Recombinant Human Transient receptor potential cation channel subfamily M member 4 (TRPM4), partial

Code CSB-YP819465HU
MSDS
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Source Yeast
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Code CSB-EP819465HU
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Source E.coli
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Code CSB-EP819465HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP819465HU
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Source Baculovirus
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Code CSB-MP819465HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
TRPM4
Uniprot No.
Alternative Names
1110030C19Rik; AW047689; Calcium-activated non-selective cation channel 1; FLJ20041; hTRPM4; Long transient receptor potential channel 4; LTrpC-4; LTrpC4; Melastatin 4; Melastatin like 2 protein; Melastatin-4; Melastatin-like 2; Mls2s; PFHB1B; Transient receptor potential cation channel subfamily M member 4; Transient receptor potential cation channel, subfamily M, member 4; Trpm4; TRPM4_HUMAN; TRPM4B
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. Plays a role in keratinocyte differentiation.
Gene References into Functions
  1. Data suggest that TRPM4 exhibits binding sites for calmodulin (CaM) and S100 calcium-binding protein A1 (S100A1) located in very distal part of TRPM4 N-terminus. PMID: 29240297
  2. Here, we report the functional effects of previously uncharacterized variants of uncertain significance (VUS) that we have found while performing a "genetic autopsy" in individuals who have suffered sudden unexpected death. We have identified thirteen uncommon missense VUS in TRPM4 by testing 95 targeted genes implicated in channelopathy and cardiomyopathy in 330 cases PMID: 30391667
  3. We identified a double heterozygosity for pathogenic mutations in SCN5A and TRPM4 in a Brugada syndrome patient. PMID: 28494446
  4. The electron cryomicroscopy structure of human transient receptor potential melastatin subfamily member 4 (TRPM4) in a closed, Na(+)-bound, apo state at pH 7.5 to an overall resolution of 3.7 A is reported. PMID: 29463718
  5. electron cryo-microscopy structure of the most widespread CAN channel, human TRPM4, bound to the agonist Ca(2+) and the modulator decavanadate PMID: 29211723
  6. TRPM4 protein expression is up-regulated in diffuse large B cell lymphoma PMID: 28248435
  7. study presents 2 structures of TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo-electron microscopy; these structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain PMID: 29217581
  8. The loss-of-function variants A432T/G582S found in 2 unrelated patients with atrioventricular block are most likely caused by misfolding-dependent altered trafficking. PMID: 27207958
  9. Study supports the view that TRPM4 variants could be responsible for about 2% of LQT syndrome cases. The impact of these variants results in electrophysical disturbances. PMID: 28315637
  10. A large pedigree diagnosed with progressive familial heart block type I was linked to a mutation of the TRPM4 ion channel. PMID: 26820365
  11. Identify TRPM4 as a regulator of store operated calcium entry in prostate tumor cells, and demonstrate a role for TRPM4 in cancer cell migration. PMID: 26496025
  12. TRPM4 channels regulate human detrusor smooth muscle excitability and contractility and are critical determinants of human urinary bladder function PMID: 26791488
  13. TRPM4 protein expression is widely expressed in benign and cancerous prostate tissue PMID: 26590985
  14. new insight into the ligand binding domains of the TRPM4 channel PMID: 26071843
  15. Casein kinase 1 phosphorylates S839 and is responsible for the basolateral localization of TRPM4. PMID: 25231975
  16. TRPM4 acts to maintain endothelial features and its loss promotes fibrotic conversion via TGF-beta production. PMID: 25909699
  17. we demonstrate that the inhibition of TRPM4 activity alters cellular contractility in vivo, affecting cutaneous wound healing. PMID: 26110647
  18. The PKC-dependent effect of GLP-1 on membrane potential and electrical activity was mediated by activation of Na(+)-permeable TRPM4 and TRPM5 channels by mobilization of intracellular Ca(2+) from thapsigargin-sensitive Ca(2+) stores PMID: 26571400
  19. TRPM4 protein is a ROS-modulated non-selective cationic channel that performs several cell functions, including regulating intracellular Ca(2+) overload and Ca(2+) oscillation PMID: 24518820
  20. these data suggest an important role for the Sur1-Trpm4 channel in the pathophysiology of postischemic cell death PMID: 26172285
