Recombinant Human Histone-lysine N-methyltransferase 2C (KMT2C), partial

Code CSB-YP822778HU
MSDS
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Source Yeast
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Code CSB-EP822778HU
MSDS
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Source E.coli
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Code CSB-EP822778HU-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-BP822778HU
MSDS
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Source Baculovirus
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Code CSB-MP822778HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Histone-lysine N-methyltransferase MLL3; Homologous to ALR protein; KMT2C; Lysine N-methyltransferase 2C; MLL3; MLL3_HUMAN; Myeloid/lymphoid or mixed-lineage leukemia protein 3; Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog
Species
Homo sapiens (Human)
Target Protein Sequence
MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR ARKKPRSRGK TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN SKQLIPTLQR SVSEESANSL VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL KQFRITPGFI LPWRNQPSNK KDIDDNSNGT YEKMQNSAPR KQRGQRKERS PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ ALFDSTGTCW AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP GDLLDQFFCT TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED SKMLVCDTCD KGYHTFCLQP VMKSVPTNGW KCKNCRICIE CGTRSSSQWH HNCLICDNCY QQQDNLCPFC GKCYHPELQK DMLHCNMCKR WVHLECDKPT DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT DYNNEMEVEG PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT ENIEVVTHQI TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV SPHEESISLC PEEQLVIERL QGEKEQKENS ELSTGLMDSE MTPTIEGCVK DVSYQGGKSI KLSSETESSF SSSADISKAD VSSSPTPSSD LPSHDMLHNY PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP RSKQGAWSTH NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS DKFTLNQDMC VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK GWRCLECTVC EACGKATDPG RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK CKWCVWCRHC GATSAGLRCE WQNNYTQCAP CASLSSCPVC YRNYREEDLI LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM PASNVPSSDC CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES SPEREAVDDE TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR SVIRKDSSGS ISEQLPCRDD GWSEQLPDTL VDESVSVTES TEKIKKRYRK RKNKLEETFP AYLQEAFFGK DLLDTSRQSK ISLDNLSEDG AQLLYKTNMN TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT DDDILGIISD DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI HNQDAFSRMP LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK NSAFNPMASD PNNSWTSSAP TVEGENDTMS NAQRSTLKWE KEEALGEMAT VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK LWRKASSQER APYVQKARDN RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL KQRESEHEQE WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP QAPPPPPAPS RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK MVGTPRPPPV GHSFSRRNSA APVENCTPLS SVSRPLQMNE TTANRPSPVR DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK SLGLSRSPVV SEQTAKGPIA AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP GPFKTPMQPP PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG TARSNTDPYS QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS DPYAHPPGTP RPGISVPYSQ PPATPRPRIS EGFTRSSMTR PVLMPNQDPF LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG PGLSDTFSRV SPSAARDPYD QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS PMHSQGQQFS GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP LGPRYAVFPK DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV PPQQIQGSGV SPQLRRSVSV DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS VVEASSNLRH GNFIPRPDFP GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH SSSMVMRTLN HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR SGEFDIIAYT DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE NKTLVLSDKH SPQKKSTVTN EVKTEVLSPN SKVESKCETE KNDENKDNVD TPCSQASAHS DLNDGEKTSL HPCDPDLFEK RTNRETAGPS ANVIQASTQL PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP PTLPASPSNH VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE QPLLLQDLLD QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK MVALKGINKV MAQNNLGMPP MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP QDGSITHQIS RPNPPNFGPG FVNDSQRKQY EEWLQETQQL LQMQQKYLEE QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ QSMVQKQLEQ IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR IQPPIAQLPI KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER KERLREQQER QRIQLMQEVD RQRALQQRME MEQHGMVGSE ISSSRTSVSQ IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG QVLQQQNIQQ GSINSPSTQT FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS GTSFQQSPVR PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS ELPQQADQES VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA NSEVDKLSME TPAKTEEIKL EKAETESCPG QEEPKLEEQN GSKVEGNAVA CPVSSAQSPP HSAGAPAAKG DSGNELLKHL LKNKKSSSLL NQKPEGSICS EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT DGGSETKKQR SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ QNNLSNPPTP PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP FRPQDDLLAR ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS FVPSSSPESV VGVEVSRYPD LSLVKEEPPE PVPSPIIPIL PSTAGKSSES RRNDIKTEPG TLYFASPFGP SPNGPRSGLI SVAITLHPTA AENISSVVAA FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ HLLLRGPPPG SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA QAKNSENKES IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS PPASPPIAFP PAFEAAQVEA KPDELKVTVK LKPRLRAVHG GFEDCRPLNK KWRGMKWKKW SIHIVIPKGT FKPPCEDEID EFLKKLGTSL KPDPVPKDYR KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY ETQAGALINV ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV GSLIFHTIGQ LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC SIEEKDGRPV FVIRIVEQGH EDLVLSDISP KGVWDKILEP VACVRKKSEM LQLFPAYLKG EDLFGLTVSA VARIAESLPG VEACENYTFR YGRNPLMELP LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS TVTGELNAPY SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS CAPNCVAEVV TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH CGAVNCRKWM N
Protein Length
partial
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.
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.

