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Bethyl 195a
195a, supplied by Bethyl, used in various techniques. Bioz Stars score: 90/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/195a/product/Bethyl
Average 90 stars, based on 33 article reviews

195a - by Bioz Stars, 2026-03

90/100 stars

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(A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and MCM5 (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.

Journal: bioRxiv

Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

doi: 10.1101/2025.05.31.656953

Figure Lengend Snippet: (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and MCM5 (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.

Article Snippet: The following antibodies against human proteins were used for immunoblotting and immunofluorescence: MCM2 (Bethyl Laboratories; A300-191A), MCM3 (Bethyl Laboratories; A300-192A), MCM3 (Santa Cruz; sc-390480), MCM5 (Bethyl Laboratories; A300-195A-2), CHK1 phospho-S345 (CST; 2341), CHK1 (Santa Cruz; sc-8408), RPA32 (Santa Cruz; sc-56770), CDC6 (Santa Cruz; sc-9964), FLAG (Sigma; F1804-200UG), HA (Sino Biology; 100028-MM10), HA (CST; 3724S), GAPDH (Proteintech; 10494-1-AP and 60004-1-Ig), Histone H3 (Abclonal; A2348).

Techniques: Cryo-EM Sample Prep, Binding Assay

(A) Cryo-EM density map of an MCM2–7 single hexamer (SH) superimposed with the atomic model, with a close-up view of the MCM3 WHD-MCM2 interface. (B and C) Close-up views of key interacting residues at the MCM3 WHD–MCM2 interface. (D) The closed DNA entry gate in DNA-bound MCM2–7 DH (PDB ID: 7W1Y) with only MCM2 and MCM5 shown. A close-up view of the MCM2-MCM5 interface is shown on the right. (E) Cryo-EM density maps of recombinant human MCM2–7 SH that contains either MCM3 wild type (WT; top) or the MCM3 3A mutant (bottom). The density of MCM3 WHD (top) and its corresponding location (bottom) are boxed by red dashed lines. (F) Schematic diagram depicting the closed MCM3 WHD latch, which is expected to block DNA entry. (G) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the recombinant MCM2–7 complex containing MCM3 with its WHD deleted (MCM3 ΔWHD ). The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE and Coomassie staining. The experiment was repeated three times with similar results. (H) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the ORC1-6–CDC6 complex. The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE followed by Coomassie staining (bottom panel) and immunoblotting with anti-ORC1 and anti-CDC6 antibodies (top panels). The experiment was repeated three times with similar results.

Journal: bioRxiv

Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

doi: 10.1101/2025.05.31.656953

Figure Lengend Snippet: (A) Cryo-EM density map of an MCM2–7 single hexamer (SH) superimposed with the atomic model, with a close-up view of the MCM3 WHD-MCM2 interface. (B and C) Close-up views of key interacting residues at the MCM3 WHD–MCM2 interface. (D) The closed DNA entry gate in DNA-bound MCM2–7 DH (PDB ID: 7W1Y) with only MCM2 and MCM5 shown. A close-up view of the MCM2-MCM5 interface is shown on the right. (E) Cryo-EM density maps of recombinant human MCM2–7 SH that contains either MCM3 wild type (WT; top) or the MCM3 3A mutant (bottom). The density of MCM3 WHD (top) and its corresponding location (bottom) are boxed by red dashed lines. (F) Schematic diagram depicting the closed MCM3 WHD latch, which is expected to block DNA entry. (G) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the recombinant MCM2–7 complex containing MCM3 with its WHD deleted (MCM3 ΔWHD ). The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE and Coomassie staining. The experiment was repeated three times with similar results. (H) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the ORC1-6–CDC6 complex. The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE followed by Coomassie staining (bottom panel) and immunoblotting with anti-ORC1 and anti-CDC6 antibodies (top panels). The experiment was repeated three times with similar results.

