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Mouse Anti-MEF2D (AA 346-511) Recombinant Antibody (CBFYM-2036) (CBMAB-M2216-FY)

This product is mouse antibody that recognizes MEF2D. The antibody CBFYM-2036 can be used for immunoassay techniques such as: WB, IF.
See all MEF2D antibodies

Summary

Host Animal
Mouse
Specificity
Human, Dog, Mouse, Rat
Clone
CBFYM-2036
Antibody Isotype
IgG1
Application
WB, IF

Basic Information

Immunogen
Mouse MEF2D aa. 346-511
Specificity
Human, Dog, Mouse, Rat
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
Concentration
0.25 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.
Epitope
AA 346-511

Target

Full Name
myocyte enhancer factor 2D
Introduction
This gene is a member of the myocyte-specific enhancer factor 2 family of transcription factors. Members of this family are involved in control of muscle and neuronal cell differentiation and development, and are regulated by class II histone deacetylases. Fusions of the encoded protein with Deleted in Azoospermia-Associated Protein 1 due to a translocation have been found in an acute lymphoblastic leukemia cell line, suggesting a role in leukemogenesis. The encoded protein may also be involved in Parkinson disease and myotonic dystrophy. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
Human4209
Mouse17261
Rat81518
Dog490413
UniProt ID
HumanQ14814
MouseQ63943
RatO89038
DogJ9P151
Alternative Names
Myocyte Enhancer Factor 2D
Function
Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT]4TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity).
Biological Process
Adult heart development Source: UniProtKB
Apoptotic process Source: UniProtKB-KW
Cell differentiation Source: GO_Central
Chondrocyte differentiation Source: Ensembl
Endochondral ossification Source: Ensembl
Muscle organ development Source: ProtInc
Nervous system development Source: UniProtKB-KW
Osteoblast differentiation Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Regulation of transcription by RNA polymerase II Source: GO_Central
Skeletal muscle cell differentiation Source: Ensembl
Cellular Location
Nucleus
Note: Translocated by HDAC4 to nuclear dots.
PTM
Phosphorylated on Ser-444 by CDK5 is required for Lys-439 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by CaMK4.
Acetylated on Lys-439 by CREBBP. Acetylated by EP300. Deacetylated by SIRT1 and HDAC3.
Sumoylated on Lys-439 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3.
Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation (By similarity).

Kim, Y. J., Oh, J., Jung, S., Kim, C. J., Choi, J., Jeon, Y. K., ... & Choi, Y. S. (2023). The transcription factor Mef2d regulates B: T synapse–dependent GC-TFH differentiation and IL-21–mediated humoral immunity. Science Immunology, 8(81), eadf2248.

Zhang, M., Zhang, H., Li, Z., Bai, L., Wang, Q., Li, J., ... & Chen, S. J. (2022). Functional, structural, and molecular characterizations of the leukemogenic driver MEF2D-HNRNPUL1 fusion. Blood, The Journal of the American Society of Hematology, 140(12), 1390-1407.

Wang, P., Zhao, J., & Sun, X. (2021). DYRK1A phosphorylates MEF2D and decreases its transcriptional activity. Journal of Cellular and Molecular Medicine, 25(13), 6082-6093.

Zhao, L., Zhang, P., Galbo Jr, P. M., Zhou, X., Aryal, S., Qiu, S., ... & Lu, R. (2021). Transcription factor MEF2D is required for the maintenance of MLL-rearranged acute myeloid leukemia. Blood Advances, 5(22), 4727-4740.

Lu, F., Wang, R., Xia, L., Nie, T., Gao, F., Yang, S., ... & Yang, Q. (2021). Regulation of IFN-Is by MEF2D promotes inflammatory homeostasis in microglia. Journal of Inflammation Research, 14, 2851.

Pattison, M. J., Naik, R. J., Reyskens, K. M., & Arthur, J. S. C. (2020). Loss of Mef2D function enhances TLR induced IL-10 production in macrophages. Bioscience Reports, 40(8), BSR20201859.

Xiang, J., Zhang, N. I., Sun, H., Su, L., Zhang, C., Xu, H., ... & Qian, C. (2020). Disruption of SIRT7 increases the efficacy of checkpoint inhibitor via MEF2D regulation of programmed cell death 1 ligand 1 in hepatocellular carcinoma cells. Gastroenterology, 158(3), 664-678.

Ohki, K., Kiyokawa, N., Saito, Y., Hirabayashi, S., Nakabayashi, K., Ichikawa, H., ... & Ohara, A. (2019). Clinical and molecular characteristics of MEF2D fusion-positive B-cell precursor acute lymphoblastic leukemia in childhood, including a novel translocation resulting in MEF2D-HNRNPH1 gene fusion. Haematologica, 104(1), 128.

Mohawk, J. A., Cox, K. H., Sato, M., Yoo, S. H., Yanagisawa, M., Olson, E. N., & Takahashi, J. S. (2019). Neuronal myocyte-specific enhancer factor 2D (MEF2D) is required for normal circadian and sleep behavior in mice. Journal of Neuroscience, 39(40), 7958-7967.

Hirano, D., Hayakawa, F., Yasuda, T., Tange, N., Yamamoto, H., Kojima, Y., ... & Kiyoi, H. (2019). Chromosomal translocation-mediated evasion from miRNA induces strong MEF2D fusion protein expression, causing inhibition of PAX5 transcriptional activity. Oncogene, 38(13), 2263-2274.

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

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