蛋白名称
Collagen V α2 (Cleaved-Leu1229)
免疫原
Synthesized peptide derived from human Collagen V α2 (Cleaved-Leu1229)
特异性
This antibody detects endogenous levels of Human Collagen V α2 (Cleaved-Leu1229, protein was cleaved amino acid sequence between 1229-1230 )
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
来源
Polyclonal, Rabbit,IgG
稀释比例
WB 1:1000-2000 ELISA 1:5000-20000
纯化工艺
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
其他名称
Collagen alpha-2(V) chain
背景
This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II. [provided by RefSeq, Jul 2008],
功能
disease:Defects in COL5A2 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis or severe classic type Ehlers-Danlos syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.,disease:Defects in COL5A2 are a cause of Ehlers-Danlos syndrome type 2 (EDS2) [MIM:130010]; also known as Ehlers-Danlos syndrome mitis or mild classic type Ehlers Danlos syndrome.,disease:Genetic variation in COL5A2 is associated with spontaneous cervical artery dissections (sCAD). sCAD are an important cause of stroke among young and middle-aged patients. Ultrastructural abnormalities are observed in skin biopsies of most patients with sCAD. Major findings included enlarged and irregular collagen fibrils
