Recombinant Human Myocyte-specific enhancer factor 2A (MEF2A)

Code CSB-YP013670HU
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP013670HU
MSDS
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP013670HU-B
MSDS
Size Pls inquire
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP013670HU
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP013670HU
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
MEF2A
Uniprot No.
Alternative Names
ADCAD1; MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A) ; MEF2; MEF2A; MEF2A_HUMAN; Myocyte enhancer factor 2A; Myocyte-specific enhancer factor 2A; RSRFC4; RSRFC9; Serum response factor like protein 1 ; Serum response factor-like protein 1
Species
Homo sapiens (Human)
Expression Region
1-507
Target Protein Sequence
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFNSPGMLS LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI SIKSEPISPP RDRMTPSGFQ QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE DRESPSVKRM RMDAWVT
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

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

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. PCGME1 silencing by small interfering RNA significantly induced early cell apoptosis but this effect was reduced by a miR148a inhibitor. In conclusion, the present study demonstrated a positive regulatory association between MEF2 and PCGEM1, and a reciprocal negative regulatory association between PCGEM1 and miR148a that controls cell apoptosis. PMID: 29749452
  2. H cordata promotes the activation of HIF-1A-FOXO3 and MEF2A pathways. PMID: 27698266
  3. in leiomyosarcomas (LMS), this two-faced trait of MEF2 is relevant for tumor aggressiveness. Class IIa HDACs are overexpressed in 22% of LMS, where high levels of MEF2, HDAC4 and HDAC9 inversely correlate with overall survival. The knock out of HDAC9 suppresses the transformed phenotype of LMS cells, by restoring the transcriptional proficiency of some MEF2-target loci PMID: 28419090
  4. The discovery of a novel MEF2A mutation in a Chinese family with premature CAD/MI suggests that MEF2A may have a significant role in the pathogenesis of premature CAD/MI. PMID: 27221044
  5. The findings of this study are consistent with MEF2A deregulation conferring risk of formal thought disorder. PMID: 26421691
  6. Variants in the 3'-UTR of MEF2A are associated with coronary artery disease in a Chinese Han population. PMID: 26400337
  7. p38 MAPK is a key regulator of canonical Wnt signaling by promoting a phospho-dependent interaction between MEF2 and beta-catenin to enhance cooperative transcriptional activity and cell proliferation. PMID: 26552705
  8. Mechanistically, MEF-2 was recruited to the viral promoter (LTR, long terminal repeat) in the context of chromatin, and constituted Tax/CREB transcriptional complex via direct binding to the HTLV-1 LTR. PMID: 25809782
  9. Our results revealed a link and interaction between MEF2A and miR-143 and suggested a potential mechanism for MEF2A to regulate H(2)O(2) -induced VSMC senescence. PMID: 25655189
  10. six or seven amino acid deletions and synonymous mutations (147143G-->A)in exon 11 of the MEF2A gene may be correlated with susceptibility to coronary artery disease in the Chinese population PMID: 25366733
  11. 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
  12. MEF2 transcription factors promotes epithelial-mesenchymal transition and invasiveness of hepatocellular carcinoma through TGF-beta1 autoregulation circuitry. PMID: 25087096
  13. MEF2 is the key cis-acting factor that regulates expression of a number of transcriptional targets involved in pulmonary vascular homeostasis, including microRNAs 424 and 503, connexins 37, and 40, and Kruppel Like Factors 2 and 4. PMID: 25336633
  14. SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation. PMID: 23224591
  15. This study expands our understanding of the regulation of MEF2 in skeletal muscle and identifies the mAKAP scaffold as a facilitator of MEF2 transcription and myogenic differentiation. PMID: 22484155
  16. Correlation studies depicted two distinct groups of soft tissue sarcomas: one in which MEF2 repression correlates with PTEN downregulation and a second group in which MEF2 repression correlates with HDAC4 levels. PMID: 24043307
  17. Mutations in MEF2A exon12 are implicated in pathogenesis of premature coronary artery disease in the Chinese population. PMID: 23461724
  18. Substitution of any of the TFBS from our particular search of MEF2, CREB and SRF significantly decreased the number of identified clusters. PMID: 23382855
  19. DNA methylation of genes in retinol metabolism and calcium signaling pathways (P < 3 x 10-6) and with known functions in muscle and T2D including MEF2A, RUNX1, NDUFC2, and THADA decreased after exercise PMID: 23028138
  20. The rare 21-bp deletion might have a more compelling effect on coronary artery disease (CAD) than the common (CAG)(n) polymorphism, and MEF2A genetic variant might be a rare but specific cause of CAD/myocardial infarction. PMID: 22363637
