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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.
In contrast to BMP-2 (show BMP2 Proteins), BMP-7 concomitantly inhibited the expression of profibrotic genes
On the contrary, BMP7 specific antibody inhibits the HNK-induced activation of p53 (show TP53 Proteins) in colon cancer cells and partly decreases the total level of p53 (show TP53 Proteins). Our findings suggested that HNK may be a promising anticancer drug for CRC (show CALR Proteins); activation of p53 (show TP53 Proteins) plays an important role in the anticancer activity of HNK, which may be initialized partly by the HNK-induced upregulation of BMP7.
All isoforms of type I and type II BMP receptors were expressed in both Ca9 (show CA9 Proteins)-22 and HSC3 cells and BMP7 stimulation resulted in the phosphorylation of Smad1 (show GARS Proteins)/5/8 in both cell lines
the results of the present study indicate that BMP7 may inhibit excessive scar formation via activation of the BMP7/Smad1 (show GARS Proteins)/5/8 signaling pathway.
BMP7, in particular combined with MSC (show MSC Proteins), seems to have a favourable application also in periodontal regeneration.
Synergistic effects of BMP-2 (show BMP2 Proteins), BMP-6 (show BMP6 Proteins) or BMP-7 with human plasma fibronectin (show FN1 Proteins) onto hydroxyapatite coatings.
Implantation of morphogenetic protein-7 (BMP-7) gene activated fat tissue fragments can elicit regeneration of large bone defects in rats and could become a clinically expeditious strategy for in vivo bone tissue engineering.
the present results showed that OP-1 might serve as a biochemical parameter for determining disease severity in primary knee Osteoarthritis (OA). Further studies with larger sample size need to be carried out to confirm OP-1 as a marker of disease status. Studies are required to be done to examine the genetic and lifestyle factors that may contribute to the development of knee OA
BMP7-Based Functionalized Self-Assembling Peptides Protect Nucleus Pulposus-Derived Stem Cells From Apoptosis In Vitro
results showed that the expression of cartilage-associated markers in ESC-MSCs induced by the TGFbeta1 (show TGFB1 Proteins) and BMP7 combination was increased compared to induction with TGFbeta1 (show TGFB1 Proteins) alone. The TGFbeta1 (show TGFB1 Proteins) and BMP7 combination upregulated the expression of TGFbeta (show TGFB1 Proteins) receptor and the production of endogenous TGFbetas compared to TGFbeta1 (show TGFB1 Proteins) induction.
BMP 7 is a key regulator of Tmem100-mediated cell proliferation in metanephric mesenchymal cells.There is a complicated regulation network among Tmem100, BMP7, and BMPR-II (show BMPR2 Proteins) in mouse embryonic kidney-derived cells.
Overexpression of miR (show MLXIP Proteins)-384-5p significantly decreased BMP7 protein, while depletion of miR (show MLXIP Proteins)-384-5p significantly increased BMP7 protein in renal epithelial cells.
Bone morphogenetic protein 7 (BMP7) exerts differential effects depending on the concentration; it may expand mesenchymal cells in the stroma where BMP7 concentration is low and may upregulate cadherin-11 promoting condensation around the tip of ureteric buds.
BMP-7 therefore is an attractive candidate for tackling a multifaceted disease such as diabetes, since it not only reduces body fat, but also strengthens insulin (show INS Proteins) signaling, causing improved glucose uptake and ameliorating peripheral insulin (show INS Proteins) resistance.
Our studies indicate that BMP7 is an important factor during the process of implantation that contributes to healthy embryonic development.
Western blot analysis demonstrated that following BMP2 (show BMP2 Proteins) and BMP7 cotransfection of MC3T3E1 cells, the protein expression levels of BMP2 (show BMP2 Proteins), BMP4 (show BMP4 Proteins), BMP6 (show BMP6 Proteins), BMP7, BMP9 (show GDF2 Proteins) and Wnt3a (show WNT3A Proteins) were increased compared with control cells
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
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.
BMP7 enhances the effect of BMSCs on extracellular matrix remodeling in a rabbit model of intervertebral disc degeneration.
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