BD Transduction Laboratories™ Purified Mouse Anti-MEF2D
Clone 9/MEF2D (RUO)
Western blot analysis of MEF2D on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2) . Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-MEF2D antibody.
Immunoflurorescence staining of Human Fibroblasts.
Western blot analysis of MEF2D on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2) . Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-MEF2D antibody.
Immunoflurorescence staining of Human Fibroblasts.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Companion Products
MEF2D is a member of the MEF2 (Myocyte-specific Enhancer-binding Factor 2) transcription factor family. Members of this family (MEF2A, B, C, & D) contain several characteristic motifs that include a MEF2 domain and a MADS box. MEF2 proteins bind the DNA sequence, 5'- (C/T)T(A/T)(A/T)AAATA(A/G)-3', and binding occurs primarily, although not exclusively, in muscle cells. MEF2D gene expression is ubiquitous and the mRNA is alternatively spliced. This results in multiple protein isoforms that heterodimerize with other family members. In addition to the MEF2 and MADS domains, MEF2D has a glutamine-/proline-rich region, amino acids 365-404, and a basic region, in the MADS domain near the N-terminus. The glutamine-/proline-rich region is involved in transactivation, while the basic region mediates sequence-specific DNA binding. MEF2D displays 75% similarity to hMEF2A and hMEF2C. Myogenin gene transcription requires MEF2D, indicating that MEF2D is involved in myogenesis and muscle cell differentiation. MEF2D has been reported to have a calculated molecular weight of 56 kD, but can be observed migrating in a range of 56-70 kD.
Development References (4)
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Breitbart RE, Liang CS, Smoot LB, Laheru DA, Mahdavi V, Nadal-Ginard B. A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage. Development. 1993; 118(4):1095-1106. (Biology). View Reference
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Guttridge DC, Mayo MW, Madrid LV, Wang CY, Baldwin AS. NF-kappaB-induced loss of MyoD messenger RNA: possible role in muscle decay and cachexia. J Biol Chem. 2000; 298(5488):2363-2366. (Biology: Western blot). View Reference
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Martin JF, Miano JM, Hustad CM, Copeland NG, Jenkins NA, Olson EN. A Mef2 gene that generates a muscle-specific isoform via alternative mRNA splicing. Mol Cell Biol. 1994; 14(3):1647-1656. (Biology). View Reference
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Mora S, Pessin JE. The MEF2A isoform is required for striated muscle-specific expression of the insulin-responsive GLUT4 glucose transporter. J Biol Chem. 2000; 275(21):16323-16328. (Biology: Immunoprecipitation). View Reference
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