B-RAF^V600E Monoclonal Antibody (Clone RM8)

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. A single amino acid substitution of glutamic acid for valine at codon 600 in the kinase domain (B-RAF^V600E) is an activating mutation that is found in melanoma and non-small cell lung cancer (NSCLC), as well as breast, thyroid, colorectal, and ovarian cancers.^1,2 B-RAF^V600E is associated with early-stage ovarian cancer, as well as with increased risk of brain metastasis and shorter survival in melanoma.^1,3 Cayman’s B-RAF^V600E Monoclonal Antibody (Clone RM8) can be used for ELISA, immunocytochemistry (ICC), immunohistochemistry (IHC), and Western blot (WB) applications.

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1. Chavda, J., and Bhatt, H. Systemic review on B-RafV600E mutation as potential therapeutic target for the treatment of cancer. Eur. J. Med. Chem. 206, 112675 (2020).

2. Frisone, D., Friedlaender, A., Malapelle, U., et al. A BRAF new world. Crit. Rev. Oncol. Hematol. 152, 103008 (2020).

3. Patel, H., Yacoub, N., Mishra, R., et al. Current advances in the treatment of BRAF-mutant melanoma. Cancers (Basel) 12(2), 482 (2020).