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VE-Cadherin (C-terminal) Antibody

Applications

  • WB

Reactivity

  • Human
  • Mouse
  • Rat
Overview
Catalog # bs-70370r-100ul
Product Name VE-Cadherin (C-terminal) Antibody
Applications WB
Specificity The antibody detects a 140 kDa* band corresponding to VE-cadherin in western blots of human endothelial cells, and this reactivity can be specifically blocked using VE-cadherin peptide (CX2235). This sequence has significant homology to the conserved site in rat and mouse, and has less than 50% homology with other cadherins.
Reactivity Human, Mouse, Rat
Specifications
Conjugation Unconjugated
Host Rabbit
Source VE-Cadherin synthetic peptide (coupled to carrier protein) corresponds to amino acids from the C-terminal region of human VE-cadherin.
Clonality Polyclonal
Isotype IgG
Purification Antigen Affinity purification
Storage Buffer PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage Condition Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Target
Swiss Prot P33151
Synonyms Cadherin-5, vascular endothelial Cadherin, CD144
Background Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. VE-cadherin (Cadherin 5) is the major cadherin found in endothelial cells and has important roles during angiogenesis and maintenance of barrier permeability. The cytoplasmic domain of VE-cadherin comprises the juxtamembrane domain that binds to the p120 catenin, and the carboxylterminal domain that interacts with β- or γ-catenins. Modulation of tyrosine phosphorylation on one or more of the nine tyrosine sites in the cytoplasmic domain may be important for regulating both angiogenesis and permeability. Phosphorylation of Tyr-658 and Tyr-731 alters catenin binding, restores cell migration, and decreases barrier permeability. While VEGF-induced phosphorylation of Tyr-685 occurs through c-Src, and regulates endothelial cell migration, but not permeability
Application Dilution
WB 1:300-5000