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anti-Human GDF2 Antibodies:
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Human Polyclonal GDF2 Primary Antibody for IHC (p), ELISA - ABIN544843
Miller, Harvey, Thies, Olson: Bone morphogenetic protein-9. An autocrine/paracrine cytokine in the liver. in The Journal of biological chemistry 2000
Show all 3 Pubmed References
Human Polyclonal GDF2 Primary Antibody for IHC (p), WB - ABIN388817
Herrera, van Dinther, Ten Dijke, Inman: Autocrine bone morphogenetic protein-9 signals through activin receptor-like kinase-2/Smad1/Smad4 to promote ovarian cancer cell proliferation. in Cancer research 2009
Show all 5 Pubmed References
Human Polyclonal GDF2 Primary Antibody for ELISA - ABIN449713
Scharpfenecker, van Dinther, Liu, van Bezooijen, Zhao, Pukac, Löwik, ten Dijke: BMP-9 signals via ALK1 and inhibits bFGF-induced endothelial cell proliferation and VEGF-stimulated angiogenesis. in Journal of cell science 2007
Human Polyclonal GDF2 Primary Antibody for WB - ABIN4256550
David, Mallet, Keramidas, Lamandé, Gasc, Dupuis-Girod, Plauchu, Feige, Bailly: Bone morphogenetic protein-9 is a circulating vascular quiescence factor. in Circulation research 2008
BMP9 promoted the expression of ECM in NPCs via inhibition of Notch1 and DLL1
Case-control analyses reveal significant overrepresentation of rare variants in ATP13A3, AQP1 and SOX17, and provide independent validation of a critical role for GDF2 in heritable pulmonary arterial hypertension.
Low BMP9 expression is associated with breast cancer.
BMP-9 was found the most effective to induce osteogenic transdifferentiation of fat tissue in vitro
Epigenetic Regulation of GDF2 Suppresses Anoikis in Ovarian and Breast Epithelia.
levels of the angiogenesis mediators endoglin, HB-EGF, BMP-9 and FGF-2 in patients with severe sepsis and septic shock
BMP9 is highly expressed in bladder cancer cells. BMP9 promotes bladder cancer cell proliferation and migration through up-regulation of lncRNA UCA1.
Bone morphogenetic protein 9 (BMP9) was identified as a target of miR-149 in MG63 cells, and BMP9 expression was negatively correlated with miR149 level in osteosarcoma clinical samples. miR-149 promotes osteosarcoma progression via targeting BMP9.
The binding free energies indicate that ALK-3 preferably binds to BMP-2 instead of BMP-9. The structural analysis shows that ALK-3 binding with BMP-2 occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 interactions with BMP-9
The BMP9-induced phosphorylation of Smad1/5/8 was increased with the overexpression of RUNX3, and yet was decreased with the knockdown of RUNX3. Collectively, our findings suggest that RUNX3 is an essential modulator of the BMP9-induced osteoblast lineage differentiation of mesenchymal stem cells (MSCs).
BMP9 is overexpressed in hepatic stellate cells in a cohort of liver fibrosis patients.
our study indicates that BMP9 can inhibit the growth and metastasis of breast cancer cells, which may be related to interaction between pre-adipocytes/adipocytes and MDA-MB-231 cells via leptin signaling pathway.
BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation.
this is the first study that accurately identifies BMP9 as a profibrotic factor in fibroblasts.
the combination of BMP-9 and MC-GAG stimulates chondrocytic and osteogenic differentiation of hMSCs.
The results from this study demonstrate that the use of rhBMP9 significantly and markedly induced osteoblast differentiation when compared to rhBMP2 and
The results demonstrate that although BMP9 alone does not influence leukocyte recruitment, it primes the vascular endothelium to mount a more intense response when challenged with LPS through an increase in TLR4, E-selectin, and VCAM-1 and ultimately through enhanced leukocyte recruitment.
