Raf1 RBD Protein, Human, Recombinant, Biotinylated

Ras Binding Domain (RBD) of Human Raf-1 Proto-Oncogene, Serine/Threonine Kinase (RAF1), (UniProt # P04049, amino acids 50-140) with the N-terminal AviTag™ peptide and His-tag is produced in E. coli cells and site-specifically biotinylated at AviTag with BirA enzyme.

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.

Catalog # RAF1-B-301

This product is for laboratory research use only.