Reactive species
Human;Rat;Mouse;
Antibody type
Polyclonal Antibody
Protein name
Collagen V α1 (Cleaved-Ala1605)
Immunogen
Synthesized peptide derived from human Collagen V α1 (Cleaved-Ala1605)
Specificity
This antibody detects endogenous levels of Human Collagen V α1 (Cleaved-Ala1605, protein was cleaved amino acid sequence between 1605-1606 )
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB 1:1000-2000 ELISA 1:5000-20000
Purification process
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
Other name
Collagen alpha-1(V) chain
Background
disease:Defects in COL5A1 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 COL5A1 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.,function:Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.,PTM:Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.,PTM:Sulfated on 40% of tyrosines.,similarity:Belongs to the fibrillar collagen family.,similarity:Contains 1 laminin G-like domain.,similarity:Contains 1 TSP N-terminal (TSPN) domain.,subunit:Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta. Interacts with CSPG4.,
Function
blood vessel development, eye development, vasculature development, heart morphogenesis, cell motion, plasma membrane organization, cell adhesion, ectoderm development, sensory organ development, heart development,epidermis development, response to wounding, membrane organization, cell migration, biological adhesion,extracellular matrix organization, collagen fibril organization, collagen metabolic process, collagen biosynthetic process, wound healing, spreading of epidermal cells, wound healing, extracellular structure organization, fibril organization, skin development, multicellular organismal metabolic process, multicellular organismal macromolecule metabolic process, integrin biosynthetic process, eye morphogenesis, cell motility, localization of cell,
