Preparation And Storage
Recommended Assay Procedures
Applications include western blot analysis (0.25-1.0 µg/ml). WI-38 cells are suggested as a positive control. Other applications include gel shift (supershifts) and immunoprecipitation, which are not routinely tested by BD Biosciences Pharmingen. The antibody has been used to detect in vitro translated TFE3-L and TFE3-L, expressed as a recombinant protein in bacteria. In gel shift assays, using µE3 as a probe, this antibody supershifts the complex.
Product Notices
- 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.
TFE3 is a ubiquitously expressed 50 kDa transcription factor containing both basic helix-loop-helix (bHLH) and leucine zipper (ZIP) motifs. It was initially identified as a protein which bound to the µE3 site in the immunoglobulin heavy chain enhancer. In addition, it binds to the MLTF/USF site in the adenovirus major late promoter. Upon binding as a dimer, it induces a minor groove-oriented bend in the DNA, similar to other HLH proteins such as TFEB, USF, myc, and max. Binding results in transcriptional activation and is mediated through the basic region located just N-terminal to the HLH domain. Clone G138-312 recognizes TFE3. The antibody was raised against a bacterially expressed TFE3-L protein consisting of 327 amino acids encoded by nucleotides 361-2469 of the cloned cDNA.
Development References (5)
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Beckmann H, Su LK, Kadesch T. TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif. Genes Dev. 1990; 4(2):167-179. (Biology). View Reference
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Fisher DE, Parent LA, Sharp PA. Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove. Proc Natl Acad Sci U S A. 1992; 89(24):11779-11783. (Biology). View Reference
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Murre C, McCaw PS, Baltimore D. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell. 1989; 56(5):777-783. (Clone-specific: Activation). View Reference
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Roman C, Matera AG, Cooper C. mTFE3, an X-linked transcriptional activator containing basic helix-loop-helix and zipper domains, utilizes the zipper to stabilize both DNA binding and multimerization. Mol Cell Biol. 1992; 12(2):817-827. (Biology). View Reference
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Zhao GQ, Zhao Q, Zhou X, Mattei MG, de Crombrugghe B. TFEC, a basic helix-loop-helix protein, forms heterodimers with TFE3 and inhibits TFE3-dependent transcription activation. Mol Cell Biol. 1993; 13(8):4505-4512. (Clone-specific). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Refer to manufacturer's instructions for use and related User Manuals and Technical Data Sheets before using this product as described.
Comparisons, where applicable, are made against older BD technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
