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Western blot analysis of FBP on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2). Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-FBP antibody.
Immunofluorescence staining of HCT-8 cells (Human colorectal adenocarcinoma; ATCC CCL-244).
BD Transduction Laboratories™ Purified Mouse Anti-FBP
BD Transduction Laboratories™ Purified Mouse Anti-FBP
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Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
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- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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Companion Products
The c-myc proto-oncogene is an essential participant in regulation of normal cell proliferation and programmed cell death. The far-upstream FUSE Binding Protein (FBP) is one of many factors that bind to a single strand of DNA in the 5' region of the c-myc gene. FBP, FBP2, and FBP3 comprise a family of single-strand DNA binding proteins that possess many features found in more conventional transcription factors. All FBP proteins bind specifically to a single strand of FUSE via a centrally located DNA binding domain and all contain a potent C-terminal transactivation domain. The transactivation domain of FBP contains three motif copies composed of tyrosine diads. However, a single tyrosine motif is sufficient to activate transcription. The N-terminal portion of FBP can repress the C-terminal transactivation potential. This repression is thought to be mediated by interactions between N- and C-terminal domains that produce an inactive conformation. Although FBP2 and FBP3 exhibit no specific pattern of expression, FBP expression mimics that of c-myc. These data implicate FBP as a transcription factor that is important for the regulation of cell growth and differentiation.
Development References (3)
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Davis-Smyth T, Duncan RC, Zheng T, Michelotti G, Levens D. The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators. J Biol Chem. 1996; 271(49):31679-31687. (Biology). View Reference
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Duncan R, Bazar L, Michelotti G. A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif. Genes Dev. 1994; 8(4):465-480. (Biology). View Reference
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Duncan R, Collins I, Tomonaga T, Zhang T, Levens D. A unique transactivation sequence motif is found in the carboxyl-terminal domain of the single-strand-binding protein FBP. Mol Cell Biol. 1996; 16(5):2274-2282. (Biology). View Reference
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