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Mouse Anti-EMD Recombinant Antibody (3B9) (CBMAB-A2581-LY)

The product is antibody recognizes EMD. The antibody 3B9 immunoassay techniques such as: WB, ELISA.
See all EMD antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3B9
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
EMD (AAH00738, 1 a.a. ~ 110 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
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
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
emerin
Introduction
Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene. [provided by RefSeq]
Entrez Gene ID
2010
UniProt ID
P50402
Alternative Names
EDMD; LEMD5; STA
Research Area
Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C.
Biological Process
Cellular response to growth factor stimulus Source: BHF-UCL
Muscle contraction Source: ProtInc
Muscle organ development Source: ProtInc
Negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
Negative regulation of fibroblast proliferation Source: BHF-UCL
Nuclear membrane organization Source: FlyBase
Positive regulation of protein export from nucleus Source: BHF-UCL
Regulation of canonical Wnt signaling pathway Source: BHF-UCL
Skeletal muscle cell differentiation Source: Ensembl
Cellular Location
Nucleus inner membrane; Nucleus outer membrane. Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.
Involvement in disease
Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1):
A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Topology
Helical: 223-243
PTM
Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle.

Du, Z., Zhu, T., Lin, M., Bao, Y., Qiao, J., Lv, G., ... & Xie, Y. (2022). A novel mutation in human EMD gene and mitochondrial dysfunction in emerin knockdown cardiomyocytes. Journal of Cellular and Molecular Medicine.

Lee, B., Lee, S., Lee, Y., Park, Y., & Shim, J. (2021). Emerin represses stat3 signaling through nuclear membrane-based spatial control. International journal of molecular sciences, 22(13), 6669.

Wu, K. Y., Xie, H., Zhang, Z. L., Li, Z. X., Shi, L., Zhou, W., ... & Shen, W. G. (2021). Emerin knockdown induces the migration and invasion of hepatocellular carcinoma cells by up-regulating the cytoplasmic p21. Neoplasma.

Iyer, A., & Holaska, J. M. (2020). EDMD-Causing Emerin Mutant Myogenic Progenitors Exhibit Impaired Differentiation Using Similar Mechanisms. Cells, 9(6), 1463.

Nastały, P., Purushothaman, D., Marchesi, S., Poli, A., Lendenmann, T., Kidiyoor, G. R., ... & Maiuri, P. (2020). Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus. Nature communications, 11(1), 1-12.

Wang, Y., Shin, J. Y., Nakanishi, K., Homma, S., Kim, G. J., Tanji, K., ... & Worman, H. J. (2019). Postnatal development of mice with combined genetic depletions of lamin A/C, emerin and lamina-associated polypeptide 1. Human molecular genetics, 28(15), 2486-2500.

Dharmaraj, T., Guan, Y., Liu, J., Badens, C., Gaborit, B., & Wilson, K. L. (2019). Rare BANF1 alleles and relatively frequent EMD alleles including ‘healthy lipid’emerin p. D149H in the ExAC cohort. Frontiers in Cell and Developmental Biology, 7, 48.

Wada, E., Kato, M., Yamashita, K., Kokuba, H., Liang, W. C., Bonne, G., & Hayashi, Y. K. (2019). Deficiency of emerin contributes differently to the pathogenesis of skeletal and cardiac muscles in LmnaH222P/H222P mutant mice. Plos one, 14(8), e0221512.

Dubińska-Magiera, M., Kozioł, K., Machowska, M., Piekarowicz, K., Filipczak, D., & Rzepecki, R. (2019). Emerin is required for proper nucleus reassembly after mitosis: Implications for new pathogenetic mechanisms for laminopathies detected in EDMD1 patients. Cells, 8(3), 240.

Pradhan, R., Ranade, D., & Sengupta, K. (2018). Emerin modulates spatial organization of chromosome territories in cells on softer matrices. Nucleic acids research, 46(11), 5561-5586.

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

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