epitope corresponding to amino acids 651-722 mapping within a C-terminal cytoplasmic domain of VE-cadherin of human origin
Conjugation
Agarose
Modification
Acetylated
Modification Notes
The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy-terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including ∫-catenin, to regulate cadherin function. VE-cadherin (for vascular endothelial cadherin, also designated cadherin-5) is localized at intercellular junctions of endothelial cells, where it is thought to play a role in the cohesion and organization of intercellular junctions.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
ELISAIFIPWB
recommended for detection of VE-cadherin of mouse, rat and human origin by WB, IP, IF and ELISA: WB:1:100~1:500 IP:1:20~1:100 IF:1:20~1:100
Species Reactivity
HumanMouseRat
Predicted Reactivity
equine, bovine and porcine
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 651-722 mapping within a C-terminal cytoplasmic domain of VE-cadherin of human origin
Molecular Weight(MW)
88 kDa
Tissue Specificity
epitope corresponding to amino acids 651-722 mapping within a C-terminal cytoplasmic domain of VE-cadherin of human origin