Data suggest BMP9/GDF2 and BMP10 synergize with TNFA to increase monocyte recruitment to vascular endothelial cells; process appears to be mediated mainly via ALK2/ACVR1 (which exhibits protein kinase activity). These studies used in vitro flow monocyte adhesion assay. (BMP9 = growth differentiation factor 2; BMP10 = bone morphogenetic protein 10; TNFA = tumor necrosis factor alpha; ALK2/ACVR1 = activin A receptor type 1)
These results suggest that BMP9-transduced calvarial mesenchymal progenitor cells seeded in a PPCN-g thermoresponsive scaffold is capable of inducing bone formation in vivo and is an effective means of creating tissue engineered bone for critical sized defects.
circulating levels significantly decreased in type 2 diabetes mellitus patients and associated with glucose homoeostasis and insulin sensitivity
BMP9 stimulates regeneration of a synovial joint that forms an articulation with the stump bone.
suggests that Hmox1 is likely to potentiate osteogenic differentiation and yet decrease adipogenic differentiation induced by BMP9 possibly through regulation of multiple signaling pathways
our data show that in a tumor environment BMP9 and BMP10 play different roles and thus blocking their shared receptor ALK1 is maybe not appropriate. Indeed, BMP9, but not BMP10, acts as a quiescence factor on tumor growth, lung metastasis and vessel normalization.
These results suggest that RUNX1 may be an essential modulator in BMP9- induced osteogenic differentiation of mesenchymal stem cells.
results provide a better understanding into how BMP-9 induces osteoblast differentiation and its synergy with IGF-2 at the signaling level.
Our findings provide a clearer understanding of the cellular pathways utilized by BMP-9 for chondrogenesis that may help improve current therapies for regenerative cartilage repair.
Constitutive expression of low levels of BMP-9 stabilises hepatocyte function in the healthy liver. High levels of BMP-9 cause enhanced damage upon acute or chronic injury.
Notch signaling may play an important role in BMP9-induced osteogenesis and angiogenesis. It's conceivable that simultaneous activation of the BMP9 and Notch pathways should efficiently couple osteogenesis and angiogenesis of MSCs for successful bone tissue engineering.
Western blot analysis demonstrated that following BMP2 and BMP7 cotransfection of MC3T3E1 cells, the protein expression levels of BMP2, BMP4, BMP6, BMP7, BMP9 and Wnt3a were increased compared with control cells
he results of the present study demonstrated that BMP9 promoted the osteoclast differentiation of osteoclast precursors via binding to the ALK1 receptor on the cell surface, and inhibiting the ERK1/2 signaling pathways in the cell
that Dkk1 negatively regulates BMP9-induced osteogenic differentiation.
Data show athat beta-catenin can be activated by bone morphogenetic protein 9 (BMP9) and the activation of beta-catenin plays an important role in the differentiation of C3H10T1/2 cells into cardiomyocyte-like cells induced by BMP9.
miR23b inhibits BMP9induced C2C12 myoblast osteogenesis via targeting of the Runx2 gene, acting as a suppressor.
We have established a producer line that stably expresses a high level of active BMP9 protein. Such producer line should be a valuable resource for generating biologically active BMP9 protein for studying BMP9 signaling
Data show that microRNA miR-21 was significantly upregulated by bone morphogenetic protein 9 (BMP9) during the osteogenesis the multilineage cells (MMCs) by suppressing Smad7 protein.
Hh signaling is involved and plays a regulatory role in the osteogenic differentiation of MSCs induced by BMP9.
data indicate that BMP9 and BMP13 (BMP9 might be more effective) promoted the differentiation of C3H10T1/2 cells into cardiomyocyte-like cells
BMP9/ALK1 augmented vasculogenesis and angiogenesis, and thereby enhanced neovascularization. Thus, we suggest that BMP9/ALK1 may improve the efficacy of EPC-based therapies for treating ischemic diseases.
result was supported by the identification of the regulation by BMP9 and BMP10 of several genes known to be involved in this process
The protein encoded by this gene is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Studies in rodents suggest that this protein plays a role in the adult liver and in differentiation of cholinergic central nervous system neurons.
bone morphogenetic protein 9
, growth/differentiation factor 2