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GREM2 encodes a member of the BMP (bone morphogenic protein) antagonist family. Zusätzlich bieten wir Ihnen Gremlin 2 Antikörper (55) und Gremlin 2 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
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Through regulation of bone morphogenetic protein signaling, GREM2 is required for cardiac laterality and atrial differentiation during embryonic development.
Gremlin 2 regulates distinct roles of BMP and Endothelin 1 (zeige EDN1 Proteine) signaling in dorsoventral patterning of the facial skeleton.
Prdc is expressed in the developing eyes and the first two pharyngeal arches, in the outer layers of the optic cup, in the arch mesenchyme expands stepwise to the remaining posterior arches, and in the somites and the the swim bladder.
Grem2 knockdown inhibited cardiomyocyte differentiation, and this effect was similar to that of Notch1 (zeige NOTCH1 Proteine) pathway inhibition in vitro. Grem2 enhances the protective effect of cardiac progenitor cells on heart function in a mouse model of myocardial infarction.
Grem2 provides a molecular barrier that controls the extent of inflammatory cell infiltration by suppressing BMP2 (zeige BMP2 Proteine) after myocardial infarction.
Grem2 expression is regulated during development and embryonic stem cell differentiation.
PRDC binds heparin with high affinity and that heparin binding to PRDC interferes with BMP antagonism.
We show that Tbx2 directly represses Grem1 in distal regions of the posterior limb mesenchyme allowing Bone morphogenetic protein (Bmp) signaling to abrogate Fgf4/9/17 expression in the overlying epithelium.
Through a combination of biophysical and biochemical studies, the authors determined that PRDC forms biologically active dimers that potently inhibit BMP ligands.
The differential regulation of Gremlin2 gene expressions by BMP2 (zeige BMP2 Proteine) may explain the critical function of these genes during osteoblast differentiation.
ovarian PRDC expressed in granulosa cells could be involved in follicular development by antagonizing the actions of theca cell-derived Bone morphogenetic proteins
We propose that PRDC might serve as a mediator to antagonize BMP-4 (zeige BMP4 Proteine) signaling by Wnt (zeige WNT2 Proteine).
PRDC expression in osteoblasts suppresses differentiation and that reduction of PRDC expression promotes osteogenesis in vitro. PRDC is accordingly identified as a potential novel therapeutic target for the regulation of bone formation.
Data show that the GREMLIN 2 (GREM2) expression during Induced Pluripotent Stem Cell (hiPS) cell cardiac differentiation follows the expression pattern of cardiac-specific genes.
The structure of Grem2-GDF5 (zeige GDF5 Proteine) complex has revealed a number of key findings for DAN-family mediated BMP2 (zeige BMP2 Proteine) inhibition.
This study showed that si-Grem2 increased the BMP-2 (zeige BMP2 Proteine)-induced osteogenic differentiation of hBMSCs via the BMP-2 (zeige BMP2 Proteine)/Smad (zeige SMAD1 Proteine)/Runx2 (zeige RUNX2 Proteine) pathway.
The present study shows that the Grem2 heparin/HS and BMP2 (zeige BMP2 Proteine)-binding epitopes are unique and independent, where the Grem2-BMP2 (zeige BMP2 Proteine) complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope.
Gremlin 2 inhibits adipocyte differentiation through activation of Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) signaling
GREM2 variants have been identified in atrial fibrillation cohort studies, demonstrating abnormalities in cardiac excitation - supra ventricular tachycardia and atrial fibrillation.
The minor allele of rs4454537 is significantly associated with low bone density at the total hip of southern Chinese people. Our study further suggests GREM2 as a novel susceptibility gene for osteoporosis.
and that a genetic variant in the FMN2/GREM2 locus influences GREM2 expression in osteoblasts and thereby trabecular number and thickness as well as fracture risk.
This gene encodes a member of the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists contain cystine knots and typically form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which this gene belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein encoded by this gene is likely due to its direct binding to BMP proteins. As an antagonist of BMP, this gene may play a role in regulating organogenesis, body patterning, and tissue differentiation.
gremlin 2, cysteine knot superfamily, homolog (Xenopus laevis)
, gremlin 2, cysteine knot superfamily, homolog
, protein related to DAN and cerberus homolog
, gremlin 2, cysteine knot superfamily
, gremlin 2 homolog, cysteine knot superfamily
, cysteine knot superfamily 1, BMP antagonist 2
, protein related to DAN and cerberus
, DAN domain family member 3