h. sapiens (hs) m. musculus trpm4 genes coding full-length trpm4 Search Results


trpm4 genes  (GenScript corporation)
90
GenScript corporation trpm4 genes
a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of <t>TRPM4</t> are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.
Trpm4 Genes, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h%2E+sapiens+(hs)+m%2E+musculus+trpm4+genes+coding+full-length+trpm4/chicken+anti+trpm4+antiserum/pmc11743598-240-10-43
Average 90 stars, based on 1 article reviews
trpm4 genes - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
plasmid constructs design and cloning  (GenScript corporation)
90
GenScript corporation plasmid constructs design and cloning
a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of <t>TRPM4</t> are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.
Plasmid Constructs Design And Cloning, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h%2E+sapiens+(hs)+m%2E+musculus+trpm4+genes+coding+full-length+trpm4/plasmid+constructs+design+and+cloning/pm39828793-201-4-48
Average 90 stars, based on 1 article reviews
plasmid constructs design and cloning - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
pcdna-3.1 plasmid  (GenScript corporation)
90
GenScript corporation pcdna-3.1 plasmid
a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of <t>TRPM4</t> are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.
Pcdna 3.1 Plasmid, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h%2E+sapiens+(hs)+m%2E+musculus+trpm4+genes+coding+full-length+trpm4/pcdna3+1/pmc11743598-240-31-43
Average 90 stars, based on 1 article reviews
pcdna-3.1 plasmid - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
mouse monoclonal antibody against trpm4  (Novus Biologicals)
92
Novus Biologicals mouse monoclonal antibody against trpm4
a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of <t>TRPM4</t> are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.
Mouse Monoclonal Antibody Against Trpm4, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h%2E+sapiens+(hs)+m%2E+musculus+trpm4+genes+coding+full-length+trpm4/TRPM4+Antibody+(OTI10H5)/10__5137_slash_1019___5149__jtn__36251___21__4-73-21-26
Average 92 stars, based on 1 article reviews
mouse monoclonal antibody against trpm4 - by Bioz Stars, 2026-11
92/100 stars
  Buy from Supplier

Image Search Results


a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of TRPM4 are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.

Journal: Nature Communications

Article Title: Identification of a binding site for small molecule inhibitors targeting human TRPM4

doi: 10.1038/s41467-025-56131-2

Figure Lengend Snippet: a , b Two views of the cryo-EM densities of HsTRPM4apo in surface representation. Alternating protomers of TRPM4 are shown in blue and white. The TRPM homology regions (MHR3/4) are indicated. c , d Cartoon representation of the HsTRPM4apo corresponding to the cryo-EM densities in ( a , b ). The positions of bound cholesterol molecules (CHR) are indicated. The black box indicates the positions of CHR-1 and CHR-3, as shown in yellow. In contrast, the pink box indicates the position of CHR-2. e Cryo-EM density in mesh representation for CHR-2 ( f ) Cryo-EM density in mesh representation for CHR-1. In e and f, the density threshold level is indicated by σ.

Article Snippet: For this study, the wild-type codon-optimized H. sapiens (Hs) and M. musculus (Mm) TRPM4 genes coding full-length TRPM4 were synthesized, fused to consecutive C-terminal HA (hemagglutinin)—and FLAG-tags, and cloned into a pCDNA-3.1 plasmid for expression in HEK293 cells by the CMV (cytomegalovirus) promoter (GenScript Biotech).

Techniques: Cryo-EM Sample Prep

a Amino acid residues of HsTRPM4 involved in interactions with the anthranilic acid moiety of NBA (in purple) and ( b ) IBA (cyan) are shown. c Amino acid residues of HsTRPM4 involved in hydrophobic interactions with NBA (in purple) and ( d ) IBA (in cyan) are shown. e Graphical plot of normalized recorded sodium current of the calcium-activated HsTRPM4 channel for the wildtype (WT) and HsTRPM4 variants. Data are presented as mean values +/− SEM. (*) represents the p -value < 0.05 compared to the wildtype condition. The number of cells per condition recorded is: Empty ( n = 6), HsTRPM4 WT ( n = 15), HsTRPM4 S863A ( n = 6), HsTRPM4 V901W ( n = 6), HsTRPM4 V904W ( n = 7), HsTRPM4 H908A (n = 7), HsTRPM4 S924A ( n = 11), HsTRPM4 K925A ( n = 7), HsTRPM4 Y1057A ( n = 7), HsTRPM4 Q1061A ( n = 6), HsTRPM4 R1064A ( n = 7), HsTRPM4 R1064G ( n = 6), HsTRPM4 R1064S ( n = 7), and HsTRPM4 S863A/S924A ( n = 6). The Mann-Whitney test, which is two-tailed, has been used to compare Hs TRPM4 to another condition, and multiple comparisons have been performed. The p -values are: HsTRPM4 WT versus Empty ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 S863A ( p = 0.9852), HsTRPM4 WT versus HsTRPM4 V901W ( p = 0.0057), HsTRPM4 WT versus HsTRPM4 V904W (( p < 0.0001), HsTRPM4 WT versus HsTRPM4 H908A ( p = 0.02), HsTRPM4 WT versus HsTRPM4 S924A ( p = 0.4495), HsTRPM4 WT versus HsTRPM4 K925A ( p = 0.0022), HsTRPM4 WT versus HsTRPM4 Y1057A ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 Q1061A ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 R1064A ( p = 0.0528), HsTRPM4 WT versus HsTRPM4 R1064G ( p = 0.6085), HsTRPM4 WT versus HsTRPM4 R1064S ( p < 0.0001), and HsTRPM4 WT versus HsTRPM4 S863A/S924A ( p = 0.0133). f , g Representative traces of wildtype (WT) and variants sodium currents of the calcium-activated HsTRPM4 channels: S924A and Q1061A. Sodium currents of the calcium-activated HsTRPM4 variant channels are generally smaller than WT currents, as depicted in ( e ), due to the amino acid alteration.

