Collagen V α1 (Cleaved-Ala1605) rabbit pAb

• 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.

• Description :

  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.

• UniProt :

  P20908

• Swiss Prot :

  P20908

• Reactivity :

  Human; Rat; Mouse

• Immunogen :

  Synthesized peptide derived from human Collagen V α1 (Cleaved-Ala1605)

• Clonality :

  Polyclonal

• Source :

  Rabbit

• Applications :

  WB; ELISA

• Concentration :

  1 mg/ml

• Dilution :

  WB 1:1000-2000 ELISA 1:5000-20000

• Molecular Weight :

  175 202kD

• Storage Conditions :

  -20°C/1 year

• Observed Molecular Weight :

  175 202kD

• Fragment :

  IgG

• Subcellular Location :

  Secreted, extracellular space, extracellular matrix .

• Other Product Names :

  Collagen alpha-1 (V) chain

• Gene ID (Human) :

  1289