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Human BMP2 Protein expressed in Escherichia coli (E. coli) - ABIN2017696
Sampath, Coughlin, Whetstone, Banach, Corbett, Ridge, Ozkaynak, Oppermann, Rueger: Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily. dans The Journal of biological chemistry 1990
Show all 18 Pubmed References
Human BMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1589575
Suliman, Xing, Wu, Xue, Pedersen, Sun, Døskeland, Nickel, Waag, Lygre, Finne-Wistrand, Steinmüller-Nethl, Krueger, Mustafa: Release and bioactivity of bone morphogenetic protein-2 are affected by scaffold binding techniques in vitro and in vivo. dans Journal of controlled release : official journal of the Controlled Release Society 2014
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Human BMP2 Protein expressed in Escherichia coli (E. coli) - ABIN413080
Sharapova, Kotnova, Galushkina, Lavrova, Poletaeva, Tukhvatulin, Tukhvatullin, Semikhin, Gromov, Soboleva, Ershova, Za?tsev, Sergienko, Lunin, Kariagina: [Production of the recombinant human bone morphogenetic protein-2 in Escherichia coli and testing of its biological activity in vitro and in vivo]. dans Molekuliarnaia biologiia 2011
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Human BMP2 Protein expressed in Escherichia coli (E. coli) - ABIN2002823
Wozney, Rosen, Celeste, Mitsock, Whitters, Kriz, Hewick, Wang: Novel regulators of bone formation: molecular clones and activities. dans Science (New York, N.Y.) 1989
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In contrast to BMP-2, BMP-7 (Montrer BMP7 Protéines) concomitantly inhibited the expression of profibrotic genes
The binding free energies indicate that ALK-3 (Montrer BMPR1A Protéines) preferably binds to BMP-2 instead of BMP-9 (Montrer GDF2 Protéines). The structural analysis shows that ALK-3 (Montrer BMPR1A Protéines) binding with BMP-2 occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 (Montrer BMPR1A Protéines) interactions with BMP-9 (Montrer GDF2 Protéines)
The results demonstrate the efficacy of HPP-GC hydrogel in minimizing the diffusive loss of rhBMP-2 from the implantation site, compared to the collagen hydroxyapatite scaffold.
The in vitro results suggest that altered BMP2 regulatory function at rs1884302 may contribute to the etiology of sagittal nonsyndromic craniosynostosis. The in vivo results indicate that differences in regulatory activity depend on the presence of a C or T allele at rs1884302.
Collectively, according to our study, rhIL-6 could induce the extracellular calcification and osteogenic differentiation of human artery smooth muscle cells through upregulating endogenous BMP2 in vitro. This may be one of the underlying mechanisms of the overwhelming vascular calcification in rheumartoid arthritis.
HUCB-MSC (Montrer MSC Protéines) transfected with mTAT/PEI were shown to express more BMP-2 protein and mRNA.
These results showed that BMP2 activated SMAD1 (Montrer GARS Protéines)/5/8 phosphorylation and up-regulated BAMBI (Montrer BAMBI Protéines) mRNA in human granulosa-lutein cells.
BMP-2 can enhance HUVEC proliferation, migration and angiogenesis through P38, ERK and Akt/m-TOR pathway.
Study shows that recombinant human bone morphogenetic protein-2 activates hippo signaling through RASSF1 (Montrer RASSF1 Protéines) in esophageal cancer cells
SNPs in BMP2 can predict grade >/= 2 or 3 RP after radiotherapy for NSCLC and improve the predictive power of MLD (Montrer ARSA Protéines) model.
widespread myocardial Bmp2 and endocardial Notch (Montrer NOTCH1 Protéines) signaling drive presumptive ventricular endocardium to differentiate into valve endocardium
CTGF (Montrer CTGF Protéines) and BMP2 are induced following myocardial ischemia in mice and humans.
Results indicate that Notch (Montrer NOTCH1 Protéines) signaling induces cell cycle arrest and thereby initiates chondrocyte cell enlargement via bone morphogenetic protein 2 (BMP2) signaling.
Collectively, our findings indicate that CBFA2T2 (Montrer CBFA2T2 Protéines) is required for BMP-2-induced osteogenic differentiation of MSCs through inhibition of EHMT1 (Montrer EHMT1 Protéines)-mediated histone methylation at Runx2 (Montrer RUNX2 Protéines) promoter.
The data suggest that SDF-1beta provides synergistic effects supporting BMP-2-induced, BMSC-mediated bone formation and appears suitable for optimization of bone augmentation in combination therapy protocols.
study revealed that only BMP-6 (Montrer BMP6 Protéines) was able to induce bone formation at the used dose and that the addition of IGF-1 (Montrer IGF1 Protéines) contributed to an increase of the mineralization in the implants. Hence, the combination of BMP-6 (Montrer BMP6 Protéines) with IGF-1 (Montrer IGF1 Protéines) might be a better alternative than BMP-2 for orthopedic surgery or bone tissue engineering approaches.
