Recombinant Human RAF1 protein

RAF1 (also known as CRAF or c-Raf) is a serine/threonine-protein kinase that plays a pivotal role in the RAS-RAF-MEK-ERK signaling cascade, a critical pathway regulating cell proliferation, differentiation, survival, and apoptosis. As a member of the RAF kinase family, RAF1 is activated by RAS GTPases in response to extracellular stimuli, such as growth factors or cytokines. Upon activation, it phosphorylates and activates MEK1/2. which subsequently activates ERK1/2. leading to downstream transcriptional and metabolic responses. Dysregulation of this pathway, often due to mutations in RAF1 or related components, is implicated in numerous cancers and developmental disorders.

Recombinant RAF1 protein is engineered through molecular cloning and expression in heterologous systems (e.g., E. coli, insect, or mammalian cells) to produce functional, purified kinase for research and therapeutic applications. Its recombinant form retains key structural domains: three conserved regions (CR1-CR3), including a RAS-binding domain (CR1) and a kinase domain (CR3), essential for its activation and signaling functions. Researchers utilize recombinant RAF1 to study kinase activity, pathway interactions, and mutations (e.g., oncogenic variants like RAF1 S259L) linked to Noonan syndrome or cancers. It also serves as a tool for high-throughput drug screening to identify RAF inhibitors, with implications for targeting RAF-driven malignancies. Additionally, structural studies of recombinant RAF1 have advanced understanding of its regulation, including autoinhibition mechanisms and dimerization processes critical for pathway activation. Its role in resistance to BRAF inhibitors (e.g., in melanoma) further underscores its therapeutic relevance. Overall, recombinant RAF1 is a vital resource for dissecting RAF biology and developing precision oncology therapies.