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EMILIN1 encodes an extracellular matrix glycoprotein that is characterized by an N-terminal microfibril interface domain, a coiled-coiled alpha-helical domain, a collagenous domain and a C-terminal globular C1q domain. 再加上，我们可以发Emilin1 抗体 (52) 和 Emilin1 试剂盒 (44)和数多这个蛋白质的别的产品。
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Expression of certain emilin genes in peculiar areas, such as the central nervous system or the posterior notochord, suggests that they may play a role in key morphogenetic processes:[Emilin]
Data suggested mechanisms for homo- and hetero-typic EMILINs multimers formation: EMILIN1 or EMILIN2 alone can form trimers and multimers in the absence of each other or they can co-polymerize in a head-to-tail fashion to form hetero-typic multimers.
Emilin1 deficiency results in aortic valve disease, mediated by non-canonical (MAPK/phosphorylated Erk1 and Erk2) TGF-beta dysregulation.
EMILIN1/integrin alpha 9 beta 1 interaction contributes to lymphatic valve formation, maintenance, and function.
these data established that EMILIN1 exerts a protective role in tumor growth, in tumor lymphatic vessel formation, as well as in metastatic spread to lymph nodes
Emilin-1 produced by vascular smooth muscle cells acts as a main regulator of resting blood pressure levels by controlling the myogenic response in resistance arteries through TGF-beta.
Pull-down assays indicated that the binding to organ of Corti CNGA3 was attributable to the EMILIN1 intracellular sequence that follows a predicted transmembrane domain in the C-terminus
EMILIN1 is identified as a novel ligand for keratinocyte alpha9beta1 integrin, suggesting prospective roles for this receptor-ligand pair in skin homeostasis.
may regulate elastogenesis and vascular cell maintenance by stabilizing molecular interactions between elastic fiber components and by endowing elastic fibers with specific cell adhesion properties
transcription in different tissues is achieved through combinatorial cooperation between various regions
EMILIN1 is a novel local regulator of lymphangiogenesis
Study discloses a novel mechanism of interaction occurring between the trimeric gC1q domain of EMILIN1 and the alpha4beta1 integrin and determines that the three E933 residues (one from each monomer) are all required for ligand binding. Furthermore, R904 was identified as a synergistic residue for cell adhesion.
This study is the first to identify EMILIN-1 and ILK as prospective markers of islet regenerative function in human mesenchymal stem cells.
These findings collectively suggest that EMILIN1 may represent a new disease gene associated with an autosomal-dominant connective tissue disorder.
The present findings highlight the peculiar activity of PMN elastase in disabling EMILIN1 suppressor function.
All three SNPs in introns 1 and 5 (rs2289360, rs2011616 and rs7424556) of EMILIN1 were in strong pair-wise linkage disequilibrium and were significantly associated with hypertension.
There were significant associations of rs2011616 and rs2304682 polymorphisms in the EMILIN1 gene with hypertension among Japanese.
EMILIN-1 may regulate the formation of oxytalan fibers and play a role in their homeostasis.
rs2289360, rs2011616, and rs2304682 in the human EMILIN1 gene, as well as the haplotype constructed using rs2536512, rs2011616, and rs17881426, are useful genetic markers of essential hypertension in Japanese men.
beta1 Integrin-dependent cell adhesion to this protein is mediated by its gC1q domain
NMR assignments for the C-terminal globular domain of EMILIN-1
EMILIN1 interacts with anthrax protective antigen and inhibits toxin action in vitro. EMILIN1 may be a potential target and/or a protein useful for countermeasures against B. anthracis toxin lethality.
EMILIN1 gC1q-alpha4beta1 represents a unique ligand/receptor system, with a requirement for a 3-fold arrangement of the interaction site.
Our findings don't support positive association of Emilin1 gene with EH, but the interaction of age and genotype variation of rs3754734 and rs2011616 might increase the risk to hypertension
This gene encodes an extracellular matrix glycoprotein that is characterized by an N-terminal microfibril interface domain, a coiled-coiled alpha-helical domain, a collagenous domain and a C-terminal globular C1q domain. The encoded protein associates with elastic fibers at the interface between elastin and microfibrils and may play a role in the development of elastic tissues including large blood vessels, dermis, heart and lung.
, elastin microfibril interfacer 1
, elastin microfibril interface located protein 1
, elastin microfibril interface-located protein 1
, elastin microfibril interface located protein