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The secreted polypeptide, encoded by NOG, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). Additionally we are shipping Noggin Antibodies (149) and Noggin Kits (18) and many more products for this protein.
Showing 10 out of 66 products:
Mouse (Murine) NOG Protein expressed in Human Cells - ABIN2008158
Brunet, McMahon, McMahon, Harland: Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton. in Science (New York, N.Y.) 1998
Show all 6 references for ABIN2008158
Mouse (Murine) NOG Protein expressed in Escherichia coli (E. coli) - ABIN2666487
Bonaguidi, Peng, McGuire, Falciglia, Gobeske, Czeisler, Kessler: Noggin expands neural stem cells in the adult hippocampus. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2008
Show all 6 references for ABIN2666487
Human NOG Protein expressed in HEK-293 - ABIN2666472
Chiba, Lee, Zhou, Freed: Noggin enhances dopamine neuron production from human embryonic stem cells and improves behavioral outcome after transplantation into Parkinsonian rats. in Stem cells (Dayton, Ohio) 2008
Show all 6 references for ABIN2666472
Human NOG Protein expressed in Human Cells - ABIN2002466
Groppe, Greenwald, Wiater, Rodriguez-Leon, Economides, Kwiatkowski, Affolter, Vale, Izpisua Belmonte, Choe: Structural basis of BMP signalling inhibition by the cystine knot protein Noggin. in Nature 2002
Show all 5 references for ABIN2002466
Human NOG Protein expressed in Escherichia coli (E. coli) - ABIN1080387
Guan, Du, Lv, Qu, Fu, Yuan et al.: Oxygen-glucose deprivation preconditioning protects neurons against oxygen-glucose deprivation/reperfusion induced injury via bone morphogenetic protein-7 mediated ERK, p38 and Smad signalling ... in Clinical and experimental pharmacology & physiology 2016
Human NOG Protein expressed in Escherichia coli (E. coli) - ABIN413676
Umezu, Yamanouchi, Iida, Miura, Tomooka: Follistatin-like-1, a diffusible mesenchymal factor determines the fate of epithelium. in Proceedings of the National Academy of Sciences of the United States of America 2010
A New Subtype of Multiple Synostoses Syndrome Is Caused by a Mutation in GDF6 That Decreases Its Sensitivity to Noggin and Enhances Its Potency as a BMP Signal.
An imbalance between BMP-2 (show BMP2 Proteins) and Noggin secretion induces abnormal osteogenic differentiation of ankylosing spondylitis-mesenchymal stem cells.
early noggin exposure may play a specific role in the directed differentiation of DA cells from human embryonic stem cells.
Novel p.W150C NOG mutation associated with proximal symphalangism and conductive hearing impairment was identified in a Chinese family.Impaired dimerization of mutant NOG is an important pathogenic mechanism for the NOG-related disorder.
No association between SPRY2 (show SPRY2 Proteins), single-nucleotide polymorphisms, and nonsyndromic cleft lip with or without cleft palate risk were observed in this cohort of patients.
The study did not provide support for NOG being the causal gene at 17q22 in nonsyndromic cleft lip with or without cleft palate.
a novel NOG mutation in a Chinese family with proximal symphalangism
this study proposes that the decreased binding affinity of NOG with the p.R136C mutation to HSPG leads to an excess of bone morphogenetic protein signaling and underlies the proximal symphalangism and conductive hearing loss phenotype of carriers.
High-quality studies show that otosclerosis in Japanese patients is not linked to the NOG gene. [Review]
Even though gremlin 1 (show GREM1 Proteins) and noggin were not widely expressed in adult tissues, in a subset of organs their expression pattern indicated a potential role in normal tissue homeostasis as well as in malignancies.
we observed a glial reaction and an activity-dependent modification of Shh (show SHH Proteins), Noggin, and Numb (show NUMB Proteins) proteins. we found that Shh (show SHH Proteins) and Noggin could affect motor performance and that these proteins could be associated with both TDP-43 (show TARDBP Proteins) and Numb (show NUMB Proteins)
Molecular analysis demonstrated that ectopic Noggin-expressing regions in the early heart's pacemaker region, failed to express the potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (show HCN4 Proteins)
endogenous Bmp2 (show BMP2 Proteins), Bmp4 (show BMP4 Proteins), and Noggin transcript levels in postnatal bone and cartilage mirrored the activity of their respective reporters in these tissues
A band of noggin-expressing cells insulates a region of proliferative chondrocytes from the influence of BMP signaling, allowing them to differentiate as articular cartilage upon exposure to Wnt (show WNT2 Proteins) signaling emanating from the interzone.
Taken together, these results show that hair follicle development in Trps1 KO embryos is impaired directly or indirectly by decreased Noggin expression.
BMP signaling was stimulated in adipose derived stem cells (ASCs) by downregulating noggin.
The axial midline domain of Nog expression is critical to promote pharyngeal arch 1 development in early stages, necessary for adequate outgrowth of the mandibular bud.
Follistatin (show FST Proteins) aids in maintaining proper somite size, and consequently sclerotome progenitor numbers, by preventing paraxial mesoderm from adopting an intermediate/lateral plate mesodermal fate in the Noggin-deficient state.
Noggin antagonizes BMP, which is required in presumptive notochord cells for mammalian foregut morphogenesis
Noggin is expressed constantly in Meckel's cartilage (MC) and in the absence of Noggin, MC is significantly thickened attributing to dramatically elevated cell proliferation rate associated with enhanced phosphorylation of Smad1 (show SMAD1 Proteins)/5/8.
Noggin did not affect oocyte nuclear maturation. Noggin supplementation up-regulated the expression of HSP70 and MATER genes in matured oocytes.
Noggin, a cytokine inhibiting the BMP4 pathway, successfully upregulated the relative expression of NANOG mRNA in the ICM explants with respect to controls.
a new role for Noggin1 in determining specific anterior neural structures by the modulation of TGFbeta (show TGFB1 Proteins) and SHH (show SHH Proteins) signaling.
This allow one to compare the expression levels of Noggin1 and Noggin 2 constructs, to purify them on the affine immunosorbent and to show the activity of Noggin proteins by analyzing their ability to bind BMP4 (show BMP4 Proteins) factor
Both Noggin proteins could induce a secondary head, including the forebrain. During normal development, Noggin1 mRNA was translated with low efficiency, providing sufficient Noggin1 only for antagonizing Bone morphogenetic protein.
A 2066 bp noggin 5' flanking sequence which recapitulates the roof-plate expression of endogenous gene in transgenic frog tadpoles has been identified; this roof-plate enhancer has been mapped to a sequence as short as 79 bp.
Noggin specifically blocks chondrogenic differentiation, rather than osteogenic differentiation, in mesodermal stem cell line C1 and skeletal cells.
Chordin (show CHRD Proteins), Noggin, beta-Catenin (show CTNNB1 Proteins), and Cerberus (show CER1 Proteins) have roles in neural induction in Xenopus
X-epilectin expression is down-regulated by Noggin and tBR and that this effect is inhibited by BMP4 over-expression, suggesting X-epilectin expression is mediated by the BMP signalling pathway
maternal mRNA encoding noggin is enriched in animal tiers and at low concentrations in the C-tier, suggesting that the neural fates of C-tier blastomeres may be responsive to early signaling from their neighboring cells
The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified\; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as this gene. All of these mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of this human gene is highly homologous to that of Xenopus, rat and mouse.
, noggin protein
, symphalangism 1 (proximal)
, noggin 1