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Human Polyclonal GREM1 Primary Antibody for IHC (p), IHC - ABIN252810
Okamoto, Lezhava, Hosaka, Okamoto-Hosoya, Ochi: Enhanced expression of S-adenosylmethionine synthetase causes overproduction of actinorhodin in Streptomyces coelicolor A3(2). in Journal of bacteriology 2003
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Human Polyclonal GREM1 Primary Antibody for WB - ABIN966222
Stabile, Mitola, Moroni, Belleri, Nicoli, Coltrini, Peri, Pessi, Orsatti, Talamo, Castronovo, Waltregny, Cotelli, Ribatti, Presta: Bone morphogenic protein antagonist Drm/gremlin is a novel proangiogenic factor. in Blood 2007
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Human Polyclonal GREM1 Primary Antibody for IHC (p), ELISA - ABIN545640
Wordinger, Fleenor, Hellberg, Pang, Tovar, Zode, Fuller, Clark: Effects of TGF-beta2, BMP-4, and gremlin in the trabecular meshwork: implications for glaucoma. in Investigative ophthalmology & visual science 2007
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Human Monoclonal GREM1 Primary Antibody for ELISA, WB - ABIN565294
Sha, Zhang, Zhang, Wan, Zhao, Li, Lang: Elevated levels of gremlin-1 in eutopic endometrium and peripheral serum in patients with endometriosis. in Fertility and sterility 2009
Human Polyclonal GREM1 Primary Antibody for IF (p), IHC (p) - ABIN687082
Wellbrock, Sheikhzadeh, Oliveira-Ferrer, Stamm, Hillebrand, Keyser, Klokow, Vohwinkel, Bonk, Otto, Streichert, Balabanov, Hagel, Rybczynski, Bentzien, Bokemeyer, von Kodolitsch, Fiedler: Overexpression of Gremlin-1 in patients with Loeys-Dietz syndrome: implications on pathophysiology and early disease detection. in PLoS ONE 2014
FGF signaling in establishment of the developmental hematopoietic stem cell niche occurs via inhibition of bmp4 transcription, and activation of bmp antagonists, nog2 and grem1a.
Results suggest that the negative regulatory loops between BMP/Tbx2 and Gremlin or Hey1 are responsible for defining the territory of the pronephric nephron.
Gremlin encodes a maternal transcript, and the zygotic transcription is turned on at the mid-blastula transition.
remlin can aggravate podocyte lesions through the TGF-beta signaling pathway.
We conclude that gremlin promotes RPE cell proliferation, migration and VEGF production possibly via activating VEGFR2-Akt-mTORC2 signaling. Gremlin could be a novel therapeutic target of ROP or other retinal vasoproliferation diseases.
Wild-type gremlin is able to bind broadly across the various regions of kidney in an heparin sulfate-dependent manner, with particularly intense binding to tubular structures in the renal cortex. In a model of chronic kidney disease, fibrotic changes in the kidney result in a loss of gremlin binding sites. Gremlin mutants with reduced affinity for heparin showed negligible binding under the same conditions.
involved in regulation of bone morphogenetic protein activities in cartilage tissues in the adult skeleton
Gremlin1 accelerates hepatic stellate cell activation through upregulation of TGF-B1, alpha-SMA, and COL1a1 expression in a liver fibrosis disease model.
Grem1 expression in the tubular epithelial compartment plays a significant role in the fibrotic response to renal injury in vivo.
Gremlin-1 protein expression was detected specifically in the lung after birth and did not result in any signs of respiratory insufficiency. CXCL10 chemokine levels correlate negatively with gremlin-1 levels in mouse and human lung.
Data show that parathyroid hormone-related protein (PTHrP) regulates gremlin levels in pancreatic acinar and stellate cells.
Gremlin is a key pro-fibrogenic factor in chronic pancreatitis
Gremlin/VEGFR2 axis participates in renal inflammation and could be a novel target for kidney disease.
GREM1 induces fibrosis and angiogenesis in mouse peritoneum and is associated with increased solute transport in peritoneal dialysis patients.
Grem1 expression identifies distinct connective tissue stem cells in both the bone (osteochondroreticular stem cells) and the intestine (reticular stem cells).
A Gli-dependent cis-regulatory module (CRM), regulation of Grem1 in the mouse limb bud, is reported.
Suggest cross-talk between angiogenesis and inflammation and demonstrate a crucial role of CREB activation in the modulation of the VEGFR2-mediated proinflammatory/proangiogenic response of endothelial cells to gremlin.