BMP2 may induce osteogenic differentiation.
Increased bone mass in Crmp4 (Montrer DPYSL3 Protéines)(-/-) mice was associated with enhanced BMP2 signaling and BMP2-induced osteoblast differentiation in Crmp4 (Montrer DPYSL3 Protéines)(-/-) osteoblasts (OBs (Montrer LEP Protéines)).
Deletion of the "ultra-conserved sequence" within the 3'UTR of the Bmp2 was associated with elevated Bmp2 mRNA and BMP signaling levels, reduced fitness, and embryonic malformations.
Bone morphogenetic protein 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.
Bmp antagonists and morpholinos designed against Bmp4, Bmp2, and Bmp7 demonstrate that Bmp signaling is critical for ventral, but not dorsoanterior endoderm formation
High BMP2 expression is associated with cystic ovarian disease.
both FSH (Montrer BRD2 Protéines) and BMP-2 reduced follicular mRNA expression of GDF9 (Montrer GDF9 Protéines) and NLRP5 when compared to follicles cultured in media containing only FSH (Montrer BRD2 Protéines)
The BMP2/4 (Montrer BMP4 Protéines) ligand and receptor system presides within bovine trophectoderm prior to uterine attachment.
concluded that a bone morphogenetic protein (BMP)-signaling system, consisting of BMP2, BMP4, type II and I receptors, is present in bovine antral follicles and plays a role in development and functioning of follicles rather than oocyte maturation
The transfecting capability of a BMP-2 specific vector is examined and supports the idea that BMP-2 might diminish osseointegration and implant fixation.
While BMP2 expression begins at (pregastrulation) stage 1 in the hypoblast, BMP4 (Montrer BMP4 Protéines) expression commences--distinctly delayed compared to the mouse--diffusely at (pregastrulation) stage 2; from stage 3 onwards.
Maxillary sinus floor elevation using BMP-2 gene-modified bone marrow stromal cells and TCP in rabbits
Data show that BMP-2, BMP-4 (Montrer BMP4 Protéines), and BMP-7 (Montrer BMP7 Protéines), noggin (Montrer NOG Protéines), and chordin (Montrer CHRD Protéines) were colocalized in rimming osteoblasts, osteoclasts, and chondrocytes.
BMP2 is not suitable to regenerate osteochondral lesions completely
High yield isolation of BMP-2 from bone and in vivo activity of a combination of BMP-2/TGF-beta1 (Montrer TGFB1 Protéines).
Report temporal regulation of BMP2 mRNA expression in the oocyte, granulosa and theca cells of developing preovulatory follicles in the pig.
Regional variation of periosteal activity at the mandibular ramus is regulated by differential induction of BMP2.
The effects of soy- and cow's milk-based formulas compared to nursing on bone development through BMP2 expression in neonatal pigs are reported.
The effect of bone morphogenetic protein (BMP) 12 and BMP2 expression on differentiation of bone marrow-derived mesenchymal stem cells and superficial digital flexor tenocytes is reported.
Study found that BMP-2 (Montrer BMP4 Protéines) is negatively regulated by miR (Montrer MYLIP Protéines)-140 during early embryogenesis and bone development in zebra fi sh.
Structures of Bmp2a, Bmp2b (Montrer BMP4 Protéines), Bmp4 (Montrer BMP4 Protéines) and Bmp16 were found to be remarkably similar; with residues involved in receptor binding being highly conserved.
bmp2a is a crucial player in the specification of the ventral pancreatic bud in zebrafish embryos.
results indicate that both the induction of a photoreceptor fate and the interaction with Notch (Montrer NOTCH1 Protéines) relies on a canonical BMP/Smad5 (Montrer SMAD5 Protéines) pathway
Mypt1 (Montrer PPP1R12A Protéines) mediates coordination between mesoderm and endoderm cell movements in order to carefully position the liver primordium such that it receives a Bmp2 (Montrer BMP4 Protéines) signal that is essential for liver formation
The protein encoded by this gene belongs to the transforming growth factor-beta (TGFB) superfamily. The encoded protein acts as a disulfide-linked homodimer and induces bone and cartilage formation.
, bone morphogenetic protein 2A
, bone morphogenetic protein 2 B
, bone morphogenetic protein 2-B
, bone morphogenetic protein 2
, Bone morphogenetic protein 2
, bone morphogenetic protein 2-like
, bone morphogenetic protein 2 precursor (BMP-2) (BMP-2A)