MEF2D antibody (Myocyte Enhancer Factor 2D) (N-Term)

Details for Product anti-MEF2D Antibody No. ABIN966557, Supplier: Log in to see
Antigen
  • sl1
  • sl-1
  • XMEF2D
  • MGC145245
  • C80750
  • myocyte enhancer factor 2D
  • MADS box transcription enhancer factor 2, polypeptide D (myocyte enhancer factor 2D)
  • mef2d
  • MEF2D
  • Mef2d
Epitope
N-Term
22
16
12
11
11
10
9
8
8
7
6
6
4
3
2
2
2
1
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
131
63
61
4
4
3
3
2
2
1
1
1
Host
Rabbit
109
22
Clonality
Polyclonal
Conjugate
This MEF2D antibody is un-conjugated
7
7
7
4
4
4
3
3
3
3
3
3
3
3
3
3
3
Application
Immunohistochemistry (IHC)
89
44
39
19
17
10
5
4
1
Options
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human MEF2D (Myocyte-specific enhancer factor 2D)
Alternative Name MEF2D (MEF2D Antibody Abstract)
Background MEF2D (Myocyte-specific enhancer factor 2D) is a transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. MEF2D mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. MEF2D 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. MEF2D plays a critical role in the regulation of neuronal apoptosis (By similarity). MEF2D forms a complex with class II HDACs in undifferentiating cells. On myogenic differentiation, HDACs are released into the cytoplasm allowing MEF2s to interact with other proteins for activation. Interacts with HDAC4 (in undifferentiating cells), the interaction translocates MEF2D to nuclear dots. Forms a heterodimer with MEF2A. 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. Phsophorylation on Ser-180 can be enhanced by EGF.
Restrictions For Research Use only
Background publications Beausoleil, Jedrychowski, Schwartz, Elias, Villén, Li, Cohn, Cantley, Gygi: "Large-scale characterization of HeLa cell nuclear phosphoproteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 33, pp. 12130-5, 2004 (PubMed).

Wang, Bertos, Vezmar, Pelletier, Crosato, Heng, Thng, Han, Yang: "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor." in: Molecular and cellular biology, Vol. 19, Issue 11, pp. 7816-27, 1999 (PubMed).

Product cited in: Okamoto, Li, Ju, Scholzke, Mathews, Cui, Salvesen, Bossy-Wetzel, Lipton: "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 6, pp. 3974-9, 2002 (PubMed).

Kato, Zhao, Morikawa, Sugiyama, Chakravortty, Koide, Yoshida, Tapping, Yang, Yokochi, Lee: "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family." in: The Journal of biological chemistry, Vol. 275, Issue 24, pp. 18534-40, 2000 (PubMed).

Zhao, New, Kravchenko, Kato, Gram, di Padova, Olson, Ulevitch, Han: "Regulation of the MEF2 family of transcription factors by p38." in: Molecular and cellular biology, Vol. 19, Issue 1, pp. 21-30, 1999 (PubMed).

Breitbart, Liang, Smoot, Laheru, Mahdavi, Nadal-Ginard: "A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage." in: Development (Cambridge, England), Vol. 118, Issue 4, pp. 1095-106, 1994 (PubMed).