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AB153385

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.

View Alternative Names

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 (AB153385)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human TRPM7 protein (AB153385)

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

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q96QT4

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

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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>" } } }
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Sequence info

[{"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"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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.
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Specifications

Form

Liquid

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General info

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 (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.

Sequence similarities

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.

Post-translational modifications

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.

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

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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Product promise

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For full details, please see our Terms & Conditions
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