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Raf1 RBD Protein Human Recombinant |  Inhibitor screening for RAS-RAF interaction | Cancer Drug Discovery

Amid Biosciences | Protein Engineering Company

Raf1 RBD Protein, Human, Recombinant

$ 280.00

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.

  • 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. 

International Shipping:  Product requires shipping on ice packs. Please contact for shipment estimates

This product is for laboratory research use only.

For Bulk Orders or Custom Packaging, please contact:

de Rooij, J., Bos, J. Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene 14623–625 (1997).


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