|Other Names||Cadherin-4, Retinal cadherin, R-CAD, R-cadherin, CDH4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1401a was selected from the N-term region of human CDH4. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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. May play an important role in retinal development.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed mainly in brain but also found in other tissues|
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Provided below are standard protocols that you may find useful for product applications.
CDH4 is a classical cadherin from the cadherin superfamily. It is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Based on studies in chicken and mouse, this cadherin is thought to play an important role during brain segmentation and neuronal outgrowth. In addition, a role in kidney and muscle development is indicated. Of particular interest are studies showing stable cis-heterodimers of cadherins 2 and 4 in cotransfected cell lines. Previously thought to interact in an exclusively homophilic manner, this is the first evidence of cadherin heterodimerization.
Miotto,E., Cancer Res. 64 (22), 8156-8159 (2004)Johnson,E., J. Biol. Chem. 279 (30), 31041-31049 (2004)Kitagawa,M., Biochem. Biophys. Res. Commun. 271 (2), 358-363 (2000)
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