- Peptide (C)KPPIKRQDGELVGYR, corresponding to amino acid residues 402 - 416 of mouse MERTK (Accession Q60805). Extracellular, N-terminus.
- Rat and mouse brain lysate; human HepG2 hepatocellular carcinoma cell line; mouse BV-2 microglia cell; human MEG-01 megakaryoblastic leukemia cell line (1:400-1:2000).
- Western blot analysis of rat brain lysate (lanes 1 and 3) and mouse brain lysate (lanes 2 and 4):1, 2. Anti-MERTK (extracellular) Antibody (#ATR-033), (1:400).
3, 4. Anti-MERTK (extracellular) Antibody, preincubated with MERTK (extracellular) Blocking Peptide (#BLP-TR033).
- Mouse and rat brain sections (1:300).
- Mouse BV-2 microglia cells (5 µg).
Myeloid-epithelial-reproductive tyrosine kinase, MERTK, is a receptor tyrosine kinase of the TAM (Tyro3, Axl and MERTK) family, expressed in numerous cancers1.
The extracellular N-terminal domain contains two immunoglobulin-like and two fibronectin 3 domains, followed by a hydrophobic single pass transmembrane domain, and a cytoplasmic C-terminal tail containing a tyrosine kinase domain1,2.
Auto-phosphorylation induced by ligand binding influences a range of downstream signaling pathways and cellular functions2. The physiological roles of MERTK include regulation of tissue homeostasis and repair, innate immune control, and platelet aggregation. However, aberrant expression of this protein promotes neoplasia, cell cycle progression, proliferation and tumor growth, resistance to apoptosis, and promotion of tumor metastases.
MERTK is involved in the activation of several canonic oncogenic signaling pathways in various types of cancers including: leukemia, non-small cell lung cancer, glioblastoma, melanoma, prostate cancer, breast cancer, colon cancer and gastric cancer1,3,4.
Due to its pivotal role in cancer development and metastasis, multiple therapeutic approaches are currently in development to inhibit MERTK, including ligand "traps" and small-molecule tyrosine kinase inhibitors4.