The present data disclose that Gremlin-1 is an endogenous antagonist of MIF and define a role for Gremlin-1/MIF interaction in atherosclerosis.
endogenous Gremlin blockade inhibited TGF-beta-mediated matrix production and epithelial mesenchymal transition in kidney fibroblasts
gremlin was clearly elevated in high glucose cultured mouse podocytes, and likely employed endogenous canonical TGFbeta1/Smad signaling to induce podocyte injury. Knockdown gremlin1 by siRNA may be clinically useful in the attenuation of podocyte injury.
This study establishes that distant cis-regulatory regions scattered through a larger genomic landscape control the highly dynamic expression of Grem1, which is key to normal progression of mouse limb bud development.
The results demonstrate a non-redundant role for alpha(v)beta(3) in gremlin-induced angiogenesis.
Gremlin1 was down-regulated by BMP2
Wattles in goats are associated with the FMN1/GREM1 region on chromosome 10
We resequenced DNA from 397 sub-Saharan Africans with CL/P and 192 controls using Sanger sequencing. Following analyses of the sequence data, we observed 2 novel coding variants in GREM1. These variants were not found in the 192 African controls and have never been previously reported.
Gremlin 1 is overexpressed in pancreatic cancer (PC) tissue and correlates with poor clinical prognosis. Its expression is regulated by a paracrine SHH signaling. In vitro experiments suggest that Gremlin 1 promoted the proliferation, migration, invasion and epithelial-mesenchymal transformation of pancreatic cancer cells.
an interaction between the BMP2-Gremlin and SLIT2 pathways in human kidney cells
the GREM1rs1258763 polymorphism was significantly associated with the risk of non-syndromic orofacial cleft in the Chinese population.
High gremlin1 expression is associated with gastric cancer.
study suggested that GREM1 delivered by MSCs promoted EMT in esophageal squamous cell carcinoma in vitro and in vivo, which is partly through TGF-beta/BMP signaling pathway.
COX-2, GREM1, and HAS2 are cumulus cell genes that potentially determine oocyte and embryo developmental competence. (Review)
Results indicate that Gremlin1 could be involved in gastric cancer (GC) progression and may be a good marker of long-term survival in GC.
Platelet derived Gremlin-1 might contribute to the elevated circulating levels of Gremlin-1 in acute coronary syndromes and serve as a thrombo-inflammatory mediator in cardiovascular pathophysiologies.
gremlin protects skin cells from UV damages via activating VEGFR2-Nrf2 signaling
Gene duplication upstream of GREM1 was screened for in all sixty-five SPS individuals with no carriers being identified.
Nox1-SHH-Grem1 signaling axis in pulmonary vascular endothelium that is likely to contribute to Pulmonary hypertension.
GREM1 plays an important role in the development of glioma, and it may serve as a potential target in glioma therapy.
Describe a hereditary mixed polyposis syndrome in which is characterized by SCG5-GREM1 duplication.
GREM1 is frequently expressed by myofibroblasts in scars or in the stroma of basal cell carcinomas, suggesting that GREM1 expression can be a marker for activated myofibroblasts in the cancer stroma or in scar tissue.
Clinical features of hereditary mixed polyposis syndrome caused by GREM1 gene duplication include extracolonic tumors, onset of polyps in adolescence, and rapid progression of some polyps to advanced adenomas.
In human Idiopathic Pulmonary Fibrosis patient samples the study established a strong negative correlation in the mRNA expression levels of gremlin-1 and CXCL10. The results suggest that in addition to regulation of epithelial-mesenchymal crosstalk during tissue injury, gremlin-1 modulates inflammatory cell recruitment and anti-fibrotic chemokine production in the lung.
Gremlin1 protein expression in colorectal cancer associates with low tumour stage and extended survival independently of tumour stage, suggesting that it represents a relevant prognostic indicator in colorectal cancer
The results suggest that inhibition of BMP-2 by Gremlin-1 occurs by a mechanism that is distinct from other known inhibitors such as Noggin and Chordin and study propose a novel model of BMP-2-Gremlin-1 interaction yet not seen among any BMP antagonists, and cannot rule out that several different oligomeric states could be found, depending on the concentration of the two proteins.
both the regenerating and contralateral, developing limb of grem1 transgenics developed skeletal defects, suggesting that overexpressing grem1 negatively affects limb patterning
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. In mouse, this protein has been shown to relay the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
gremlin 1 homolog a, cysteine knot superfamily
, gremlin 1 homolog, cysteine knot superfamily
, gremlin 1, cysteine knot superfamily, homolog (Xenopus laevis)
, gremlin 1
, cysteine knot superfamily 1
, cysteine knot superfamily 1, BMP antagonist 1
, down-regulated in Mos-transformed cells protein
, down-regulated in v-mos-transformed cells
, gremlin 1, cysteine knot superfamily, homolog
, Cysteine knot superfamily 1, BMP antagonist 1
, DAN domain family member 2
, cell proliferation-inducing gene 2 protein
, gremlin 1-like protein
, increased in high glucose-2