Overview
- Peptide (C)HTFQGKEWDPKKHVQE, corresponding to amino acid residues 105-120 of mouse TRPM2 (Accession Q91YD4). Intracellular, N-terminus.
- Rat lung frozen section (1:50).
Expression of TRPM2 in rat lungImmunohistochemical staining of rat lung frozen sections using Anti-TRPM2-ATTO Fluor-594 Antibody (#ACC-043-AR), (1:50). A. TRPM2 staining is specific for respiratory epithelium in the bronchi. B. Merged with bright field.
The mammalian melastatin-related transient receptor potential (TRPM) is a subfamily of the TRP family. The family was named after the first discovered member, melastatin (TRPM1) whose gene was identified in metastatic and benign melanomas1-3.
The TRPM family consists of eight members designated as TRPM1-8 that can be further divided into four pairs: TRPM1 and TRPM3; TRPM2 and TRPM8; TRPM4 and TRPM5; and TRPM6 and TRPM71,2.
The TRPM proteins share structural homology with other members of the TRP superfamily channels; six putative transmembrane domains, and cytoplasmic N- and C-termini. However, due to their long N- and C-termini they are also named the long TRP channel family1-3.
The C-terminal regions of three TRPM members (TRPM2, TRPM6 and TRPM7) are occupied by enzymatic domains. Almost all the C-terminal region of TRPM2 has an enzymatic domain with sequence similarities to Nudix hydrolases (cleave mononucleotide and dinucleotide polyphosphates2,4.
TRPM2 is a Ca2+-permeable, nonselective cation channel that is predominantly expressed in various regions of the brain, where it is preferentially localized in microglial cells, the host macrophages of the central nervous system and is also expressed in other tissues, including spleen, heart, liver, lung, and bone marrow. Several splice variants of TRPM2 have been identified5,3.