  21. MEF2A dominant negative mutation enhanced cell proliferation and cell migration. PMID: 22028303
  22. [review] In this work, the mechanisms of regulation of MEF2 function by several well-known neurotoxins and their implications in various neurodegenerative diseases are reviewed. PMID: 21741404
  23. In a cohort of patients undergoing coronary angiography for suspected coronary artery disease the MEF2A exon 11 deletion occurred in 0.09%. PMID: 21450604
  24. HCVne particles are capable of inducing the recently discovered ERK5 pathway, in a dose dependent way. PMID: 21767578
  25. MEF2 positively regulates the expression of HZF1. PMID: 21468593
  26. No Chinese Taiwanese coronary patients had Pro279Leu & 21-bp deletion mutations in exons 7 & 11 respectively. The distribution of the allele frequencies of MEF2A exon 11 CAG repeat (CAG)n polymorphism was similar in both patients and controls. PMID: 19153100
  27. 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
  28. These results identify MEF2A gene as a susceptibility gene for coronary artery disease. PMID: 19782985
  29. The current structure suggests that the ligand-binding pocket is not induced by cofactor binding but rather preformed by intrinsic folding. PMID: 20132824
  30. 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
  31. MEF2A is not a susceptibility gene for coronary artery disease and premature myocardial infarction in the Italian population. PMID: 20031581
  32. The C-terminal region in MEF2A contains signals that are necessary to localize the histone deacetylase 4/MEF2 complex to the nucleus. PMID: 11792813
  33. identification of two aspects of MEF2 regulation, a highly conserved phosphoacceptor site and an indirect pathway of regulation by p38 MAPK PMID: 12586839
  34. MEF2a binding to HDAC5 is inhibited by HDAC5 when bound to Ca(2+)/calmodulin PMID: 12626519
  35. GEF and MEF2A have roles in regulating the GLUT4 promoter PMID: 14630949
  36. an autosomal dominant form of coronary artery disease/myocardial infarction (adCAD1) that is caused by the deletion of seven amino acids in transcription factor MEF2A is described PMID: 14645853
  37. Activation of MEF2 in skeletal muscle is regulated via parallel intracellular signaling pathways in response to insulin, cellular stress, or activation of AMPK. PMID: 14960415
  38. MEF2A is a candidate for chronic diaphragmatic hernia; it maps to chromosome 15. PMID: 15057983
  39. myogenin and myocyte enhancer factor-2 expression are triggered by membrane hyperpolarization during human myoblast differentiation PMID: 15084602
  40. promoter- and cell-specific functional interaction between PITX2 and MEF2A PMID: 15466416
  41. Myocyte enhancer factor 2 activates P2 promoter of the AbetaH-J-J locus. PMID: 15798210
  42. One disease-causing gene for CAD and MI has been identified as MEF2A, which is located on chromosome 15q26.3 and encodes a transcriptional factor with a high level of expression in coronary endothelium. PMID: 15811259
  43. 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
  44. Results suggest that MEF2A mutations are not a common cause of coronary artery disease (CAD) in white people and argue strongly against a role for the MEF2A 21-bp deletion in autosomal dominant CAD. PMID: 15841183
  45. The MEF2A mutations may account for up to 1.93% of the disease population; thus, genetic testing based on mutational analysis of MEF2A may soon be available for many coronary artery disease/myocardial infarction patients. PMID: 15861005
  46. The genetic risk factor for myocardial infarction could be the result of a reduced transcriptional activity on MEF2A with 279Leu. PMID: 15958500
  47. MEF2/HAND1 interaction results in synergistic activation of MEF2-dependent promoters, and MEF2 binding sites are sufficient to mediate this synergy PMID: 16043483
  48. Binding of this protein to DNA resulted in significant changes of its diffusion. PMID: 16314281
  49. data show a dosage-dependent cardiomyopathic phenotype and a progressive reduction in ventricular performance associated with MEF2A or MEF2C overexpression PMID: 16469744
  50. Study demonstrates that human intestinal cell BCMO1 expression is dependent on the functional cooperation between peroxisome proliferator-activated receptor-gamma and myocyte enhancer factor 2 isoforms. PMID: 16504037

Show More

Hide All

Involvement in disease
Coronary artery disease, autosomal dominant, 1 (ADCAD1)
Subcellular Location
Nucleus.
Protein Families
MEF2 family
Tissue Specificity
Isoform MEF2 and isoform MEFA are expressed only in skeletal and cardiac muscle and in the brain. Isoform RSRFC4 and isoform RSRFC9 are expressed in all tissues examined.
Database Links

HGNC: 6993

OMIM: 600660

KEGG: hsa:4205

STRING: 9606.ENSP00000346389

UniGene: Hs.268675

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1