Immunogen:synthetic peptide. The epitope recognized by A300-293A maps to a region between residues 400 and 450 of human fusion (involved in t(12,16) in malignant liposarcoma) using the numbering given in SwissProt entry P35637 (GeneID 2521).
Bemerkungen:FUS has been identified as a frequent translocation fusion partner of various transcription factors. FUS fusion genes have been shown to be associated with multiple tumor types which include liposarcoma, leukemia, histocytoma, and sarcoma. FUS is a multifunctional RNA-binding protein that associates with the nuclear matrix and Cajal bodies and appears to play a role in splicesome assembly, pre-mRNA splicing, DNA repair, transcriptional regulation and homologous recombination. Alternate names for FUS include RNA-binding protein FUS, oncogene FUS, oncogene TLS, translocated in liposarcomas, TLS, 75 kDa DNA-pairing protein, POMp75, CHOP, FUS-CHOP, TLS/CHOP, and hnRNP-P2.
Rabbit anti-FUS Antibody, Affinity Purified
Detection of Human FUS by Western Blot and Immunoprecipitation. Samples: Whole cell lysate from HeLa (15 and 50 µg for WB; 1 mg for IP, 20% of IP loaded), 293T (T; 50 µg) and Jurkat (J; 50 µg) cells. Antibodies: Affinity purified rabbit anti-FUS antibody A300-293A (lot A300-293A-2) used for WB at 0.1 µg/ml (A) and 1 µg/ml (B) and used for IP at 6 µg/mg lysate. FUS was also immunoprecipitated by a previous lot (lot A300-293A-1) of this antibody. Detection: Chemiluminescence with exposure times of 3 seconds (A) and 10 seconds (B).
This antibody is qualified for the Proximity Ligation Assay (PLA). PLA uses paired antibodies, so please refer to the PLA page of our website for specific imaging obtained by pairing this antibody with other qualified antibodies. The above image shows representative results for PLA using three color fluorescence, including DAPI stained nuclei (blue), phalloidin stained cytoplasmic F-actin (green), and PLA positive signal (red).
Detection of Human and Mouse FUS by Immunohistochemistry. Sample: FFPE section of human ovarian carcinoma (left) and mouse teratoma (right). Antibody: Affinity purified rabbit anti-FUS (Cat. No. A300-293A Lot2) used at a dilution of 1:5,000 (0.2and 1:1,000 (1 Detection: DAB
Detection of Mouse FUS by Western Blot. Samples: Whole cell lysate (50 µg) from TCMK-1, 4T1, and CT26.WT cells. Antibodies: Affinity purified rabbit anti-FUS antibody A300-293A (lot A300-293A-2) used for WB at 0.1 µg/ml. Detection: Chemiluminescence with an exposure time of 10 seconds.
Gene and Protein Information
Rat, Bovine, Dog, Rabbit, Pig, Orangutan, Rhesus Monkey, Gorilla, Chimpanzee, Northern white-cheeked gibbon, Gray short-tailed opossum, Duckbill platypus, Chinese hamster, Thirteen-lined ground squirrel, Little brown bat, African elephant, Tasmanian devil, White-tufted-ear marmoset less...
Ward CL et al., A loss of FUS/TLS function leads to impaired cellular proliferation. Cell Death Dis. 2014 Dec 11;5:e1572. ICC, IF
Dossi R et al., Antiangiogenic activity of trabectedin in myxoid liposarcoma: Involvement of host TIMP-1 and TIMP-2 and tumor thrombospondin-1. Int J Cancer. 2014 Jun 10. IP
Fujioka Y et al., FUS-regulated region- and cell-type-specific transcriptome is associated with cell selectivity in ALS/FTLD. Sci Rep. 2013 Aug 8;3:2388. WB, RIP
Sama RR et al., FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress. J Cell Physiol. 2013 Nov;228(11):2222-31. WB
Ishigaki S et al., Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions. Sci Rep. 2012;2:529. IHC-P
Aoki N et al., Localization of fused in sarcoma (FUS) protein to the post-synaptic density in the brain. Acta Neuropathol. 2012 Sep;124(3):383-94. WB, IHC-P
Necchi D et al., Dysfunction of the ubiquitin-proteasome system in the cerebellum of aging Ts65Dn mice. Exp Neurol. 2011 Dec;232(2):114-8. ICC
Bosco DA et al., Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet. 2010 Nov 1;19(21):4160-75. WB
Groen EJ et al., FUS mutations in familial amyotrophic lateral sclerosis in the Netherlands. Arch Neurol. 2010 Feb;67(2):224-30. IHC-P
Nash K et al., Identification of cellular proteins that interact with the adeno-associated virus rep protein. J Virol. 2009 Jan;83(1):454-69. ICC, IP
Goulet I et al., TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Hum Mol Genet. 2008 Oct 1;17(19):3055-74. WB, ICC
Hume DA et al., The Ewing sarcoma protein (EWS) binds directly to the proximal elements of the macrophage-specific promoter of the CSF-1 receptor (csf1r) gene. J Immunol. 2008 May 15;180(10):6733-42. ChIP