Techniques: Cryo-EM Sample Prep, Recombinant, Mutagenesis, Blocking Assay, Binding Assay, SDS Page, Staining, Western Blot

$(A) Immunoblots of whole-cell extracts (left panels) or chromatin fractions (right panels) of the indicated 293FT cells treated with DMSO or dTAG-13 (1 µM) for 16 h. GAPDH and histone H3 are used as loading controls. Relative intensities of HA-MCM3 and the endogenous MCM2 are quantified and shown below respective panels. (B) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) without pre-extraction before fixation. The HA signals in this staining protocol represent total cellular HA-MCM3. (C) Quantification of HA-MCM3 intensities of cells in (B). Each dot in the graph represents a single cell. (D) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) with pre-extraction before fixation. The HA signals in this staining protocol represent chromatin-bound HA-MCM3. (E) Quantification of HA-MCM3 intensities of cells in (D). (F) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) without pre-extraction before fixation. (G) Quantification of MCM5 intensities of cells in (F). (H) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) with pre-extraction before fixation. (I) Quantification of MCM5 intensities of cells in (H). For all relevant panels, the scale bar indicates 10 µm. Mean ± SD are shown.$

Journal: bioRxiv

Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

doi: 10.1101/2025.05.31.656953

Figure Lengend Snippet: (A) Immunoblots of whole-cell extracts (left panels) or chromatin fractions (right panels) of the indicated 293FT cells treated with DMSO or dTAG-13 (1 µM) for 16 h. GAPDH and histone H3 are used as loading controls. Relative intensities of HA-MCM3 and the endogenous MCM2 are quantified and shown below respective panels. (B) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) without pre-extraction before fixation. The HA signals in this staining protocol represent total cellular HA-MCM3. (C) Quantification of HA-MCM3 intensities of cells in (B). Each dot in the graph represents a single cell. (D) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) with pre-extraction before fixation. The HA signals in this staining protocol represent chromatin-bound HA-MCM3. (E) Quantification of HA-MCM3 intensities of cells in (D). (F) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) without pre-extraction before fixation. (G) Quantification of MCM5 intensities of cells in (F). (H) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) with pre-extraction before fixation. (I) Quantification of MCM5 intensities of cells in (H). For all relevant panels, the scale bar indicates 10 µm. Mean ± SD are shown.

Techniques: Western Blot, Staining, Extraction

a The level of miR-195a-5p in Mφ from WT and Atg7 Δmye mice. n = 4 biological replicates for each group. b The level of miR-195a-5p in Mφ-derived exosomes. c The level of miR-195a-5p in TECs after the incubation with exosomes (10 μg/ml). n = 3 biological replicates for each group. d Flow cytometry analysis of the mitochondrial membrane potential ( Δψm ) in TECs. n = 3 biological replicates for each group. e Representative images and quantification of mitochondrial ROS (mtROS) (red) in TECs. Scale bars, 10 µm, n = 3 biological replicates for each group f Representative immunofluorescence images and quantification of mitochondrial morphology (green) in TECs loaded with MitoTracker Green. Scale bars, 10 µm and 2 µm. g The ATP content of TECs was measured by an ATP assay kit, and the ATP concentration was calculated in nmol/mg protein. n = 3 biological replicates for each group. h Measurement of the mitochondrial OCR in TECs using a Mito Stress kit, and the quantification of basal respiration, ATP production, maximal respiration, and spare respiration capacity. n = 3 biological replicates for each group. The data are presented as the means ± SEMs. All statistical analysis were performed by unpaired two-tailed Student’s t test. EXO1, Mφ WT -EXO; EXO2, Mφ Atg7Δmye -EXO. Source data are provided as a Source data file.

Journal: Nature Communications

Article Title: Autophagy-deficient macrophages exacerbate cisplatin-induced mitochondrial dysfunction and kidney injury via miR-195a-5p-SIRT3 axis

doi: 10.1038/s41467-024-47842-z

Figure Lengend Snippet: a The level of miR-195a-5p in Mφ from WT and Atg7 Δmye mice. n = 4 biological replicates for each group. b The level of miR-195a-5p in Mφ-derived exosomes. c The level of miR-195a-5p in TECs after the incubation with exosomes (10 μg/ml). n = 3 biological replicates for each group. d Flow cytometry analysis of the mitochondrial membrane potential ( Δψm ) in TECs. n = 3 biological replicates for each group. e Representative images and quantification of mitochondrial ROS (mtROS) (red) in TECs. Scale bars, 10 µm, n = 3 biological replicates for each group f Representative immunofluorescence images and quantification of mitochondrial morphology (green) in TECs loaded with MitoTracker Green. Scale bars, 10 µm and 2 µm. g The ATP content of TECs was measured by an ATP assay kit, and the ATP concentration was calculated in nmol/mg protein. n = 3 biological replicates for each group. h Measurement of the mitochondrial OCR in TECs using a Mito Stress kit, and the quantification of basal respiration, ATP production, maximal respiration, and spare respiration capacity. n = 3 biological replicates for each group. The data are presented as the means ± SEMs. All statistical analysis were performed by unpaired two-tailed Student’s t test. EXO1, Mφ WT -EXO; EXO2, Mφ Atg7Δmye -EXO. Source data are provided as a Source data file.

