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Mouse Anti-DCX Recombinant Antibody (2G5) (CBMAB-1518-CN)

This product is a mouse antibody that recognizes DCX of human. The antibody 2G5 can be used for immunoassay techniques such as: IHC-P, ICC, IF, WB, FC, ELISA.
See all DCX antibodies
Published Data
Fig.1 Example of DCX triple-stainings carried out in attempt to confirm nuclear localization and neuronal origin of Ki67 signal.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
2G5
Antibody Isotype
IgG1
Application
IHC-P, ICC, IF, WB, FC, ELISA

Basic Information

Immunogen
Purified recombinant fragment of human DCX (aa. 362-411) expressed in E. coli
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.05% protein stabilizer
Preservative
0.05% Sodium azide
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Neuronal migration protein doublecortin
Introduction
Doublecortin is a cytoplasmic protein and contains two doublecortin domains, which bind microtubules. Doublecortin appears to direct neuronal migration by regulating the organization and stability of microtubules. Also, Doublecortin interacts with LIS1, which is important to proper microtubule function in the developing cortex. Mutations in doublecortin cause abnormal migration of neurons during development and disrupt the layering of the cortex, leading to epilepsy, cognitive disability, subcortical band heterotopia ("double cortex" syndrome) in females and lissencephaly ("smooth brain" syndrome) in males.
Entrez Gene ID
1641
UniProt ID
O43602
Alternative Names
DC; DBCN; LISX; SCLH; XLIS
Function
Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.
Biological Process
Axoneme assembly Source: GO_Central
Central nervous system development Source: ProtInc
Intracellular signal transduction Source: InterPro
Nervous system development Source: ProtInc
Neuron migration Source: UniProtKB
Photoreceptor cell development Source: GO_Central
Retina development in camera-type eye Source: GO_Central
Cellular Location
Cytoplasm; Neuron projection. Localizes at neurite tips.
Involvement in disease
Lissencephaly, X-linked 1 (LISX1):
A classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.
Subcortical band heterotopia X-linked (SBHX):
SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.
PTM
Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (By similarity).
Ubiquitinated by MDM2, leading to its degradation by the proteasome. Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells.

Bott, C. J., McMahon, L. P., Keil, J. M., Yap, C. C., Kwan, K. Y., & Winckler, B. (2020). Nestin selectively facilitates the phosphorylation of the Lissencephaly-linked protein doublecortin (DCX) by cdk5/p35 to regulate growth cone morphology and Sema3a sensitivity in developing neurons. Journal of Neuroscience, 40(19), 3720-3740.

Manka, S. W., & Moores, C. A. (2020). Pseudo‐repeats in doublecortin make distinct mechanistic contributions to microtubule regulation. EMBO reports, 21(12), e51534.

Leung, J. M., Nagayasu, E., Hwang, Y. C., Liu, J., Pierce, P. G., Phan, I. Q., ... & Hu, K. (2020). A doublecortin-domain protein of Toxoplasma and its orthologues bind to and modify the structure and organization of tubulin polymers. BMC molecular and cell biology, 21(1), 1-25.

Ayanlaja, A. A., Ji, G., Wang, J., Gao, Y., Cheng, B., Kanwore, K., ... & Gao, D. (2020). Doublecortin undergo nucleocytoplasmic transport via the RanGTPase signaling to promote glioma progression. Cell Communication and Signaling, 18(1), 1-17.

Unger, M. S., Marschallinger, J., Kaindl, J., Klein, B., Johnson, M., Khundakar, A. A., ... & Aigner, L. (2018). Doublecortin expression in CD8+ T-cells and microglia at sites of amyloid-β plaques: A potential role in shaping plaque pathology?. Alzheimer's & Dementia, 14(8), 1022-1037.

Liu, J. Y., Matarin, M., Reeves, C., McEvoy, A. W., Miserocchi, A., Thompson, P., ... & Thom, M. (2018). Doublecortin-expressing cell types in temporal lobe epilepsy. Acta neuropathologica communications, 6(1), 1-13.

Moslehi, M., Ng, D. C., & Bogoyevitch, M. A. (2017). Dynamic microtubule association of Doublecortin X (DCX) is regulated by its C-terminus. Scientific reports, 7(1), 1-11.

Boulanger, J. J., & Messier, C. (2017). Doublecortin in oligodendrocyte precursor cells in the adult mouse brain. Frontiers in Neuroscience, 11, 143.

Ayanlaja, A. A., Xiong, Y., Gao, Y., Ji, G., Tang, C., Abdikani Abdullah, Z., & Gao, D. (2017). Distinct features of doublecortin as a marker of neuronal migration and its implications in cancer cell mobility. Frontiers in molecular neuroscience, 10, 199.

Nagayasu, E., Hwang, Y. C., Liu, J., Murray, J. M., & Hu, K. (2017). Loss of a doublecortin (DCX)-domain protein causes structural defects in a tubulin-based organelle of Toxoplasma gondii and impairs host-cell invasion. Molecular biology of the cell, 28(3), 411-428.

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For research use only. Not intended for any clinical use.

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