Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: > 90% SDS-PAGE
- Active: Yes
- Tags: GST tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant human KMT2A / MLL protein (Active)
The specific activity of ab268799 was 600 pmol/min/mg in a methyltransferase assay using histone H3 peptide (1-21) as substrate.
Purity> 90 % SDS-PAGE.
Expression systemBaculovirus infected Sf9 cells
Protein lengthProtein fragment
SequenceKHCRNYKFRF HKPEEANEPP LNPHGSARAE VHLRKSAFDM FNFLASKHRQ PPEYNPNDEE EEEVQLKSAR RATSMDLPMP MRFRHLKKTS KEAVGVYRSP IHGRGLFCKR NIDAGEMVIE YAGNVIRSIQ TDKREKYYDS KGIGCYMFRI DDSEVVDATM HGNAARFINH SCEPNCYSRV INIDGQKHIV IFAMRKIYRG EELTYDYKFP IEDASNKLPC NCGAKKCRKF LN
Molecular weight information52 kDa by SDS-PAGE
Amino acids3738 to 3969
TagsGST tag N-Terminus
Additional sequence informationNM_005933
Our Abpromise guarantee covers the use of ab268799 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.79% Tris HCl, 0.87% Sodium chloride, 0.31% Glutathione, 0.003% EDTA, 0.004% DTT, 0.002% PMSF, 25% Glycerol (glycerin, glycerine)
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- C-terminal cleavage product of 180 kDa
FunctionHistone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis.
Tissue specificityHeart, lung, brain and T- and B-lymphocytes.
Involvement in diseaseNote=Chromosomal aberrations involving MLL are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with MLLT4/AF6; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with CASC5 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins MLL-MLLT1, MLL-MLLT3 and MLL-ELL interact with PPP1R15A and, on the contrary to unfused MLL, inhibit PPP1R15A-induced apoptosis.
Note=A chromosomal aberration involving MLL may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11.
Sequence similaritiesBelongs to the histone-lysine methyltransferase family. TRX/MLL subfamily.
Contains 3 A.T hook DNA-binding domains.
Contains 1 bromo domain.
Contains 1 CXXC-type zinc finger.
Contains 1 FY-rich C-terminal domain.
Contains 1 FY-rich N-terminal domain.
Contains 3 PHD-type zinc fingers.
Contains 1 post-SET domain.
Contains 1 SET domain.
Domainthe 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity.
The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides.
modificationsProteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site.
Cellular localizationNucleus and Nucleus. Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab268799 has not yet been referenced specifically in any publications.