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BMPER encodes a secreted protein that interacts with, and inhibits bone morphogenetic protein (BMP) function. De plus, nous expédions BMPER Anticorps (36) et BMPER Protéines (6) et beaucoup plus de produits pour cette protéine.
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Mouse (Murine) BMPER Kit ELISA pour Sandwich ELISA - ABIN649186
Hasebe, Tanaka, Sawada, Nakajima, Ohtake, Fujiya, Kohgo: Bone morphogenetic protein-binding endothelial regulator of liver sinusoidal endothelial cells induces iron overload in a fatty liver mouse model. dans Journal of gastroenterology 2016
The bone morphogenetic protein- binding protein Cv-2 negatively regulates bone morphogenetic protein signaling.
Cv-2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling.
The NMR structure of the Danio rerio CV2 VWC1 domain in its unbound state shows the key features for high affinity binding to BMP-2 (Montrer BMP4 Kits ELISA) are a pre-oriented peptide loop.
Crossveinless 2 functions in a positive-feedback loop to locally enhance BMP activity and is required for neural crest fate determination.
LRP1 (Montrer LRP1 Kits ELISA) acts as an endocytic receptor for Bmper and a coreceptor of Bmp4 (Montrer BMP4 Kits ELISA) to mediate the endocytosis of the Bmper/Bmp4 (Montrer BMP4 Kits ELISA) signaling complex.
Binding of CV2 to Chordin (Montrer CHRD Kits ELISA) promotes BMP-2 (Montrer BMP4 Kits ELISA) signaling.
Cvl2 was identified as an essential pro-bone morphogenetic protein factor during zebrafish embryogenesis.
Bmper is a conserved regulator of hematopoietic and vascular development in zebrafish.
Initial crystallographic analysis suggests that a complete binary complex consisting of one BMP2 (Montrer BMP4 Kits ELISA) dimer bound to two crossveinless 2 (CV2) von Willebrand type C (VWC1) domains is present in the asymmetric unit.
The structure of the complex between CV-2 Von Willebrand factor (Montrer VWF Kits ELISA) type C (VWC) domain 1 and BMP-2 (Montrer BMP4 Kits ELISA), is reported.
CV2/Chordin interaction may help coordinate bone morphogenetic protein (BMP) diffusion to the ventral side of the embryo, ensuring that BMPs liberated from Chordin inhibition by tolloid proteolysis cause peak signaling levels.
Overexpression of BMPER remarkably enhanced BMP-2 (Montrer BMP2 Kits ELISA)-induced osteogenic differentiation, while suppression of BMPER effectively inhibited this process both in vitro and in vivo.
that BMPER-modulated BMP pathway activity regulates VE-cadherin (Montrer CDH5 Kits ELISA) expression and vascular barrier function
BMPER variants associated with a novel, attenuated subtype of diaphanospondylodysostosis.
BMPER-dependent pathway involved in high glucose induced alkaline phosphatase expression in vascular smooth muscle cells.
The proangiogenic BMPER effect in endothelial cells is mediated by inhibition of antiangiogenic thrombospondin-1 (Montrer THBS1 Kits ELISA) and enhanced expression and activation of the FGF signaling pathway that is crucial in the promotion of angiogenesis.
these results suggest that BMPER and Tsg maintain a fine-tuned equilibrium that controls BMP pathway activity and is necessary for vascular cell homeostasis.
BMPER is a novel regulator of the osteoblast-like differentiation of HCASMCs.
Bmper is a critical regulator of Bmp-mediated vascular inflammation and that the fine-tuning of Bmp and Bmper levels is essential in the maintenance of normal vascular homeostasis.
The data unequivocally demonstrated that BMPER is highly expressed in malignant tumors and that the growth of lung, colon, and uterine carcinomas is dependent on the presence of BMPER.
Mutual regulation by BMP-9 (Montrer GDF2 Kits ELISA) and CV2 is essential in regulating the development of the vascular endothelium.
Results identified variant SNPs in BMPER gene associated with phenotypic variation in cattle that can be used as genetic markers for breeding.
BMPER promoter polymorphisms have an effect on the intramuscular fat deposition in longissimus dorsi muscle content.
BMPER contributes to the precise control of BMP activity within the aorta-gonad-mesonephros region, enabling the maturation of hematopoietic stem cells within a BMP-negative environment.
CV2 binds directly to BMP10 (Montrer BMP10 Kits ELISA), as determined by co-immunoprecipitation, and inhibits BMP10 (Montrer BMP10 Kits ELISA) from initiating SMAD (Montrer SMAD1 Kits ELISA) signaling, as determined by luciferase reporter gene assays. BMP10 (Montrer BMP10 Kits ELISA) and CV2 have important roles in coordinating cardiomyogenesis in progenitor cells.
BMPER/low-density lipoprotein receptor-related protein 1 (Montrer LRP1 Kits ELISA) axis plays a pivotal role in pulmonary inflammatory response.
BMPER-induced BMP signaling promotes coronary artery remodeling.
BMPER appears to play a role in regulating both vessel density and cardiac development
BMPER expression is decreased following lung injury, which in turn impairs epithelial integrity, characterized by reduction of E-cadherin (Montrer CDH1 Kits ELISA) and epithelial leakage in vitro and in vivo.
Bmper may play an important role in suppressing hepcidin (Montrer HAMP Kits ELISA) production in hypotransferrinemic mice.
This gene encodes a secreted protein that interacts with, and inhibits bone morphogenetic protein (BMP) function. It has been shown to inhibit BMP2- and BMP4-dependent osteoblast differentiation and BMP-dependent differentiation of the chondrogenic cells. Mutations in this gene are associated with a lethal skeletal disorder, diaphanospondylodysostosis.
BMP-binding endothelial regulator precursor protein
, BMP binding endothelial regulator
, crossveinless 2
, BMP-binding endothelial regulator protein-like
, BMP-binding endothelial regulator protein
, bone morphogenetic protein-binding endothelial cell precursor-derived regulator