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Mouse Anti-DBN1 Recombinant Antibody (CBYCD-166) (CBMAB-D0300-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Drebrin 1 (DBN1). The antibody can be used for immunoassay techniques, such as WB, ICC.
See all DBN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYCD-166
Antibody Isotype
IgG1
Application
WB, ICC

Basic Information

Immunogen
E. coli-derived recombinant human Drebrin 1, Asn482-Asp649 (Ser553Pro), Accession # Q16643
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!]

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
drebrin 1
Introduction
DBN1 is a cytoplasmic actin-binding protein thought to play a role in the process of neuronal growth. It is a member of the drebrin family of proteins that are developmentally regulated in the brain. A decrease in the amount of this protein in the brain has been implicated as a possible contributing factor in the pathogenesis of memory disturbance in Alzheimer's disease.
Entrez Gene ID
UniProt ID
Alternative Names
Drebrin 1; Developmentally-Regulated Brain Protein; D0S117E; Drebrin E2; Drebrin E; Drebrin;
Function
Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400).

Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400).

Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity).

Involved in memory-related synaptic plasticity in the hippocampus (By similarity).
Biological Process
Actin filament organization Source: UniProtKB
C communication by chemical coupling Source: Ensembl
Cell communication by electrical coupling Source: Ensembl
Cytoplasmic sequestering of protein Source: UniProtKB
In utero embryonic development Source: Ensembl
Maintenance of protein location in cell Source: Ensembl
Neural precursor cell proliferation Source: Ensembl
Neuron projection morphogenesis Source: GO_Central
Positive regulation of axon extension Source: GO_Central
Positive regulation of dendritic spine morphogenesis Source: UniProtKB
Positive regulation of receptor localization to synapse Source: UniProtKB
Positive regulation of synaptic plasticity Source: UniProtKB
Postsynaptic actin cytoskeleton organization Source: GO_Central
Regulation of actin filament polymerization Source: GO_Central
Regulation of dendrite development Source: UniProtKB
Regulation of neuronal synaptic plasticity Source: UniProtKB
Cellular Location
Cytoplasm; Dendrite; Cell cortex; Cell junction; Growth cone. In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm (PubMed:20215400). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC) (PubMed:20215400). Colocalized with RUFY3 and F-actin at the transitional domain of the axonal growth cone (By similarity).
Involvement in disease
Alzheimer disease (AD):
The protein represented in this entry may be involved in disease pathogenesis. In brains of patients with AD, decreased expression and absence from dystrophic neurites in amyloid plaques. Disappearance of debrin from the hippocampus may contribute to the pathogenesis of memory disturbance in AD. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death.

Shan, Y., Farmer, S. M., & Wray, S. (2021). Drebrin regulates cytoskeleton dynamics in migrating neurons through interaction with CXCR4. Proceedings of the National Academy of Sciences, 118(3).

Guoren, Z., Zhaohui, F., Wei, Z., Mei, W., Yuan, W., Lin, S., ... & Bo, S. (2020). TFAP2A induced ITPKA serves as an oncogene and interacts with DBN1 in lung adenocarcinoma. International journal of biological sciences, 16(3), 504.

Hironaka, T., Ueno, T., Mae, K., Yoshimura, C., Morinaga, T., Horii, Y., ... & Nakaya, M. (2020). Drebrin is induced during myofibroblast differentiation and enhances the production of fibrosis-related genes. Biochemical and Biophysical Research Communications, 529(2), 224-230.

Elizondo, D. M., Andargie, T. E., Haddock, N. L., Boddie, T. A., & Lipscomb, M. W. (2019). Drebrin 1 in dendritic cells regulates phagocytosis and cell surface receptor expression through recycling for efficient antigen presentation. Immunology, 156(2), 136-146.

Gan, Y. J., Fang, A. W., Liu, C., Liu, B. J., Yang, F. M., Guan, J. T., ... & Chi, Z. L. (2019). Elevated Plasma Levels of Drebrin in Glaucoma Patients With Neurodegeneration. Frontiers in Neuroscience, 13, 326.

Krauss, R. S. (2017). Regulation of skeletal myoblast differentiation by drebrin. Drebrin, 361-373.

Liu, Y., Xu, Y. F., Zhang, L., Huang, L., Yu, P., Zhu, H., ... & Qin, C. (2017). Effective expression of Drebrin in hippocampus improves cognitive function and alleviates lesions of Alzheimer's disease in APP (swe)/PS 1 (ΔE9) mice. CNS neuroscience & therapeutics, 23(7), 590-604.

Li, B., Ding, S., Feng, N., Mooney, N., Ooi, Y. S., Ren, L., ... & Greenberg, H. B. (2017). Drebrin restricts rotavirus entry by inhibiting dynamin-mediated endocytosis. Proceedings of the National Academy of Sciences, 114(18), E3642-E3651.

Shirao, T., Hanamura, K., Koganezawa, N., Ishizuka, Y., Yamazaki, H., & Sekino, Y. (2017). The role of drebrin in neurons. Journal of Neurochemistry, 141(6), 819-834.

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

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