Western blot image of human autophosphorylated TRPM7 C-terminal kinase domain (lanes 1-6). The blot was treated with lambda phosphatase to dephosphorylate TRPM7 phosphosites (lanes 2, 4, & 6). The blot was probed with rabbit polyclonals anti-TRPM7 (Ser-1513), phospho-specific (lanes 1 & 2), anti-TRPM7 (a.a.1484-1497), TP5691 antibody (lanes 3 & 4), or anti-TRPM7 (Ser-1493), phospho-specific (lanes 5 & 6).
Anti-TRPM7 (Ser-1493), Phosphospecific Antibody
Bulk Order Anti-TRPM7 (Ser-1493), 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.
Antigen Affinity Purified
Phospho-TRPM7 (Ser-1493) synthetic peptide (coupled to carrier) corresponding to amino acids surrounding Ser-1493 in human TRPM7. This site is conserved in rat and mouse TRPM7, but the homology surrounding the site is low. This site has no homology to other TRPM family members.
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
The antibody was cross-adsorbed to unphosphorylated TRPM7 (Ser-1493) then affinity purified using phospho-TRPM7 (Ser-1493) peptide. This antibody detects a 220 kDa* protein on SDS-PAGE immunoblots of human MDA-MB-231 cells stimulated with calyculin A, and detects a 70 kDa autophosphorylated recombinant kinase domain of human TRPM7. These reactivities are not observed after lambda phosphatase treatment to dephosphorylate TRPM7.
Western blots performed on each lot.
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.
After date of receipt, stable for at least 1 year at -20°C.