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Mouse Anti-MEF2A (AA 71-170) Recombinant Antibody (CBFYM-2024) (CBMAB-M2203-FY)

This product is mouse antibody that recognizes MEF2A. The antibody CBFYM-2024 can be used for immunoassay techniques such as: ELISA, IF, IHC-P, WB.
See all MEF2A antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2024
Antibody Isotype
IgG2a, k
Application
ELISA, IF, IHC-P, WB

Basic Information

Immunogen
Recombinant protein with GST tag
Specificity
Human
Antibody Isotype
IgG2a, k
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
0.31 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 71-170

Target

Full Name
MEF2A
Introduction
The protein encoded by this gene is a DNA-binding transcription factor that activates many muscle-specific, growth factor-induced, and stress-induced genes. The encoded protein can act as a homodimer or as a heterodimer and is involved in several cellular processes, including muscle development, neuronal differentiation, cell growth control, and apoptosis. Defects in this gene could be a cause of autosomal dominant coronary artery disease 1 with myocardial infarction. Several transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
UniProt ID
Alternative Names
Myocyte Enhancer Factor 2A; Serum Response Factor-Like Protein 1; Mef2; MADS Box Transcription Enhancer Factor 2, Polypeptide A (Myocyte Enhancer Factor 2A); Myocyte-Specific Enhancer Factor 2A; ADCAD1; RSRFC4; RSRFC9
Function
Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT]4TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous 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. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter.
Biological Process
Apoptotic process Source: UniProtKB-KW
Cardiac conduction Source: UniProtKB
Cell differentiation Source: GO_Central
Cellular response to calcium ion Source: UniProtKB
Dendrite morphogenesis Source: UniProtKB
ERK5 cascade Source: UniProtKB
Heart development Source: UniProtKB
MAPK cascade Source: UniProtKB
Mitochondrial genome maintenance Source: UniProtKB
Mitochondrion distribution Source: UniProtKB
Muscle organ development Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of cardiac muscle hypertrophy Source: BHF-UCL
Positive regulation of gene expression Source: Ensembl
Positive regulation of glucose import Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central
Transcription, DNA-templated Source: UniProtKB
Ventricular cardiac myofibril assembly Source: UniProtKB
Cellular Location
Nucleus
Involvement in disease
Coronary artery disease, autosomal dominant, 1 (ADCAD1):
A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction.
PTM
Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.
Sumoylation on Lys-403 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-408 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity).
Acetylation on Lys-403 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure.
Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation.

Chen, C., Wu, X., Han, T., Chen, J., Bian, H., Hei, R., ... & Zheng, Q. (2023). Mef2a is a positive regulator of Col10a1 gene expression during chondrocyte maturation. American Journal of Translational Research, 15(6), 4020.

Moustafa, A., Hashemi, S., Brar, G., Grigull, J., Ng, S. H., Williams, D., ... & McDermott, J. C. (2023). The MEF2A transcription factor interactome in cardiomyocytes. Cell Death & Disease, 14(4), 240.

Smith, J. R., Dowling, J. W., McFadden, M. I., Karp, A., Schwerk, J., Woodward, J. J., ... & Forero, A. (2023). MEF2A suppresses stress responses that trigger DDX41-dependent IFN production. Cell reports, 42(8).

Gao, Y., Liu, Y., Zheng, D., Ho, C., Wen, D., Sun, J., ... & Zhang, Y. (2022). HDAC5-mediated Smad7 silencing through MEF2A is critical for fibroblast activation and hypertrophic scar formation. International Journal of Biological Sciences, 18(15), 5724.

Chen, W., Zhang, K., Yang, Y., Guo, Z., Wang, X., Teng, B., ... & Qiu, Z. (2021). MEF2A-mediated lncRNA HCP5 inhibits gastric cancer progression via MiR-106b-5p/p21 axis. International Journal of Biological Sciences, 17(2), 623.

Xiao, Q., Gan, Y., Li, Y., Fan, L., Liu, J., Lu, P., ... & Yin, G. (2021). MEF2A transcriptionally upregulates the expression of ZEB2 and CTNNB1 in colorectal cancer to promote tumor progression. Oncogene, 40(19), 3364-3377.

Cilenti, F., Barbiera, G., Caronni, N., Iodice, D., Montaldo, E., Barresi, S., ... & Ostuni, R. (2021). A PGE2-MEF2A axis enables context-dependent control of inflammatory gene expression. Immunity, 54(8), 1665-1682.

Li, H., Wang, F., Guo, X., & Jiang, Y. (2021). Decreased MEF2A expression regulated by its enhancer methylation inhibits autophagy and may play an important role in the progression of Alzheimer’s disease. Frontiers in neuroscience, 15, 682247.

Zhang, C., Li, J., Li, H., Wang, G., Wang, Q., Zhang, X., ... & Xu, H. (2021). lncRNA MIR155HG accelerates the progression of sepsis via upregulating MEF2A by sponging miR-194-5p. DNA and Cell Biology, 40(6), 811-820.

Xiong, Y., Wang, L., Jiang, W., Pang, L., Liu, W., Li, A., ... & Liu, S. M. (2019). MEF2A alters the proliferation, inflammation-related gene expression profiles and its silencing induces cellular senescence in human coronary endothelial cells. BMC Molecular Biology, 20(1), 1-13.

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

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