重组人TRPM7蛋白
Recombinant Human TRPM7 protein
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Recombinant Human TRPM7 protein is a Human Fragment protein, in the 777 to 855 aa range, expressed in Wheat germ, suitable for ELISA, WB.
查看别名
CHAK1, LTRPC7, TRPM7, Transient receptor potential cation channel subfamily M member 7, Channel-kinase 1, Long transient receptor potential channel 7, LTrpC-7, LTrpC7
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TRPM7 protein (AB153385)
ab153385 on a 12.5% SDS-PAGE stained with Coomassie Blue.
反应性数据
序列信息
性能和储存信息
运输条件
推荐的短期储存条件
推荐的长期储存条件
分装信息
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
TRPM7 regulates cellular magnesium homeostasis and calcium influx in many cell types. It is integral in maintaining the cell's ion balance and influences various cellular functions like growth proliferation and apoptosis. TRPM7 is often part of larger molecular complexes that enable it to interact with other proteins and lipids modulating signal transduction pathways. It participates in mechanosensory functions as well impacting cellular responses to mechanical stimuli.
Pathways
TRPM7 is significant in the MAPK and PI3K/Akt pathways which are pivotal for cell survival and proliferation. Through these pathways TRPM7 interacts with other proteins such as TRPM6 and TRPV4. It modulates intracellular signaling cascades by regulating ion concentrations that affect protein interactions and enzyme activities thereby controlling critical cellular responses like inflammation and differentiation.
特殊说明
形式
Liquid
常规信息
功能
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 (PubMed : 11385574, PubMed : 12887921, PubMed : 15485879, PubMed : 24316671, PubMed : 35561741, PubMed : 36027648). 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 (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed : 18365021). 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 (PubMed : 15485879, PubMed : 18394644).. 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.
序列相似性
In the C-terminal section; belongs to the protein kinase superfamily. Alpha-type protein kinase family. ALPK subfamily.. In the N-terminal section; belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM7 sub-subfamily.
翻译后修饰
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.
靶点信息
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