  21. These results showed that the cell surface expression of TRPM4 channels is mediated by 14-3-3gamma binding. PMID: 25047048
  22. Contraction of cerebral artery smooth muscle cells requires the integration of pressure-sensing signaling pathways and depolarization through the activation of TRPM4. PMID: 24866019
  23. TRPM4 is an important regulator of Ca2+ signals generated by histamine in hASCs and is required for adipogenesis. PMID: 25001294
  24. Used the Xenopus laevis oocyte expression system for expression, purification and extraction of functional human TRPM4 protein. Investigated the supra-molecular assembly of TRPM4. PMID: 24333049
  25. TRPM4 possesses the biophysical properties and upstream cellular signaling and regulatory pathways that establish it as a major physiological player in smooth muscle membrane depolarization. PMID: 23116477
  26. No role was found for TRPM4 in the peripheral blood compartment of multiple sclerosis patients. PMID: 23796873
  27. Because of its effect on the resting membrane potential, reduction or increase of TRPM4 channel function may both reduce the availability of sodium channel and thus lead to Brugada syndrome . PMID: 23382873
  28. TRPM4 cation channel mediates axonal and neuronal degeneration in experimental autoimmune encephalomyelitis and multiple sclerosis. PMID: 23160238
  29. In eight probands with atrioventricular block or right bundle branch block-five familial cases and three sporadic cases-a total of six novel and two published TRPM4 mutations were identified. PMID: 21887725
  30. Cys(1093) residue of TRPM4 is crucial for the H(2)O(2)-mediated loss of desensitization. PMID: 20884614
  31. These results identify TRPM4 as an important, unanticipated regulator of the beta-catenin pathway, where aberrant signaling is frequently associated with cancer. PMID: 20625999
  32. TRPM4 gene is a causative gene in isolated cardiac conduction disease with mutations resulting in a gain of function and TRPM4 channel being highly expressed in cardiac Purkinje fibers. PMID: 20562447
  33. Voltage dependence is not due to block by divalent cations or to voltage-dependent binding of intracellular Ca2+ to an activator site, indicating that TRPM4 is a transient receptor potential channel with an intrinsic voltage-sensing mechanism. PMID: 12799367
  34. TRPM4-mediated depolarization modulates Ca2+ oscillations, with downstream effects on cytokine production in T lymphocytes PMID: 15550671
  35. the Ca(2+) sensitivity of TRPM4 is regulated by ATP, PKC-dependent phosphorylation, and calmodulin binding at the C terminus. PMID: 15590641
  36. analysis of selectivity filter of the cation channel TRPM4 PMID: 15845551
  37. hydrolysis of PI(4,5)P(2) underlies desensitization of TRPM4, and PI(4,5)P(2) is a general regulator for the gating of TRPM ion channels PMID: 16186107
  38. PIP2 is a strong positive modulator of TRPM4 and implicate the C-terminal PH domain in PIP2 action. PMID: 16424899
  39. evidence indicates a role as a regulator of membrane potential, and thus the driving force for Ca2+ entry from the extracellular medium--{REVIEW} PMID: 17217063
  40. This study is believed to provide the first clear evidence that TRPM4b interacts physically with TRPC3. PMID: 18262493
  41. Depolarizing currents generated by TRPM4 are an important component in the control of intracellular Ca(2+) signals necessary for insulin secretion and perhaps glucagon from alpha-cells. PMID: 19063936
  42. In 3 branches of a large South African Afrikaner pedigree with an autosomal-dominant form of progressive familial heart block type I, identified the mutation c.19G-->A, which attenuated deSUMOylation of the TRPM4 channel. PMID: 19726882

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Involvement in disease
Progressive familial heart block 1B (PFHB1B)
Subcellular Location
[Isoform 1]: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum. Golgi apparatus.; [Isoform 2]: Cell membrane. Endoplasmic reticulum. Golgi apparatus.
Protein Families
Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM4 sub-subfamily
Tissue Specificity
Widely expressed with a high expression in intestine and prostate. In brain, it is both expressed in whole cerebral arteries and isolated vascular smooth muscle cells. Prominently expressed in Purkinje fibers. Expressed at higher levels in T-helper 2 (Th2
Database Links

HGNC: 17993

OMIM: 604559

KEGG: hsa:54795

STRING: 9606.ENSP00000252826

UniGene: Hs.467101

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