Amid Biosciences | Protein Engineering Company
Raf1 RBD Protein, Human, Recombinant
Human Ras Binding Domain (RBD) of Raf-1 Proto-Oncogene, Serine/Threonine Kinase (RAF1), (UniProt # P04049, amino acids 1-149), expressed with an N-terminal 6XHis and glutathione S-transferase (GST) dual tag in E. coli. The dual 6xHis-GST tag allows immobilization of Raf1 RBD Protein and RBD-Ras complexes on either Ni-NTA or glutathione agarose resin columns.
The Raf1 RBD protein binds specifically to GTP-bound Ras proteins. Ras proteins, like other small GTPases, regulate molecular events by cycling between an inactive GDP-bound form and an active GTP-bound form. In its active (GTP-bound) state, Ras binds specifically to the Ras-binding domain (RBD) of Raf1 to control downstream signaling cascades. The affinity between RBD and GDP-bound Ras is three orders of magnitude lower (1). Therefore, the RBD protein can be used to specifically precipitate active, GTP-bound Ras as well as to specifically block the activity of Ras in vitro and in vivo.Applications
- Measurement of the GTP/GDP bound ratio of Ras in vitro.
- Quantitation of GTP-bound Ras from tissue and tissue culture cell lysates.
- RAS/RAF binding studies.
- Inhibitor screening for RAS/RAF interaction
MW: 45 kDa
Tag(s): The N-terminal 6XHis and GST dual affinity tag
Amino Acids: 1-149 of Raf1, UniProt # P04049
Catalog # RAF1-301
Storage buffer: 20 mM HEPES, pH 7.5, 100 mM NaCl, and 20% Glycerol.
Concentration: 1.0 mg/mL by A280
Purity: >80% by Coomassie staining
Storage is recommended at -20°C for longer periods of time.
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This product is for laboratory research use only.
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de Rooij, J., Bos, J. Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene 14, 623–625 (1997). https://doi.org/10.1038/sj.onc.1201005