Journal: Nature Communications

Article Title: Identification of a binding site for small molecule inhibitors targeting human TRPM4

doi: 10.1038/s41467-025-56131-2

Figure Lengend Snippet: a Amino acid residues of HsTRPM4 involved in interactions with the anthranilic acid moiety of NBA (in purple) and ( b ) IBA (cyan) are shown. c Amino acid residues of HsTRPM4 involved in hydrophobic interactions with NBA (in purple) and ( d ) IBA (in cyan) are shown. e Graphical plot of normalized recorded sodium current of the calcium-activated HsTRPM4 channel for the wildtype (WT) and HsTRPM4 variants. Data are presented as mean values +/− SEM. (*) represents the p -value < 0.05 compared to the wildtype condition. The number of cells per condition recorded is: Empty ( n = 6), HsTRPM4 WT ( n = 15), HsTRPM4 S863A ( n = 6), HsTRPM4 V901W ( n = 6), HsTRPM4 V904W ( n = 7), HsTRPM4 H908A (n = 7), HsTRPM4 S924A ( n = 11), HsTRPM4 K925A ( n = 7), HsTRPM4 Y1057A ( n = 7), HsTRPM4 Q1061A ( n = 6), HsTRPM4 R1064A ( n = 7), HsTRPM4 R1064G ( n = 6), HsTRPM4 R1064S ( n = 7), and HsTRPM4 S863A/S924A ( n = 6). The Mann-Whitney test, which is two-tailed, has been used to compare Hs TRPM4 to another condition, and multiple comparisons have been performed. The p -values are: HsTRPM4 WT versus Empty ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 S863A ( p = 0.9852), HsTRPM4 WT versus HsTRPM4 V901W ( p = 0.0057), HsTRPM4 WT versus HsTRPM4 V904W (( p < 0.0001), HsTRPM4 WT versus HsTRPM4 H908A ( p = 0.02), HsTRPM4 WT versus HsTRPM4 S924A ( p = 0.4495), HsTRPM4 WT versus HsTRPM4 K925A ( p = 0.0022), HsTRPM4 WT versus HsTRPM4 Y1057A ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 Q1061A ( p < 0.0001), HsTRPM4 WT versus HsTRPM4 R1064A ( p = 0.0528), HsTRPM4 WT versus HsTRPM4 R1064G ( p = 0.6085), HsTRPM4 WT versus HsTRPM4 R1064S ( p < 0.0001), and HsTRPM4 WT versus HsTRPM4 S863A/S924A ( p = 0.0133). f , g Representative traces of wildtype (WT) and variants sodium currents of the calcium-activated HsTRPM4 channels: S924A and Q1061A. Sodium currents of the calcium-activated HsTRPM4 variant channels are generally smaller than WT currents, as depicted in ( e ), due to the amino acid alteration.

Article Snippet: For this study, the wild-type codon-optimized H. sapiens (Hs) and M. musculus (Mm) TRPM4 genes coding full-length TRPM4 were synthesized, fused to consecutive C-terminal HA (hemagglutinin)—and FLAG-tags, and cloned into a pCDNA-3.1 plasmid for expression in HEK293 cells by the CMV (cytomegalovirus) promoter (GenScript Biotech).

Techniques: MANN-WHITNEY, Two Tailed Test, Variant Assay

a , b NBA dose-response curves of wildtype (WT) and variants of the predicted binding pocket of the HsTRPM4 channel, as a function of the decadic logarithm of the NBA concentration. Data are presented as mean values +/− SEM. (n): number of cells. c Locations of S863 and S924 in the drug binding pocket ( d , e ) Representative traces of wildtype (WT) and variant HsTRPM4 sodium currents: S863A/S924A in the absence of calcium (dotted black line), in the presence of a solution with a concentration of 300 µM of free calcium (grey line) and in the presence of a solution with a concentration of 300 µM of free calcium and 1 µM of NBA (black line). f Representation of the T677I variant located outside of the drug binding pocket of the TRPM4 channel. g NBA dose-response curves of wildtype (WT) and a T677I variant. (n): number of cells.

Journal: Nature Communications

Article Title: Identification of a binding site for small molecule inhibitors targeting human TRPM4

doi: 10.1038/s41467-025-56131-2

Figure Lengend Snippet: a , b NBA dose-response curves of wildtype (WT) and variants of the predicted binding pocket of the HsTRPM4 channel, as a function of the decadic logarithm of the NBA concentration. Data are presented as mean values +/− SEM. (n): number of cells. c Locations of S863 and S924 in the drug binding pocket ( d , e ) Representative traces of wildtype (WT) and variant HsTRPM4 sodium currents: S863A/S924A in the absence of calcium (dotted black line), in the presence of a solution with a concentration of 300 µM of free calcium (grey line) and in the presence of a solution with a concentration of 300 µM of free calcium and 1 µM of NBA (black line). f Representation of the T677I variant located outside of the drug binding pocket of the TRPM4 channel. g NBA dose-response curves of wildtype (WT) and a T677I variant. (n): number of cells.

Article Snippet: For this study, the wild-type codon-optimized H. sapiens (Hs) and M. musculus (Mm) TRPM4 genes coding full-length TRPM4 were synthesized, fused to consecutive C-terminal HA (hemagglutinin)—and FLAG-tags, and cloned into a pCDNA-3.1 plasmid for expression in HEK293 cells by the CMV (cytomegalovirus) promoter (GenScript Biotech).

Techniques: Binding Assay, Concentration Assay, Variant Assay