Article Snippet: For in vitro treatment, tubular epithelial cells (TECs) treated with EXOs were transfected with miR-195a-5p inhibitor (200 nM) or inhibitor negative control (200 nM) (RiboBio Co., Ltd.) using a FECT CP Transfection Kit (RiboBio) according to the manufacturer’s protocols.

Techniques: Derivative Assay, Incubation, Flow Cytometry, Membrane, Immunofluorescence, ATP Assay, Concentration Assay, Two Tailed Test

a The level of miR-195a-5p in kidney sections from WT and Atg7 Δmye mice. n = 4 biological replicates for each group. b Representative IVIS images of different organs harvested from mice after intravenous injection of anti-miR-195a-5p-5’Cy5 (PBS vs . Anti-miR-195a-5p-CY5-24h, P = 0.0009; PBS vs . Anti-miR-195a-5p-CY5-48h, P = 0.0002; PBS vs . Anti-miR-195a-5p-CY5-72h, P = 0.0025; PBS vs . Anti-miR-195a-5p-CY5-96h, P = 0.001). n = 3 biological replicates for each group, unpaired two-tailed Student’s t test. c Representative micrographs of anti-miR-195a-5p-5’Cy5 (red) in the kidney. Scale bar, 20 μm. d Representative TEM images of kidney tissues from mice. Scale bar, 2 µm. e Representative images of western blot and quantitative analyses of OXPHOS-related genes (ATP5b, UQCRC2, mtCO1, SDHB, and NDUFS4). ACTIN was used as the loading control. n = 3 biological replicates for each group. f The serum levels of BUN and CREA in the Atg7 Δmye mice. n = 6 biological replicates for each group. g Representative images of hematoxylin-eosin (HE) and periodic acid-Schiff (PAS)-staining ( n = 6 biological replicates for each group), immunohistochemical staining and quantification of ATP5b and KIM1 ( n = 4 biological replicates for each group) in paraffin-embedded kidney sections. Scale bars, 50 µm. h Representative micrographs and quantification of TUNEL staining (green) in Atg7 Δmye mice treated with anti-NC or anti-miR-195a-5p treatment. Scale bars, 50 µm, n = 6 biological replicates for each group. i Representative images of western blots and quantitative analyses of BAX and Bcl-2 expression. ACTIN was used as the loading control. n = 5 biological replicates for each group. The data are the means ± SEMs. Statistical analysis was performed by two-way ANOVA with Tukey’s multiple comparison test in ( a ) and ( e – i ). Source data are provided as a Source data file.

Journal: Nature Communications

Article Title: Autophagy-deficient macrophages exacerbate cisplatin-induced mitochondrial dysfunction and kidney injury via miR-195a-5p-SIRT3 axis

doi: 10.1038/s41467-024-47842-z

Figure Lengend Snippet: a The level of miR-195a-5p in kidney sections from WT and Atg7 Δmye mice. n = 4 biological replicates for each group. b Representative IVIS images of different organs harvested from mice after intravenous injection of anti-miR-195a-5p-5’Cy5 (PBS vs . Anti-miR-195a-5p-CY5-24h, P = 0.0009; PBS vs . Anti-miR-195a-5p-CY5-48h, P = 0.0002; PBS vs . Anti-miR-195a-5p-CY5-72h, P = 0.0025; PBS vs . Anti-miR-195a-5p-CY5-96h, P = 0.001). n = 3 biological replicates for each group, unpaired two-tailed Student’s t test. c Representative micrographs of anti-miR-195a-5p-5’Cy5 (red) in the kidney. Scale bar, 20 μm. d Representative TEM images of kidney tissues from mice. Scale bar, 2 µm. e Representative images of western blot and quantitative analyses of OXPHOS-related genes (ATP5b, UQCRC2, mtCO1, SDHB, and NDUFS4). ACTIN was used as the loading control. n = 3 biological replicates for each group. f The serum levels of BUN and CREA in the Atg7 Δmye mice. n = 6 biological replicates for each group. g Representative images of hematoxylin-eosin (HE) and periodic acid-Schiff (PAS)-staining ( n = 6 biological replicates for each group), immunohistochemical staining and quantification of ATP5b and KIM1 ( n = 4 biological replicates for each group) in paraffin-embedded kidney sections. Scale bars, 50 µm. h Representative micrographs and quantification of TUNEL staining (green) in Atg7 Δmye mice treated with anti-NC or anti-miR-195a-5p treatment. Scale bars, 50 µm, n = 6 biological replicates for each group. i Representative images of western blots and quantitative analyses of BAX and Bcl-2 expression. ACTIN was used as the loading control. n = 5 biological replicates for each group. The data are the means ± SEMs. Statistical analysis was performed by two-way ANOVA with Tukey’s multiple comparison test in ( a ) and ( e – i ). Source data are provided as a Source data file.

