VE-Cadherin (a.a.770-781) Blocking Peptide
€155.00
In stock
SKU
ECM-CX2235
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.
Sequence: VE-Cadherin synthetic peptide corresponds to amino acids 770 to 781 in human VE-cadherin. This sequence has significant homology to the conserved site in rat and mouse, and has less than 50% homology with other cadherins.
Specificity: This peptide is specifically recognized by VE-cadherin (a.a. 770-781) antibody (CP2231) in ELISA, and has been shown to block the reactivity of CP2231 in Western blot and is recommended for blocking in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: VE-Cadherin synthetic peptide corresponds to amino acids 770 to 781 in human VE-cadherin. This sequence has significant homology to the conserved site in rat and mouse, and has less than 50% homology with other cadherins.
Specificity: This peptide is specifically recognized by VE-cadherin (a.a. 770-781) antibody (CP2231) in ELISA, and has been shown to block the reactivity of CP2231 in Western blot and is recommended for blocking in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
| Is Featured? | No |
|---|
Write Your Own Review