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AB153385

Recombinant Human TRPM7 protein (GST tag N-Terminus)

Recombinant Human TRPM7 protein (GST tag N-Terminus)

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Recombinant Human TRPM7 protein (GST tag N-Terminus) is a Human Fragment protein, in the 777 to 855 aa range, expressed in Wheat germ, suitable for ELISA, WB.

別名を表示する

CHAK1, LTRPC7, TRPM7, Transient receptor potential cation channel subfamily M member 7, Channel-kinase 1, Long transient receptor potential channel 7, LTrpC-7, LTrpC7

1 Images
SDS-PAGE - Recombinant Human TRPM7 protein (GST tag N-Terminus) (AB153385)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human TRPM7 protein (GST tag N-Terminus) (AB153385)

ab153385 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

発現系

Wheat germ

タグ

GST tag N-Terminus

アプリケーション

WB, ELISA

applications

生物活性

No

アクセッション番号

Q96QT4

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

配列情報

[{"sequence":"KTKAEMSHIPQSQDAHQMTMDDSENNFQNITEEIPMEVFKEVRILDSNEGKNEMEIQMKSKKLPITRKFYAFYHAPIVK","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":855,"aminoAcidStart":777,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q96QT4","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

TRPM7 also known as transient receptor potential melastatin 7 is an ion channel and a kinase with dual functionality. This protein has a mass of about 190 kDa and is widely expressed in a variety of tissues including brain heart kidney and lung. Mechanically TRPM7 serves as a channel for divalent cations primarily allowing the movement of magnesium (Mg²⁺) and calcium (Ca²⁺) ions across cellular membranes. Its kinase domain plays a role in autophosphorylation and substrate phosphorylation further influencing cellular processes.
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.

TRPM7 is linked to cancer and neurodegenerative diseases. In cancers altered TRPM7 expression promotes tumor growth and metastasis potentially interacting with proteins like Akt. In neurodegenerative conditions such as Alzheimer's disease abnormal TRPM7 function or expression contributes to neuronal death and is associated with other proteins like amyloid-beta and tau making TRPM7 a potential therapeutic target for modulation.

製品の性状

製品の状態

Liquid

一般的な情報

機能

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.

配列の類似性

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.

翻訳後修飾

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.

製品プロトコール

ターゲットの情報

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.
See full target information TRPM7

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