Techniques: Injection, Two Tailed Test, Western Blot, Control, Staining, Immunohistochemical staining, TUNEL Assay, Expressing, Comparison

a Prediction of SIRT3 as a target of miR-195a-5p. b Dual-luciferase assays of TECs cotransfected with a SIRT3 luciferase reporter (pmirGLO-SIRT3-WT, SIRT3-WT) and a miR-195a-5p mimic or mutant SIRT3 luciferase reporter (pmirGLO-SIRT3-MUT, SIRT3-MUT), and the luciferase activity of the cells was detected using a dual-luciferase assay kit. n = 4 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. c , d Western blot and quantitative analyses of SIRT3 in TECs treated with the treatment of miR-195a-5p mimic, or miR-195a-5p inhibitor. ACTIN was used as the loading control. n = 3 biological replicates for each group. e Representative images and quantification of mitochondrial ROS (mtROS) (red) and mitochondrial morphology (green) in TECs. Scale bars, 10 µm and 2 µm, n = 3 biological replicates for each group. f Measurement of the mitochondrial OCR in TECs using a Mito Stress kit and quantification of basal respiration, ATP production, maximal respiration, and spare respiration capacity. n = 3 biological replicates for each group. Statistical analysis were performed by unpaired two-tailed Student’s t test in ( c – f ). For lentiviral experiments, cisplatin-induced AKI was induced 3 days after intrarenal injection of lentivirus carrying SIRT3 (LV- Sirt3 ) or NC (LV-nc). g Representative micrographs of SIRT3 (red) and TEM images of the kidneys of Atg7 Δmye mice. Scale bars, 20 µm and 2 µm, n = 3 biological replicates for each group. h Serum levels of BUN and CREA in mice. n = 5 biological replicates for each group. i Representative images of hematoxylin-eosin (HE) and periodic acid-Schiff (PAS)-staining, and immunohistochemical staining and quantification of KIM1 expression in kidney sections. Scale bars, 50 µm, n = 4 biological replicates for each group. Statistical analysis was performed by two-way ANOVA with Tukey’s multiple comparison test in ( g – i ). The data are the means ± SEMs. Source data are provided as a Source data file.

Journal: Nature Communications

Article Title: Autophagy-deficient macrophages exacerbate cisplatin-induced mitochondrial dysfunction and kidney injury via miR-195a-5p-SIRT3 axis

doi: 10.1038/s41467-024-47842-z

Figure Lengend Snippet: a Prediction of SIRT3 as a target of miR-195a-5p. b Dual-luciferase assays of TECs cotransfected with a SIRT3 luciferase reporter (pmirGLO-SIRT3-WT, SIRT3-WT) and a miR-195a-5p mimic or mutant SIRT3 luciferase reporter (pmirGLO-SIRT3-MUT, SIRT3-MUT), and the luciferase activity of the cells was detected using a dual-luciferase assay kit. n = 4 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. c , d Western blot and quantitative analyses of SIRT3 in TECs treated with the treatment of miR-195a-5p mimic, or miR-195a-5p inhibitor. ACTIN was used as the loading control. n = 3 biological replicates for each group. e Representative images and quantification of mitochondrial ROS (mtROS) (red) and mitochondrial morphology (green) in TECs. Scale bars, 10 µm and 2 µm, n = 3 biological replicates for each group. f Measurement of the mitochondrial OCR in TECs using a Mito Stress kit and quantification of basal respiration, ATP production, maximal respiration, and spare respiration capacity. n = 3 biological replicates for each group. Statistical analysis were performed by unpaired two-tailed Student’s t test in ( c – f ). For lentiviral experiments, cisplatin-induced AKI was induced 3 days after intrarenal injection of lentivirus carrying SIRT3 (LV- Sirt3 ) or NC (LV-nc). g Representative micrographs of SIRT3 (red) and TEM images of the kidneys of Atg7 Δmye mice. Scale bars, 20 µm and 2 µm, n = 3 biological replicates for each group. h Serum levels of BUN and CREA in mice. n = 5 biological replicates for each group. i Representative images of hematoxylin-eosin (HE) and periodic acid-Schiff (PAS)-staining, and immunohistochemical staining and quantification of KIM1 expression in kidney sections. Scale bars, 50 µm, n = 4 biological replicates for each group. Statistical analysis was performed by two-way ANOVA with Tukey’s multiple comparison test in ( g – i ). The data are the means ± SEMs. Source data are provided as a Source data file.

