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Rapidly accelerated fibrosarcoma (Raf) kinase is a serine/threonine kinase and component of the MAPK/ERK signaling pathway.1,2 Upon activation by upstream RAS signaling, Raf dimerizes and phosphorylates MEK1 leading to activation of transcription factors for cell growth, proliferation, and survival.2 Raf exists as three isoforms, A-RAF, B-RAF, and C-RAF, that all consist of three conserved regions (CRs) with domain-specific functions.1 CR1 contains a cysteine-rich domain and a RAS-binding domain, CR2 is essential for negative regulation through inhibition of phosphorylation sites, and CR3 is the kinase domain. B-RAF is the most prominent isoform, expressed in most tissues, and localized to the cytosol. Activating mutations in B-RAF have been found in various cancers, including melanoma and non-small cell lung cancer (NSCLC), as well as in patients with Langerhans cell histiocytosis.1,2,3 Cayman’s B-RAF Rabbit Monoclonal Antibody (Clone RM308) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Systemic review on B-
2. A BRAF new world. Crit. Rev. Oncol. Hematol. 152, 103008 (2020).
3. B-