Anti-TRPM7 (Ser-1569), Phosphospecific Antibody

The transient receptor potential melastatin (TRPM) subfamily of cation-permeable TRP channels is ubiquitously expressed in mammalian tissues. This family includes TRPM1-8. In addition to acting as a calcium-permeant channel, TRPM6 and TRPM7 possess an inherent serine/threonine kinase activity. TRPM7 specifically is involved with cellular magnesium homeostasis and neurotransmitter release. Due to the magnesium inhibition, TRPM7’s ion channel activity is very low. TRPM7 has been implicated in cell proliferation and migration during cancer progression, and its expression levels correlate with prognosis in breast cancer. TRPM7 kinase activation leads to massive autophosphorylation of the C-terminal region, including phosphorylation of Ser-1493, Ser-1513, and Ser-1569. Both Ser-1513 and Ser-1569 phosphorylation is required for kinase activity, and phosphorylation of Ser-1513 may inhibit Caspase-mediated cleavage of the C-terminal tail. Thus, TRPM7 is a multifunctional transmembrane protein with roles in cell signaling, proliferation, migration, and death.

Our TRPM7 (Ser-1569) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat TRPM7 (Ser-1569) and is antigen affinity purified. It is great for use in WB.

Phospho-TRPM7 (Ser-1569) synthetic peptide (coupled to carrier) corresponding to amino acids surrounding Ser-1569 in human TRPM7. This site is well conserved in rat and mouse TRPM7, and is conserved in TRPM6 (Thr-1724) however the site is threonine instead of serine. This site has no homology to other TRPM family members.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody was cross-adsorbed to unphosphorylated TRPM7 (Ser-1569) then affinity purified using phospho-TRPM7 (Ser-1569) peptide. This antibody detects a 220 kDa* protein on SDS-PAGE immunoblots of human MDA-MB-231 stimulated with calyculin A and rat PC12 cells, as well as detects a 70 kDa autophosphorylated recombinant kinase domain of human TRPM7. These reactivities are not observed after lambda phosphatase treatment to dephosphorylate TRPM7.