Techniques: Luciferase, Mutagenesis, Activity Assay, Comparison, Western Blot, Control, Two Tailed Test, Injection, Staining, Immunohistochemical staining, Expressing

a Peritoneal Mφ isolated from AKI mice were treated with trehalose, after which the protein levels of LC3 II and P62 were measured. ACTIN was used as the loading control. n = 3 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. b The level of miR-195a-5p in Mφ from AKI mice treated with trehalose. ACTIN was used as the loading control. n = 3 biological replicates for each group, unpaired two-tailed Student’s t test. After endogenous Mφ were deleted by clodronate liposomes (Lipo-Clod), AKI was induced in mice by cisplatin. Then, Mφ from AKI mice (Mφ AKI ) or trehalose-treated Mφ AKI mice (Mφ AKI +Tre) were adoptively transferred into the mice at 6 h after cisplatin treatment. c western blot and quantitative analyses of OXPHOS-related proteins. ACTIN was used as the loading control. n = 3 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. d Representative TEM images and hematoxylin-eosin (HE) staining of kidneys from AKI mice after adoptive transfer of Mφ. Scale bars, 2 µm and 50 µm, n = 4 biological replicates for each group, unpaired two-tailed Student’s t test. e Renal function (serum levels of BUN and CREA) detection. n = 6 biological replicates for each group, one-way ANOVA with Tukey’s multiple comparisons test. f Representative micrographs and quantification of TUNEL staining (green) in each group. Scale bars, 20 µm and 50 µm, n = 6 biological replicates for each group, one-way ANOVA with Tukey’s multiple comparisons test. g Schematic representation of the data. Data in ( a ) and ( b ) show a representative of three independent experiments. The data are the means ± SEMs. Source data are provided as a Source data file.

Journal: Nature Communications

Article Title: Autophagy-deficient macrophages exacerbate cisplatin-induced mitochondrial dysfunction and kidney injury via miR-195a-5p-SIRT3 axis

doi: 10.1038/s41467-024-47842-z

Figure Lengend Snippet: a Peritoneal Mφ isolated from AKI mice were treated with trehalose, after which the protein levels of LC3 II and P62 were measured. ACTIN was used as the loading control. n = 3 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. b The level of miR-195a-5p in Mφ from AKI mice treated with trehalose. ACTIN was used as the loading control. n = 3 biological replicates for each group, unpaired two-tailed Student’s t test. After endogenous Mφ were deleted by clodronate liposomes (Lipo-Clod), AKI was induced in mice by cisplatin. Then, Mφ from AKI mice (Mφ AKI ) or trehalose-treated Mφ AKI mice (Mφ AKI +Tre) were adoptively transferred into the mice at 6 h after cisplatin treatment. c western blot and quantitative analyses of OXPHOS-related proteins. ACTIN was used as the loading control. n = 3 biological replicates for each group, two-way ANOVA with Tukey’s multiple comparison test. d Representative TEM images and hematoxylin-eosin (HE) staining of kidneys from AKI mice after adoptive transfer of Mφ. Scale bars, 2 µm and 50 µm, n = 4 biological replicates for each group, unpaired two-tailed Student’s t test. e Renal function (serum levels of BUN and CREA) detection. n = 6 biological replicates for each group, one-way ANOVA with Tukey’s multiple comparisons test. f Representative micrographs and quantification of TUNEL staining (green) in each group. Scale bars, 20 µm and 50 µm, n = 6 biological replicates for each group, one-way ANOVA with Tukey’s multiple comparisons test. g Schematic representation of the data. Data in ( a ) and ( b ) show a representative of three independent experiments. The data are the means ± SEMs. Source data are provided as a Source data file.

Techniques: Isolation, Control, Comparison, Two Tailed Test, Liposomes, Western Blot, Staining, Adoptive Transfer Assay, TUNEL Assay

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