Recombinant Mouse Myocyte-specific enhancer factor 2A (Mef2a)

Code CSB-YP726688MO
MSDS
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Source Yeast
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Code CSB-EP726688MO
MSDS
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Source E.coli
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Code CSB-EP726688MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP726688MO
MSDS
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Source Baculovirus
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Code CSB-MP726688MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Mef2a
Uniprot No.
Alternative Names
Mef2a; Myocyte-specific enhancer factor 2A
Species
Mus musculus (Mouse)
Expression Region
1-498
Target Protein Sequence
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLAASS TLADSSMLSP PPATLHRNVS PGAPQRPPST GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT GANSLGKVMP TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG FTSPGMLSLG QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI KSEPISPPRD RMTPSGFQQQ QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS SSSSSYDGSD REDPRGDFHS PIVLGRPPNT EDRESPSVKR MRMDTWVT
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-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.
Gene References into Functions
  1. Canonical pathway analysis of genes preferentially dysregulated in the atria and ventricles revealed distinct MEF2A-dependent cellular processes in each cardiac chamber. In the atria, MEF2A regulated genes involved in fibrosis and adhesion, whereas in the ventricles, it controlled inflammation and endocytosis. PMID: 29054930
  2. Both synapse silencing and elimination required de novo transcription, but only silencing required the activity-dependent transcription factors MEF2A/D. PMID: 28901289
  3. Deficiency of AKT2 in myocardium results in diminished MEF2A abundance, which induced decreased size of cardiomyocytes. We additionally confirmed that EndoG, which is also regulated by AKT2, is a suppressor of MEF2A in myocardium. PMID: 28965945
  4. Nuclear HDAC4 binds to chromatin as well as to MEF2A transcription factor, leading to histone deacetylation and altered neuronal gene expression. By using a Cdkl5 knockout (Cdkl5 -/Y) mouse model, we found that hypophosphorylated HDAC4 translocates to the nucleus of neural precursor cells, thereby reducing histone 3 acetylation. PMID: 27466189
  5. Knockdown of MEF2A significantly reduced hyperglycemia-induced cardiac fibroblast proliferation and migration, myofibroblast differentiation, matrix metalloproteinase activities, and collagen production. PMID: 26482596
  6. Lentivirus-mediated MEF 2A shRNA accelerates inflammation and atherosclerosis in APOE knockout mice, but has no effect on lipoprotein levels in plasma. PMID: 25793529
  7. microRNAs encoded by the Gtl2-Dio3 noncoding RNA locus function downstream of the MEF2A PMID: 26240138
  8. Our results indicated that exercise-induced CPT1b expression was at least in part mediated by HDAC5/MEF2A interaction. PMID: 25213552
  9. MEF2A is targeted to lysosomes for chaperone-mediated autophagy degradation; oxidative stress-induced lysosome destabilization leads to the disruption of MEF2A degradation as well as the dysregulation of its function PMID: 24879151
  10. Whereas MEF2A is absolutely required for proper myoblast differentiation, MEF2B, -C, and -D were found to be dispensable for this process. PMID: 25416778
  11. A role for endogenous MEF2 factors exclusively in hormone/Fsk/cAMP-induced Nr4a1 gene expression in mouse MA-10 Leydig cells. PMID: 24694307
  12. Combined deletion of the Mef2a, c, and d genes results in a blockade to muscle regeneration. PMID: 24591619
  13. Cross-talk between p38MAPK and GSK3beta signaling converges on MEF2 activity. PMID: 23137781
  14. Myocyte enhancer factor 2A (MEF2A) controls skeletal muscle regeneration in adult mice through direct regulation of the largest known mammalian microRNA (miRNA) cluster, the Gtl2-Dio3 locus. PMID: 23154418
  15. These results give novel insight into the molecular interplay of GR and MEF2 in the control of genes important for neuronal plasticity. PMID: 22622902
  16. MEF2A, but not MEF2C or MEF2D, is modified by ubiquitination in dopaminergic neuronal cell line SN4741 cells. PMID: 22764880
  17. The data highlighted the key in vivo role of MEF2C isoform in the brain and suggest that MEF2A and MEF2D have only subtle roles in regulating hippocampal synaptic function. PMID: 22496871
  18. establish miR-155 as an important regulator of MEF2A expression and uncover its function in muscle gene expression and myogenic differentiation. PMID: 21868385
  19. Exercise increases the nuclear MEF2A content and binding of MEF2A to their binding sites on the Glut4 gene by an AMPKalpha2-dependent mechanism. PMID: 21233771
