Anti-Acetyl MLL1 (KMT2A) (Lys 1130/1133) from rabbit

Histone-lysine N-methyltransferase 2A (UniProt: Q03164; also known as EC: 2.1.1.43, 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, MLL1, Trithorax-like protein, Zinc finger protein HRX) is encoded by the KMT2A (also known as ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1) gene (Gene ID: 4297) in human. It is expressed in heart, lung, and brain and in T- and B-lymphocytes and plays an essential role in early development and hematopoiesis. Proteolytic cleavage of MLL1 by Taspase 1 (TASP1) generates an N-terminal cleavage product of 320 kDa and a C-terminal product of 180 kDa. The catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of Lysine 4 of histone H3 (H3K4me) complex and acetylation of Lysine 16 of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. MLL1 displays weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. It does not exhibit any activity toward histone H3 phosphorylated on Threonine 3, and less activity toward H3 dimethylated on Arginine 8 or Lysine 9. However, it has higher activity toward H3 acetylated on Lysine 9. MLL1 is shown to be required for transcriptional activation of HOXA9 and it promotes PPP1R15A-induced apoptosis. MLL1 is reported to coordinate recruitment of CLOCK BMAL1 activator complexes to chromatin, an event associated with cyclic trimethylation of histone H3 Lysine 4 (H3K4) at circadian promoters. MLL1 is also reported to play a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. (Ref.: Aguilar-Arnal, L., et al. (2015). Nat. Struct. Mol. Biol. 22(4); 312-318).