|Application ||FC, IHC-P, E|
|Calculated MW||431764 Da|
|Antigen Region||3879-3908 aa|
|Other 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, MLL cleavage product N320, N-terminal cleavage product of 320 kDa, p320, MLL cleavage product C180, C-terminal cleavage product of 180 kDa, p180, KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1|
|Target/Specificity||This HRX antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 3879-3908 amino acids from the C-terminal region of human HRX.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HRX Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1|
|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).|
|Cellular Location||Nucleus. MLL cleavage product C180: Nucleus. Note=Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320|
|Tissue Location||Heart, lung, brain and T- and B-lymphocytes.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
The gene variously symbolized ALL1, HRX, or MLL located on 11q23 has been demonstrated to be fused with a number of translocation partners in cases of leukemia. Tse et al. (1995) characterized 2 t(1;11)(q21;q23) translocations that fused the MLL gene to a gene on chromosomal band 1q21, AF1Q, in 2 infants with acute myelomonocytic leukemia. In one of these patients, the derivative chromosome 11 represented an in-frame fusion of the N-terminal portion of the MLL gene to the complete AF1Q open reading frame, whereas the derivative chromosome 1 did not give rise to an open reading frame. This observation suggested that the N-terminal portion of the MLL gene is critical for leukemogenesis in translocations involving band 11q23.
Megonigal, M.D., et al., Proc. Natl. Acad. Sci. U.S.A. 97(6):2814-2819 (2000).
Pegram, L.D., et al., Blood 96(13):4360-4362 (2000).
Sano, K., et al., Blood 95(3):1066-1068 (2000).
Cui, X., et al., Nat. Genet. 18(4):331-337 (1998).
Nilson, I., et al., Br. J. Haematol. 93(4):966-972 (1996).
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