Anti-LMO2 (Rhombotin-2) Antibody, clone 299B clone 299B, from mouse

Rhombotin-2 (UniProt: P25791; also known as Cysteine-rich protein TTG-2, LIM domain only protein 2, LMO-2, T-cell translocation protein 2) is encoded by the LMO2 (also known as RBTN2, RBTNL1, RHOM2, TTG2) gene (Gene ID: 4005) in human. Rhombotin-2 is 158 amino acids, small cysteine-rich protein with multiple functions. A large portion of its structure is occupied by tandemly repeated cysteine-rich zinc-finger binding motifs, the LIM domains. However, it does not have any identifiable DNA-binding motifs. It is found predominantly in the nucleus or in the cytoplasm depending upon the tissue and the cell type. In kidney it is predominantly localized in the cytoplasm, but in hematopoietic cells it has nuclear localization. LMO2 is reported to be a proto-oncogene only in the context of T lymphocytes and is reported to play a role in T-cell leukemogenesis. It also has distinct functions in erythropoiesis. It acts with TAL1/SCL to regulate red blood cell development and interacts with LDB1 to maintain erythroid precursors in an immature state. It is reported to interact with retinoblastoma-binding protein 2 (RBP2) and human brain expressed X-linked (Bex2), both of which are shown to enhance its transcriptional activity. A chromosomal aberration involving LMO2 has been linked to T-cell acute lymphoblastic leukemia (T-ALL). (Ref.: Mao S., et al. (1997) Oncogene 14, 1531-1539).