组成
PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
背景
This gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and autosomal dominant cutis laxa. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008],
功能
Alternative products:Additional isoforms seem to exist,Disease:Defects in ELN are a cause of autosomal dominant cutis laxa [MIM:123700]. Cutis laxa is a rare connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. The skin changes are often accompanied by extracutaneous manifestations, including pulmonary emphysema, bladder diverticula, pulmonary artery stenosis and pyloric stenosis.,Disease:Defects in ELN are the cause of supravalvular aortic stenosis (SVAS) [MIM:185500]. SVAS is a congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome.,Disease:Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS) [MIM:194050]. WBS is a rare developmental disorder and a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23.,Function:Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle.,online information:Elastin entry,PTM:Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.,PTM:Hydroxylation on proline residues within the sequence motif, GXPG, is most likely 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.,similarity:Belongs to the elastin family.,subcellular location:Extracellular matrix of elastic fibers.,subunit:The polymeric elastin chains are cross-linked together into an extensible 3D network. Forms a ternary complex with BGN and MFAP2. Interacts with MFAP2 via divalent cations (calcium > magnesium > manganese) in a dose-dependent and saturating manner.,tissue specificity:Expressed within the outer myometrial smooth muscle and throughout the arteriolar tree of uterus (at protein level). Also expressed in the large arteries, lung and skin.,
