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CDH16 (cadherin 16, KSP-cadherin) Blocking Peptide (100ug)

CDH16 (cadherin 16, KSP-cadherin) Blocking Peptide (100ug)


Supplier: Aviva Systems Biology Incorporated
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This is a synthetic peptide designed for use in combination with anti-CDH16 antibody (Catalogue #: ARP41541_P050) made by Aviva Systems Biology. It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications. Please inquire for more details.
Presku: AAP41541
Size: 100 ug
Weight: 88kDa
Gene: 1014
Format: Lyophilized powder
Target: CDH16 is a member of the cadherin superfamily, which are calcium-dependent, membrane-associated glycoproteins. CDH16 consists of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain but lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins. Expression is exclusively in kidney, where the protein functions as the principal mediator of homotypic cellular recognition, playing a role in the morphogenic direction of tissue development.This gene is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Mapped to a previously identified cluster of cadherin genes on chromosome 16q22.1, the gene localizes with superfamily members CDH1, CDH3, CDH5, CDH8 and CDH11. The protein consists of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain but lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins. Expression is exclusively in kidney, where the protein functions as the principal mediator of homotypic cellular recognition, playing a role in the morphogenic direction of tissue development. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.