This TRPM7 Sandwich ELISA Kit, Ready-To-Use is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in human tissue homogenates or other biological fluids..
Applications
ELISA
Reactivity
Human
Sensitivity
33pg/mL
Detection Limit
78.1-5000pg/mL
Note
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Product Properties
Storage Instruction
The whole kit may be stored at-20°C for up to 12 months from receipt. An unopened kit may be stored in the fridge at 2-8°C for up to 6 months. Once opened store individual kit contents according to components table provided with the kit.
Palmitoylated.palmitoylation at Cys-1143, Cys-1144 and Cys-1146 promotes TRPM7 trafficking from the Golgi to the surface membrane. Autophosphorylated.autophosphorylation of C-terminus regulates TRPM7 kinase activity towards its substrates. The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. TRPM7 is cleaved by caspase-8, dissociating the kinase from the ion-conducting pore. The cleaved kinase fragments (M7CKs) can translocate to the cell nucleus and binds chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones.
Function
Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx. Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation. The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7. In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions. TRPM7 channel, cleaved form: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. TRPM7 kinase, cleaved form: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development.
Protein Name
Transient Receptor Potential Cation Channel Subfamily M Member 7Channel-Kinase 1Long Transient Receptor Potential Channel 7Ltrpc-7Ltrpc7 Cleaved Into - Trpm7 Kinase - Cleaved FormM7ck - Trpm7 Channel - Cleaved Form