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Target Background

Function
Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place. Likely plays a redundant role with KMT2D in enriching H3K4me1 mark on primed and active enhancer elements.
Gene References into Functions
  1. Our data indicate that KMT2C ELs are associated with specific genetic features and that SPRY4 ELs may add prognostic information. PMID: 28940816
  2. Overexpression of KMT2C is associated with Estrogen Receptor-positive Breast Cancer. PMID: 27986439
  3. Somatic MLL3 mutations are associated with metastatic NUT midline carcinoma. PMID: 28967088
  4. MLL3 binding was dependent on FOXA1, indicating that FOXA1 recruits MLL3 to chromatin. MLL3 silencing decreased H3K4me1 at enhancer elements but had no appreciable impact on H3K4me3 at enhancer elements. We propose a mechanism whereby the pioneer factor FOXA1 recruits the chromatin modifier MLL3 to facilitate the deposition of H3K4me1 histone marks, subsequently demarcating active enhancer elements PMID: 27926873
  5. trr and G9a also have common direct targets, including the Drosophila ortholog of Arc (Arc1), a key regulator of synaptic plasticity. Our data highlight the clinical and molecular convergence between the KMT2 and EHMT protein families, which may contribute to a molecular network underlying a larger group of intellectual disability / autism spectrum disorder -related disorders. PMID: 29069077
  6. we demonstrate that low KMT2C and KMT2D expression in biopsies defines better outcome groups in pancreatic ductal adenocarcinoma PMID: 27280393
  7. Study found that rs6943984 and rs4725443 of the MLL3 gene were significantly associated with the risk of larynx cancer. PMID: 26818916
  8. MLL3 expression plays a vital role in gastric cancer development, and that this protein is an important marker for the prognosis of gastric cancer. PMID: 25222251
  9. a minimized human RBBP5-ASH2L heterodimer is the structural unit that interacts with and activates all MLL family histone methyltransferases PMID: 26886794
  10. solution structures of the MLL3 core complex assembled with and without WDR5 by small angle x-ray scattering show similar overall topologies PMID: 26324722
  11. We propose that MLL3 and MLL4 are broadly required for controlling MAFA and MAFB transactivation during development and postnatally. PMID: 26180087
  12. Taken together, our study suggested that downregulation of MLL3 was very important in the progression of ESCC PMID: 25273170
  13. Label-free quantitative comparison of DN urinary exosomes vs control group and SRM further validation, resulted in the discovery of a panel of three proteins (AMBP, MLL3 and VDAC1) which changes in DN. PMID: 24211404
  14. concluded that this novel missense (S3660L) mutation in MLL3 gene is likely to increase the gastric cancer risk PMID: 24965397
  15. Mll3 genetic variantsare associated with gastric cancer. PMID: 23991983
  16. MLL3 and MLL4 function in the regulation of enhancer activity. PMID: 24081332
  17. frameshift mutations of MLL genes and loss of expression of MLL3 protein are common in gastric and colorectal cancers with MSI-H. PMID: 23259788
  18. Germ line mutation of MLL3 was found in a pedigee having colorectal cancer and acute myeloid leukemia. PMID: 23429989
  19. the second PHD finger (PHD2) of MLL1 is an E3 ubiquitin ligase in the presence of the E2-conjugating enzyme CDC34. This activity is conserved in the second PHD finger of MLL4, the closest homolog to MLL1 but not in MLL2 or MLL3. PMID: 23129768
  20. No somatic mutations were identified in the PTCH1, MLL2, and MLL3 genes in our cohort of hepatoblastoma samples PMID: 22183980
  21. p53-dependent histone 3-lysine-4-trimethylation of small heterodimer partner requires MLL3 PMID: 22034226
  22. Frameshift mutations of MLL3 in both colorectal cancer cells and primary tumor that were more common in cases with microsatellite instability. PMID: 21853109
  23. sequenced all 59 exons of MLL3 (14.7 Kb coding sequence) in 38 breast cancers from Chinese women, and found three somatic mutations in two of the cases, including one frameshift mutation (c.2687 ins A) PMID: 21116761
  24. These studies demonstrated that HOXC6 is an estrogen-responsive gene, and that histone methylases MLL2 and MLL3, in coordination with ERalpha and ERbeta, transcriptionally regulate HOXC6 in an estrogen-dependent manner. PMID: 21683083
  25. The trimethylation of histone H3 at Lys 4 by the MLL2/MLL3 subunits of ASCOM, enhanced by the hormone-induced displacement of the H3K4 demethylase KDM5B, stabilizes NURF binding. PMID: 21447625
  26. There were no MLL3 mutations in Korean patients with colorectal carcinomas. PMID: 17614854
  27. analysis identified 1 somatic mutation of MLL3 among 57 colon tumors (1.8%), encoding a heterozygous missense mutation, S3449F; study identified also several novel non-synonymous germline variants of MLL3, likely representing previously unidentified SNPs PMID: 19215798
  28. Study show that the C-terminal SET domain of MLL3 and MLL4 directly interacts with INI1, an integral subunit of Swi/Snf. PMID: 19221051
  29. ASCOM-MLL3 and ASCOM-MLL4 play redundant but essential roles in FXR transactivation via their histone 3 lysine 4 trimethylation activity. PMID: 19556342
  30. PTIP and PA1 are both components of the MLL3- and MLL4-containing histone H3 K4 methyltransferase complex that also includes ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, and JmjC domain-containing putative histone demethylase UTX. PMID: 17500065

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Subcellular Location
Nucleus.
Protein Families
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily
Tissue Specificity
Highly expressed in testis and ovary, followed by brain and liver. Also expressed in placenta, peripherical blood, fetal thymus, heart, lung and kidney. Within brain, expression was highest in hippocampus, caudate nucleus, and substantia nigra. Not detect
Database Links

HGNC: 13726

OMIM: 606833

KEGG: hsa:58508

STRING: 9606.ENSP00000262189

UniGene: Hs.647120

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