protein

VE-Cadherin (a.a.770-781) Peptide

MBS474068

0.05 mg

130 USD

Peptide

VE-Cadherin (a.a.770-781) Peptide

VE-Cadherin (a.a. 770-781)

VE-Cadherin (a.a. 770-781)

VE-cadherin; Cadherin-5; cadherin-5; 7B4 antigen; VE-cadherin; cd144 antigen; OTTHUMP00000174777; endothelial-specific cadherin; vascular endothelial cadherin; cadherin 5, type 2, VE-cadherin (vascular epithelium); cadherin 5, type 2 (vascular endothelium); 7B4 antigen; Vascular endothelial cadherin

CDH5; CDH5; 7B4; CD144; FLJ17376

CADH5_HUMAN

Peptide 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.

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.

Blocking Peptide is supplied in 50ul phosphate-buffered saline and 0.05% sodium azide.

Store at -20 degree C. Stable for 1 year.

Blocking: 1:1,000. ELISA: 50 ng/well

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 VEcadherin comprises the juxtamembrane domain that binds to the p120 catenin, and the carboxylterminal domain that interacts with beta or gamma 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.

Potter M.D. et al. (2005) J Biol. Chem. 280(36):31906. Baumeister U. et al. (2005) EMBOJ 24:1686. Wallez Y. et al. (2007) Oncogene 26:1067

599834

P33151

87,528 Da

Adherens Junctions Interactions Pathway 119533!!Cell Adhesion Molecules (CAMs) Pathway 83069!!Cell Adhesion Molecules (CAMs) Pathway 480!!Cell Junction Organization Pathway 160966!!Cell-cell Junction Organization Pathway 119532!!Leukocyte Transendothelial Migration Pathway 83083!!Leukocyte Transendothelial Migration Pathway 494!!S1P2 Pathway 138059!!Signaling Events Mediated By VEGFR1 And VEGFR2 Pathway 137940

This gene is a classical cadherin from the cadherin superfamily and is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. An alternative splice variant has been described but its full length sequence has not been determined. [provided by RefSeq]

Function: Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. Ref.9. Subunit structure: Interacts via cadherin 5 domain with PTPRB. By similarity. Interacts with TRPC4. Interacts with KRIT1. Ref.8 Ref.9. Subcellular location: Cell junction. Cell membrane; Single-pass type I membrane protein. Probable. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Ref.9. Tissue specificity: Endothelial tissues and brain. Post-translational modification: Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB. By similarity. Ref.7. Sequence similarities: Contains 5 cadherin domains.

0.05 mg

130 USD