Anti-MSL-2 Antibody, clone 10C3.1 clone 10C3.1, from mouse

E3 ubiquitin-protein ligase MSL2 (UniProt Q9HCI7; also known as Male-specific lethal-2 homolog, Male-specific lethal-2 homolog 1, Male-specific lethal 2-like 1, MSL-2, MSL2-like 1, RING finger protein 184) is encoded by the MSL2 (also known as KIAA1585, MSL2L1, RNF184) gene (Gene ID 55167) in human. MSL2 (male-specific lethal 2) was originally identified in Drosophila and characterized as a gene whose mution causes male-specific lethality. Human MSL (hMSL) orthologues are found in an evolutionary conserved complex known as the hMOF (Males absent on the first, human) complex that is composed of hMOF, hMSL1, hMSL2, hMSL3, and Nucleoprotein 153 (NUP153). MSL2 is a RING domain-containing E3 ligase that targets the tumor suppressor p53 Lys351 for monoubiquitination, exposing a nuclear export motif within p53 as well as releasing p53 from MDM2. MSL2 overexpression causes an upregulation of mitochondrial-dependent apoptosis as a result of p53 cytoplasmic accumulation. hMSL1/hMSL2 heterodimer is reported to ubiquitinate histone H2B on Lys34 (H2BK34ub), which promotes transcription activation by stimulating the activities of MLL/SET1 family H3K4 methyltransferases and the H3K79 methyltransferase DOT1L. In addition, both hMSL1 and hMOF are reported to be modified by hMSL2 following DNA damage induction, and hMSL2-depletion causes impaired non-homologous end joining (NHEJ) repair in human cells.