DCX Antibody (monoclonal) (M01)
Mouse monoclonal antibody raised against a full length recombinant DCX.
|Application ||WB, IF|
|Calculated MW||40574 Da|
|Other Names||Neuronal migration protein doublecortin, Doublin, Lissencephalin-X, Lis-X, DCX, DBCN, LISX|
|Target/Specificity||DCX (AAH27925, 1 a.a. ~ 360 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.|
|Format||Clear, colorless solution in phosphate buffered saline, pH 7.2 .|
|Storage||Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.|
|Precautions||DCX Antibody (monoclonal) (M01) is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the doublecortin family. The protein encoded by this gene is a cytoplasmic protein and contains two doublecortin domains, which bind microtubules. In the developing cortex, cortical neurons must migrate over long distances to reach the site of their final differentiation. The encoded protein appears to direct neuronal migration by regulating the organization and stability of microtubules. In addition, the encoded protein interacts with LIS1, the regulatory gamma subunit of platelet activating factor acetylhydrolase, and this interaction is important to proper microtubule function in the developing cortex. Mutations in this gene cause abnormal migration of neurons during development and disrupt the layering of the cortex, leading to epilepsy, mental retardation, subcortical band heterotopia (double cortex syndrome) in females and lissencephaly (smooth brain syndrome) in males. Multiple transcript variants encoding different isoforms have been found for this gene.
1.LC-MS/MS identification of doublecortin as abundant beta cell-selective protein discharged by damaged beta cells in vitro.Jiang L, Brackeva B, Stangel G, Verhaeghen K, Costa O, Couillard-Despres S, Rotheneichner P, Aigner L, Van Schravendijk C, Pipeleers D, Ling Z, Gorus F, Martens GA.J Proteomics. 2013 Jan 19. doi:pii: S1874-3919(13)00022-5. 10.1016/j.jprot.2012.12.031.
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