N-Cadherin (a.a. 811-824) Blocking Peptide
€155.00
In stock
SKU
ECM-CX1755
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. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.
Sequence: Unphosphorylated N-cadherin (a.a. 811-824) synthetic peptide generated from human N-cadherin. This sequence is conserved in rat and mouse N-cadherin, and has three amino acid differences from the conserved region in R-cadherin.
Specificity: The peptide is specifically recognized by anti-N-Cadherin (a.a. 811-824) antibody (CP1751) in ELISA, and has been shown to block the reactivity of CP1751 during Western blot. In addition, the peptide is recommended for use in blocking CP1751 reactivity 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. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.
Sequence: Unphosphorylated N-cadherin (a.a. 811-824) synthetic peptide generated from human N-cadherin. This sequence is conserved in rat and mouse N-cadherin, and has three amino acid differences from the conserved region in R-cadherin.
Specificity: The peptide is specifically recognized by anti-N-Cadherin (a.a. 811-824) antibody (CP1751) in ELISA, and has been shown to block the reactivity of CP1751 during Western blot. In addition, the peptide is recommended for use in blocking CP1751 reactivity 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.
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