Recombinant Rabbit monoclonal primary
Recombinant FUS/TLS Monoclonal Antibody (ET1701-86)
SW480, MCF-7, Hela, K562, human kidney tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
75 kDa DNA pairing protein antibody; 75 kDa DNA-pairing protein antibody; ALS6 antibody; Amyotrophic lateral sclerosis 6 antibody; fus antibody; FUS CHOP antibody; Fus like protein antibody; FUS_HUMAN antibody; FUS1 antibody; Fused in sarcoma antibody; Fusion (involved in t(12; 16) in malignant liposarcoma) antibody; Fusion derived from t(12; 16) malignant liposarcoma antibody; Fusion gene in myxoid liposarcoma antibody; Heterogeneous nuclear ribonucleoprotein P2 antibody; hnRNP P2 antibody; hnRNPP2 antibody; Oncogene FUS antibody; Oncogene TLS antibody; POMp75 antibody; RNA binding protein FUS antibody; RNA-binding protein FUS antibody; TLS antibody; TLS CHOP antibody; Translocated in liposarcoma antibody; Translocated in liposarcoma protein antibody
Belongs to the RRM TET family.
Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine.; Phosphorylated in its N-terminal serine residues upon induced DNA damage. ATM and DNA-PK are able to phosphorylate FUS N-terminal region.
EWS and FUS/TLS are nuclear RNA-binding proteins. As a result of chromosome translocation, the EWS gene is fused to a variety of transcription factors, including ATF-1, in human neoplasias. In the Ewing family of tumors, the N-terminal domain of EWS is fused to the DNA-binding domain of various Ets transcription factors, including Fli-1, ETV1 and FEV. The EWS/Fli-1 chimeric protein acts as a more potent transcriptional activator than Fli-1 and can promote cell transformation. In human myxoid liposarcomas and myeloid leukemias, chromosomal translocation results in the fusion of the N-terminal region of FUS/TLS with the open reading frame of CHOP. In normal cells, FUS/TLS binds to the DNA-binding domains of nuclear steroid receptors and is also present in subpopulations of TFIID complexes, indicating a potential role for FUS/TLS in the processing of primary transcripts that are generated in response to hormone-induced transcription.