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The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Additionally we are shipping BMP7 Antibodies (282) and BMP7 Kits (60) and many more products for this protein.
Showing 10 out of 63 products:
Human BMP7 Protein expressed in CHO Cells - ABIN2666468
Hao, Cai, Lv, Huang, Li: Oral administration of recombinant adeno-associated virus-mediated bone morphogenetic protein-7 suppresses CCl(4)-induced hepatic fibrosis in mice. in Molecular therapy : the journal of the American Society of Gene Therapy 2012
Show all 5 references for ABIN2666468
Human BMP7 Protein expressed in Escherichia coli (E. coli) - ABIN666736
González, Lund, Martin, McCartney, Tondravi, Sampath, Hruska: Treatment of a murine model of high-turnover renal osteodystrophy by exogenous BMP-7. in Kidney international 2002
Show all 2 references for ABIN666736
Human BMP7 Protein expressed in Wheat germ - ABIN1346771
Myllärniemi, Lindholm, Ryynänen, Kliment, Salmenkivi, Keski-Oja, Kinnula, Oury, Koli: Gremlin-mediated decrease in bone morphogenetic protein signaling promotes pulmonary fibrosis. in American journal of respiratory and critical care medicine 2008
BMP inhibition is sufficient for neural induction in vivo, and that in the absence of ventral BMPs, Spemann organizer signals are not required for brain formation.
Bmp7 gradients steer nerve growth cones by a balancing act of limk1 (show LIMK1 Proteins) and SSH on AD/cofilin (show CFL1 Proteins).
Bmp antagonists and morpholinos designed against Bmp4, Bmp2, and Bmp7 demonstrate that Bmp signaling is critical for ventral, but not dorsoanterior endoderm formation
these data support a model in which Tfap2a (show TFAP2A Proteins), acting through Bmp7a, modulates Fgf and Notch (show NOTCH1 Proteins) signaling to control the duration, amount and speed of SAG (show SAG Proteins) neural development.
maternally supplied Smad5 (show SMAD5 Proteins) is already required to mediate ventral specification prior to zygotic Bmp2 (show BMP4 Proteins)/7 signaling to establish the initial dorsoventral asymmetry
Cloning and expression of a second zebrafish bmp7 homolog, bmp7b.
The disequilibrium between BMP-7 and TGF-beta (show TGFB1 Proteins) signals plays a relevant role in the LV remodelling response to haemodynamic stress in aortic stenosis patients with left ventricular hypertrophy/dysfunction.
BMP7 may partly mediate the antiproliferative effect of oridonin by activating p38 MAPK (show MAPK14 Proteins) in colon cancer cells.
Data show that interaction of fibrillin-1 (show FBN1 Proteins) with the bone morphogenetic protein 7 (BMP-7) complex results in a conformational change.
the role of BMP-7 and its downstream signals in the neuroprotective effects of oxygen-glucose deprivation preconditioning
miR (show MLXIP Proteins)-137/BMP7 axis could contribute to the progression of non-small cell lung cancer.
Inhibition of BMP7 expression mediated by KDM5C (show KDM5C Proteins) promotes neoplasm invasion in hepatocellular carcinoma cells.
Adenovirus-mediated FoxC2 (show FOXC2 Proteins) expression enhances BMP7-facilitated anabolism in nucleus pulposus cells of the intervertebral discs.
Heterodimeric BMP-2 (show BMP2 Proteins)/7 significantly promoted osteogenesis of human adipose-derived stem cells in vitro and in vivo. However, BMP-2 (show BMP2 Proteins)/7 was not found to be a stronger inducer of osteogenesis compared to homodimeric either BMP-2 (show BMP2 Proteins) or BMP-7.
ANGPTL4 (show ANGPTL4 Proteins) might promote metastasis and might inhibit apoptosis of colorectal cancer cells by up-regulation of BMP7.
MiR (show MLXIP Proteins)-22 promotes the development of liver cirrhosis through BMP7 suppression.
The disequilibrium between BMP-7 and TGF-beta (show TGFB1 Proteins) signals plays a relevant role in the LV remodelling response to haemodynamic stress in mice subjected to transverse aortic constriction leading to left ventricular hypertrophy/dysfunction.
the in vivo inter-relationships between Bmp7 and Usag-1 (show SOSTDC1 Proteins), was examined.
only BMP7, not BMP2 (show BMP2 Proteins) or BMP4 (show BMP4 Proteins), is necessary for interdigital programmed cell death
odontoblast beta-catenin signaling may act through regulation of BMP signaling to maintain the integrity of HERS cells
BMP7 and FGF9 coordinately regulate AP-1 (show JUN Proteins) transcription to promote G1-S cell cycle progression and nephron progenitor cells proliferation.
Gdf-5 (show GDF5 Proteins) induced the expression of the alpha5 sub-unit, while Bmp-7 induced the expression of the alphaV sub-unit.
BMP7 induced changes in levels of mRNA and proteins associated with reactive gliosis in retinal astrocytes and Muller glial cells, including glial fibrillary acidic protein (show GFAP Proteins), glutamine synthetase (show GLUL Proteins), chondroitin sulfate proteoglycans and MMPs.
We found that the recruited macrophages are polarized to a M2 subtype after renal injury. M2 macrophages released high levels TGFb1 (show TGFB1 Proteins) to suppress BMP7 to enhance EMT (show ITK Proteins)-induced renal fibrosis.
Bmp4 (show BMP4 Proteins), Bmp7 and bmpr2 (show BMPR2 Proteins) signalling regulates the pre-implantation development of extra-embryonic cell lineages in the mouse embryo.
Study detected a 5-bp insertion-deletion at 602 bp upstream from the transcription start site of the BMP7 gene promoter among 258 pigs of 3 breeds; based on correlation analysis, the 5-bp indel site does not significantly affect porcine reproductive traits.
These results suggest that g.35161T>C is a potential candidate gene locus for litter size traits and the BMP7 gene might be associated with the quantitative trait locus controlling the litter size.
the combined treatment with TGF-beta1 (show TGFB1 Proteins) and BMP-7 or treatment first with TGF-beta1 (show TGFB1 Proteins) followed by BMP-7 was more effective than other treatment groups in both chondrogenic differentiation and SZP (show PRG4 Proteins) secretion.
Some single nucleotide polymorphisms and haplotypes in BMP7 are associated with cattle growth traits.
Data report that BMP-7 suppresses granulosa cell apoptosis by inhibiting the release of caspase-activated DNase (CAD (show DFFB Proteins)) via a mechanism which does not appear to be associated with the mitochondrial pathway, whereas BMP-4 (show BMP4 Proteins) inhibits the release of CAD.
Data show that BMP-2 (show BMP2 Proteins), BMP-4 (show BMP4 Proteins), and BMP-7, noggin (show NOG Proteins), and chordin (show CHRD Proteins) were colocalized in rimming osteoblasts, osteoclasts, and chondrocytes.
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development and possible bone inductive activity.
bone morphogenetic protein 7 (osteogenic protein 1)
, bone morphogenetic protein 7
, osteogenic protein 1
, bone moorphogenic protein-7