  20. The Mef2A transcription factor coordinately regulates a costamere gene program in cardiac muscle. PMID: 21724844
  21. A systems biology study integrating mRNA profiles with DNA-binding events of key cardiac transcription factors (Gata4, Mef2a, Nkx2.5, and Srf), activating histone modifications (H3ac, H4ac, H3K4me2, and H3K4me3), and microRNA profiles, is reported. PMID: 21379568
  22. ZAC1 is a novel and previously unknown regulator of cardiomyocyte Glut4 expression and glucose uptake; MEF2 is a regulator of ZAC1 expression in response to induction of hypertrophy PMID: 20363751
  23. active MEF2 and fragile X mental retardation protein function together in an acute, cell-autonomous mechanism to eliminate excitatory synapses. PMID: 20434996
  24. Reveal a novel MEF2A-Xirp2 pathway that functions downstream of Ang II signaling to modulate its pathological effects in the heart. PMID: 20093629
  25. TGF-beta transcriptionally upregulated MMP-10 through activation of MEF2A, concomitant with acetylation of core histones increasing around the promoter, as a consequence of degradation of the class IIa HDACs. PMID: 19935709
  26. Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via the HLH domain, MEF2 interaction, and chromatin deacetylation PMID: 11809751
  27. deficient mice suffered sudden cardiac death PMID: 12379849
  28. MEF2A expression is regulated by BMP-2-induced PI 3-kinase signaling PMID: 12663654
  29. Calcineurein regulates skeletal muscle differentiation by activating MEF2 and MyoD transcription factors. PMID: 12694204
  30. MEF2 has a role in maintaining GLUT4 in adult muscle and cooperates with MyoD transcription factors and thyroid hormone receptors in regulating GLUT4 in regenerating muscle PMID: 12893821
  31. GEF and MEF2A have roles in regulating the GLUT4 promoter PMID: 14630949
  32. MEF2A is induced by CUGPB-1 and along with p21, it inhibits myogenesis and contributes to the development of muscle deficiency myotonic dystrophy PMID: 14722059
  33. Data show that static stretch application produces a robust increase in p38 phosphorylation preceding MEF2A, but not NFATc1, nuclear translocation. PMID: 15483225
  34. MEF2 has a role in regulating genes during muscle differentiation PMID: 15507520
  35. Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo PMID: 15728583
  36. A conserved pattern of alternative splicing in vertebrate MEF2 (myocyte enhancer factor 2) genes generates an acidic activation domain in MEF2 proteins selectively in tissues where MEF2 target genes are highly expressed. (MEF2) PMID: 15834131
  37. MEF2/HAND1 interaction results in synergistic activation of MEF2-dependent promoters, and MEF2 binding sites are sufficient to mediate this synergy PMID: 16043483
  38. MEF2A up-regulates myospryn at the costamere in striated muscle potentially playing a role in myofibrillogenesis. PMID: 16407236
  39. MEF2 transcription factors in the postnatal heart activate a genetic program that minimally affects cardiac growth yet promotes chamber dilation, mechanical dysfunction, and dilated cardiomyopathy. PMID: 16847152
  40. Myomaxin functions directly downstream of MEF2A at the peripheral Z-disc complex in striated muscle potentially playing a role in regulating cytoarchitectural integrity PMID: 17046827
  41. Differences in GLUT4 transcription when whole adipose tissue and cell culture model systems are compared can be correlated to a posttranslational phosphorylation of the transcription factor MEF2A. PMID: 17164432
  42. ataxin-1 antagonizes the neuronal survival function of myocyte enhancer factor-2 PMID: 17646162
  43. SOST expression in osteocytes of adult bone and its inhibition by PTH is mediated by MEF2A, C, and D transcription factors controlling the SOST bone enhancer. PMID: 17696759
  44. MEF2 has a central role as a regulator of the transcriptional and posttranscriptional pathways that control cardiac and skeletal muscle development PMID: 18093911
  45. GLUT4 enhancer factor (GEF) interacts with MEF2A and HDAC5 to regulate the GLUT4 promoter in adipocytes. PMID: 18216015
  46. These findings support a role for MEF2A as an intermediary in coordinating respiratory chain subunit expression in heart and muscle through a NRF1 --> MEF2A --> COX(H) transcriptional cascade. PMID: 18222924
  47. miR-1 regulates cardiomyocyte growth responses by negatively regulating the calcium signaling components calmodulin, Mef2a, and Gata4 PMID: 19188439

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Subcellular Location
Nucleus.
Protein Families
MEF2 family
Tissue Specificity
Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Differentially expressed depending on if isoforms contain the beta domain or not, with the total expression of the beta domain-lacking isoforms vastl
Database Links
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