein -2 (BMP2)
(Cat. No.: C012)
Belongs to the Bone-growth regulatory factors that are members of the transforming growth factor-beta (TGF-beta) superfamily of proteins. They are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. The active form can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
Recombinant Human Bone Morphogenetic protein-2 produced in E. coli is a homodimeric, non-glycosylated, Polypeptide chain containing 115 amino acids and having a molecular mass of 26018 Dalton.
Biological activity: BMP-2 is fully biologically active when compared to standard. The ED50 as determined by the cytolysis of MC3T3-E1 cells is less then 50 ng/ml, corresponding to a specific activity of 2.0 x 104 IU/mg
Purity: Greater than 95% as determined by
(a) Analysis by SEC-HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
Amino-Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Met-Gln-Ala-Lys-His.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of Bone Morphogenetic protein-2.
Formulation: BMP2 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.
Storage: Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution BMP2 should be stored at 4oC between 2-7 days and for future use below -18oC. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Reconstitution: It is recommended to reconstitute the lyophilized rHuBMP2 in sterile 20mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
1: Shanghai Kou Qiang Yi Xue 2008
[Study of cbfalpha1 on the expression of extracellular matrix proteins in dental papilla cells induced by BMP-2 in vitro.]
[Abstract] PURPOSE: To evaluate the function of cbfalpha1 on BMP-2 signaling to extracellular matrix proteins in dental papilla cells in vitro. METHODS: RT-PCR and Western blot were performed to detect the expression of ALP, OC, ON, OPN, BSP, DMP-1 and DSPP in cultured dental papilla cells induced by 200ng/mL BMP-2 and/or down-regulated by cbfalpha1 antisense technology, the results were analysed with SPSS 11.0 software package. RESULTS: We found that the amount of ALP and OC and the expression of OPN, BSP and ON were upregulated significantly after the cells were treated with BMP-2. After transfected with antisense cbfalpha1, the cells downreguleted the expression of ALP, OC, OPN and BSP significantly(P<0.01). CONCLUSIONS: As a kind of transcription factor, cbfalpha1
could be an important tache in the BMP-2 signal networks controlling cells differentiation and mineralization.Supported by National Natural Science Foundation of China (Grant No.30772416).
2: Life Sci 2008 Dec;
Bone morphogenetic protein-2 induces the differentiation of a mesenchymal progenitor cell line, ROB-C26, into mature osteoblasts and adipocytes.
[Abstract] AIMS: Osteoblasts and adipocytes originate from common precursor cells. We examined the effects of bone morphogenetic protein-2 (BMP-2) on the molecular mechanisms governing the diametric actions of BMP-2 on simultaneous mature osteoblast and adipocyte differentiation in a clonal mesenchymal progenitor cell line, ROB-C26 (C26). MAIN METHODS: The present study using RT-PCR, Western blotting and ELISA investigated the effects of BMP-2 on transcription factors for osteoblasts (Runx2, Dlx5, Osterix, Msx2 and AJ18) and adipocytes (PPARgamma2), osteoblastic markers, alkaline phosphatase (ALP), bone sialoprotein (BSP) and osteocalcin (OC), and adipocyte differentiation-dependent protein, aP2 in C26 cells. KEY FINDINGS: BMP-2 increased not only mRNA and protein
expressions of Dlx5 followed by inducing Osterix and BSP levels in a dose- and time-dependent manner with an increase in Runx2, Msx2, AJ18, ALP and OC levels, but also induced PPARgamma2 and aP2 levels. At the light microscopic level, BMP-2 induced mature osteoblastic and adipogenic differentiation in the C26 cultures not only by an increase in the number of ALP-positive osteoblasts, in their staining intensity and in the number of mature adipocytes with Oil Red O-positive lipid droplets, but also mineralized matrix formation of the cultures assessed by detecting an increase in calcium concentration and the formation of Alizarin Red S-positive mineralization nodules. SIGNIFICANCE: These results indicate that BMP-2 induces the differentiation of C26 mesenchymal progenitors into mature
osteoblasts and adipocytes and the usefulness of this cell line for studying the regulatory mechanism of osteoblast and adipocyte differentiation from common mesenchymal progenitors.
3: Mol Biol (Mosk) ;Vol 42(6)
[NF-kappaB modulates activation of the BMP-2 gene by trichostatin A]
[Abstract] In this study, we investigated trichostatin A (TSA), a histone deacetylase inhibitor, increased the Bone morphogenetic protein-2 (BMP-2) mRNA level in human osteoblasts line. Deletion analysis of the promoter region revealed that TSA-induced luciferase was regulated by the BMP-2 promoter spanning from -320 to-310. Electrophoresis mobility shift assay (EMSA) and Chromatin immunoprecipitation (CHIP) assay proved that this position was nuclear factor NF-kappaB responsive element. The results above demonstrated that acetylation plays a crucial role in BMP-2 expression and acetylation of NF-kappaB p65 and p50 subunits by TSA treatment may activate the BMP-2 promoter.
4: J Cell Biol 2009 Jan;Vol 184(1)
Bone morphogenetic protein 2 induces pulmonary angiogenesis via Wnt-beta-catenin and Wnt-RhoA-Rac1 pathways.
[Abstract] Mutations in bone morphogenetic protein (BMP) receptor II (BMPRII) are associated with pulmonary artery endothelial cell (PAEC) apoptosis and the loss of small vessels seen in idiopathic pulmonary arterial hypertension. Given the low penetrance of BMPRII mutations, abnormalities in other converging signaling pathways may be necessary for disease development. We hypothesized that BMPRII supports normal PAEC function by recruiting Wingless (Wnt) signaling pathways to promote proliferation, survival, and motility. In this study, we report that BMP-2, via BMPRII-mediated inhibition of GSK3-beta, induces beta-catenin (beta-C) accumulation and transcriptional activity necessary for PAEC survival and proliferation. At the same time, BMP-2 mediates phosphorylated
Smad1 (pSmad1) or, with loss of BMPRII, pSmad3-dependent recruitment of Disheveled (Dvl) to promote RhoA-Rac1 signaling necessary for motility. Finally, using an angiogenesis assay in severe combined immunodeficient mice, we demonstrate that both beta-C- and Dvl-mediated RhoA-Rac1 activation are necessary for vascular growth in vivo. These findings suggest that the recruitment of both canonical and noncanonical Wnt pathways is required in BMP-2-mediated angiogenesis.
Protein Accession No.:
MQAKH KQRKR LKSSC KRHPL YVDFS DVGWN DWIVA PPGYH AFYCH GECPF PLADH LNSTN HAIVQ TLVNS VNSKI PKACC VPTEL SAISM LYLDE NEKVV LKNYQ DMVVE GCGCR
*NOTE: ALL PRODUCTS ARE FOR RESEARCH USE ONLY