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Mouse Monoclonal MLL antibody [10F8D7] (STJ98246)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:200-1:1000; ELISA 1:10000
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
KMT2A antibody, ALL1 antibody, CXXC7 antibody, HRX antibody, HTRX antibody, MLL antibody, MLL1 antibody, TRX1 antibody,|ALL-1 antibody|ALL1 antibody|C-terminal cleavage product of 180 kDa antibody|CXXC-type zinc finger protein 7 antibody|CXXC7 antibody|HRX antibody|HTRX1 antibody|KMT2A antibody|Lysine N-methyltransferase 2A antibody|Mll antibody|MLL cleavage product C180 antibody|MLL1 antibody|MLL1_HUMAN antibody|MLL1A antibody|N-terminal cleavage product of 320 kDa antibody|p180 antibody|p320 antibody|Trithorax-like protein antibody|TRX1 antibody|Zinc finger protein HRX antibody|Anti-KMT2A / MLL antibody [mmN4.4] (ab32400)
SCBT cat No: sc-101431|sc-18214|sc-377274|sc-30729|sc-374392|sc-20153|sc-53371|sc-30730|
MLL Monoclonal Antibody
|Catalogue No.|| |
MLL Monoclonal Antibody detects endogenous levels of MLL protein.
Purified recombinant fragment of MLL (aa3751-3968) expressed in E Coli
WB, IHC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:200-1:1000; ELISA 1:10000
MLL Antibody was tube-contained. Ascitic fluid containing 0.03% sodium azide.
MLL Antibody was purified using affinity purification.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Histone-lysine N-methyltransferase 2A antibody, Lysine N-methyltransferase 2A antibody, ALL-1 antibody, CXXC-type zinc finger protein 7 antibody, Myeloid/lymphoid or mixed-lineage leukemia antibody, Myeloid/lymphoid or mixed-lineage leukemia protein 1 antibody, Trithorax-like protein antibody, Zinc finger protein HRX antibody
|Protein names|| |
Histone-lysine N-methyltransferase 2A , Lysine N-methyltransferase 2A , ALL-1 , CXXC-type zinc finger protein 7 , Myeloid/lymphoid or mixed-lineage leukemia , Myeloid/lymphoid or mixed-lineage leukemia protein 1 , Trithorax-like protein , Zinc finger protein HRX
|Protein function|| |
Histone 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. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of ‘Lys-4’ of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (By similarity). / S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
|Protein tissue specificity|| |
Heart, lung, brain and T- and B-lymphocytes.
|Involvement in disease|| |
Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures. . Note: The disease is caused by mutations affecting the gene represented in this entry.; Note: Chromosomal aberrations involving KMT2A 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 KMT2A-MLLT1, KMT2A-MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. .; Note: A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. .
|Protein sequence and domain|| |
The 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. / Belongs to the class V-like SAM-binding methyltransferase superfamily. 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 FYR C-terminal domain. / Contains 1 FYR N-terminal domain. / Contains 3 PHD-type zinc fingers. / Contains 1 post-SET domain. / Contains 1 SET domain.
|Protein post-translational modifications|| |
Proteolytic 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.
|Protein cellular localization|| |
Nucleus / Nucleus / Nucleus
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St John’s Laboratory Ltd.
|Product type|| |
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