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ADAMTS1 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Additionally we are shipping ADAMTS1 Antibodies (130) and ADAMTS1 Kits (29) and many more products for this protein.
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The developmental arrest of early secondary follicles following furin (show FURIN Proteins) disruption might be rooted in the loss of the mature form of ADAMTS1 and compromised proliferation of granulosa cells in mutant mice.
Energy expenditure and thermogenesis were not significantly different between KO and WT ADAMTS5 (show ADAMTS5 Proteins)-J mice (in contrast to somewhat enhanced levels in ADAMTS5 (show ADAMTS5 Proteins)-P mice). Insulin (show INS Proteins) sensitivity was improved in the ADAMTS5 (show ADAMTS5 Proteins)-J KO mice, and they were protected against non-alcoholic steatohepatitis in the DIO model
Data show that NOTCH1 (show NOTCH1 Proteins) is a target of ADAMTS1 metalloproteinase activity, which reduces Notch (show NOTCH1 Proteins) signaling, leading to increased satellite cell activation.
Reduced tumors in ADAMTS1 knockout mice displayed a paradoxical increase in vascular density and vascular-related genes; a detailed characterization revealed an impaired vasculature, along with a minor infiltration of macrophages. melanoma xenografts showed a relevant induction of its expression in stroma compartments.
Adamts1 acts as an extracellular matrix 'modifier', with miR (show MLXIP Proteins)-181d-induced downregulation, that regulates adipocyte lineage commitment and obesity.
Adamts5 (show ADAMTS5 Proteins)(-/-) mice were protected from hepatic mitochondrial dysfunction, as indicated by increased mitochondrial respiratory chain complex activity, higher ATP levels and higher expression of antioxidant enzymes. Absence of ADAMTS5 (show ADAMTS5 Proteins) preserves liver integrity in a diet-induced obesity model.
Genetic haploinsufficiency of Adamts1 in mice caus (show NOS2 Proteins)es thoracic aortic aneurysms and dissections similar to Marfan syndrome.
An ADAMTS1 blocking antibody suppressed the SPARC (show SPARC Proteins)-induced collagen I secretion, indicating that SPARC (show SPARC Proteins) promoted collagen production directly through ADAMTS1 interaction. In conclusion, ADAMTS1 is an important mediator of SPARC (show SPARC Proteins)-regulated cardiac aging.
research emphasises the importance of ADAMTS5 (show ADAMTS5 Proteins) expression in the control of influenza virus infection and highlights the potential for development of ADAMTS5 (show ADAMTS5 Proteins)-based therapeutic strategies to reduce morbidity and mortality
increased expression of ADAMTS1 protein in macrophages and neutrophils that infiltrated aortic tissues may promote the progression of acute aortic dissection
Our study demonstrated that altered levels of ADAMTS-1 and aggrecan (show ACAN Proteins) may have a partial role in the etiopathogenesis of Polycystic ovary syndrome (PCOS), and ADAMTS-1 could be a predictive marker for implantation success in PCOS patients.
This study showed that ADAMTS1, 8, and 18 are highly expressed in GC and its nodal metastases, suggesting important roles of these proteases in carcinogenesis and lymphatic metastasis. The findings from the present study indicate that these proteases may be promising candidates for novel and alternative treatments in GC (gastric cancer)
Taken together, our findings suggested that miR (show MLXIP Proteins)-362-3p inhibits the proliferation and migration of VSMCs by directly targeting ADAMTS1, which might provide novel insight into the molecular mechanisms underlying the action of miR (show MLXIP Proteins)-362-3p in atherosclerosis.
ADAMTS1 has diverse roles in angiogenesis, tumor microenvironment and lymphangiogenesis.
Patients with Marfan syndrome showed elevated NOS2 (show NANOS2 Proteins) and decreased ADAMTS1 protein levels in the aorta.
Data indicate that serum versican (show Vcan Proteins) levels were significantly decreased in polycystic ovary syndrome (PCOS) patients, and that serum ADAMTS-1 (a disintegrin and metalloproteinase with thrombospondin motif-1) and versican (show Vcan Proteins) levels were significantly and positively correlated with each other.
Findings indicate that ADAMTS-1 has proteolytic functions in the nucleus through its interaction with aggrecan (show ACAN Proteins) substrate in normal and tumoral breast cells.
All ADAMTS (show ADAMTS13 Proteins) tested in our study were expressed in both stable and unstable carotid plaques, especially in smooth muscle cells and macrophages. Analysis of the expression pattern on mRNA level showed significant higher expression of ADAMTS1 in unstable plaques compared with stable plaques.
ADAMTS1 protein levels in semen were significantly lower in males with infertility. Sperm count and motility showed a negative correlation with levels of ADAMTS1 protein expression.
Expression and induction of ADAMTS-1 through receptor-mediated action of progesterone in cumulus cells is one of essential requirements for gonadotropin-regulated cumulus expansion of porcine cumulus-oocyte complexes.
study indicates that disintegrin and metalloproteinase with thrombospondin motifs 1(ADAMTS1) participates in bovine endometrial remodeling
Data indicate that ADAMTS1 promoter activity and mRNA expression were increased by forskolin and human chorionic gonadotropin.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene contains two disintegrin loops and three C-terminal TS motifs and has anti-angiogenic activity. The expression of this gene may be associated with various inflammatory processes as well as development of cancer cachexia. This gene is likely to be necessary for normal growth, fertility, and organ morphology and function.
metalloproteinase with thrombospondin-like motifs-1
, ADAM metallopeptidase with thrombospondin type 1 motif, 1
, A disintegrin and metalloproteinase with thrombospondin motifs 1
, ADAM-TS 1
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 1
, A disintegrin and metalloproteinase with thrombospondin motifs 5
, ADAM-TS 5
, human metalloproteinase with thrombospondin type 1 motifs
, a disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAMTS-1)
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1
, a disintegrin-like and metallopeptidse (reprolysin type) with thrombospondin type 1 motif, 1