BRAP Protein, Human

BRAP protein acts as a negative regulator of MAP kinase activation, inhibits the formation of the Raf/MEK complex, and may inactivate the KSR1 scaffolding protein. As a Ras-responsive E3 ubiquitin ligase, BRAP undergoes autopolyubiquitination upon Ras activation, releasing its inhibitory effect on Raf/MEK complex formation. BRAP Protein, Human is the recombinant human-derived BRAP protein, expressed by E. coli , with tag free. The total length of BRAP Protein, Human is 591 a.a., .

BRAP protein functions as a negative regulator of MAP kinase activation, primarily by restricting the formation of Raf/MEK complexes, potentially through the inactivation of the KSR1 scaffold protein. Additionally, it operates as a Ras-responsive E3 ubiquitin ligase, which, upon Ras activation, undergoes auto-polyubiquitination, leading to the release of its inhibitory effect on Raf/MEK complex formation. Beyond its role in kinase signaling, BRAP may serve as a cytoplasmic retention protein, playing a part in the regulation of nuclear transport processes. This multifaceted functionality positions BRAP as a crucial player in modulating key cellular pathways and responses.

Human

E. coli

Tag Free

Q7Z569 (S2-K592)

8315

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.