|Other Names||Cadherin-8, CDH8|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1402a was selected from the N-term region of human CDH8. 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.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Mainly expressed in brain. Found in certain nerve cell lines, such as retinoblasts, glioma cells and neuroblasts|
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Provided below are standard protocols that you may find useful for product applications.
CDH8 is a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the protein's homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. This particular cadherin is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.
Blaschke,S., Int. J. Cancer 101 (4), 327-334 (2002)Shimoyama,Y., Biochem. J. 349 (PT 1), 159-167 (2000)
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