|Application ||WB, E|
|Calculated MW||102063 Da|
|Antigen Region||253-282 aa|
|Other Names||Protocadherin alpha-2, PCDH-alpha-2, PCDHA2|
|Target/Specificity||This PCDHA2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 253-282 amino acids from the N-terminal region of human PCDHA2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PCDHA2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined.
Wu, C., et al. Proteomics 7(11):1775-1785(2007)
Wu, Q., et al. Genome Res. 11(3):389-404(2001)
Nollet, F., et al. J. Mol. Biol. 299(3):551-572(2000)
Yagi, T., et al. Genes Dev. 14(10):1169-1180(2000)
Wu, Q., et al. Proc. Natl. Acad. Sci. U.S.A. 97(7):3124-3129(2000)
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