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af043742 98 12b 1 alteromonas distincta type entrez nucleotide attrs text af043742 term id 6652557 term text af043742 (ATCC)

Name: af043742 98 12b 1 alteromonas distincta type entrez nucleotide attrs text af043742 term id 6652557 term text af043742
Brand: ATCC
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ATCC af043742 98 12b 1 alteromonas distincta type entrez nucleotide attrs text af043742 term id 6652557 term text af043742
16S rDNA sequences most closely related to the major bacterial populations detected by DGGE shown in Fig. Fig.4 4 and

16S rDNA sequences most closely related to the major bacterial populations detected by DGGE shown in Fig. Fig.4 4 and

Af043742 98 12b 1 Alteromonas Distincta Type Entrez Nucleotide Attrs Text Af043742 Term Id 6652557 Term Text Af043742, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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af043742 98 12b 1 alteromonas distincta type entrez nucleotide attrs text af043742 term id 6652557 term text af043742 - by Bioz Stars, 2025-06

90/100 stars

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1) Product Images from "Extracellular Polysaccharides of Rhodococcus rhodochrous S-2 Stimulate the Degradation of Aromatic Components in Crude Oil by Indigenous Marine Bacteria"

Article Title: Extracellular Polysaccharides of Rhodococcus rhodochrous S-2 Stimulate the Degradation of Aromatic Components in Crude Oil by Indigenous Marine Bacteria

Journal:

doi: 10.1128/AEM.68.5.2337-2343.2002

Figure Legend Snippet: 16S rDNA sequences most closely related to the major bacterial populations detected by DGGE shown in Fig. Fig.4 4 and

Techniques Used: Sequencing

Image Search Results

Identification of TMEM52B, upregulation of which in NPC is correlated with poor prognosis. A) Heatmap of the top 15 differentially expressed genes from RNA sequencing that were upregulated in various types of NPC cells. B) mRNA levels of TMEM52B by real‐time PCR in NPEC and NPC cells with β‐actin as the internal control. Data were represented as mean ± standard deviation (SD), n = 3, *** p < 0.001 versus NP‐69. C) Protein levels of TMEM52B by western blotting in NPEC and NPC cells, β‐tubulin was used as the internal control. D) Immunohistochemical staining of TMEM52B expression in NPC using a tissue microarray containing 132 human NPC tissues. Scale bar, 200 µm. E,F) TMEM52B expression was analyzed in NPC patients regarding tumor node metastasis (TNM) stage and recurrence using data in the NPC tissue microarray. G) Overall survival in NPC patients based on the expression of TMEM42B in the NPC tissue microarray, shown by Kaplan–Meier analysis. The median of TMEM52B levels was used to divide the high and low‐expression groups. H) TMEM52B was a biomarker for the overall survival of NPC as indicated by receiver operating curve (ROC) analysis. I,J) ROC curve analysis for TMEM52B as a diagnostic indicator in discriminating advanced stages (stages III and IV) from early stages (stages I and II), and to predict recurrence from no recurrence for NPC patients. P value calculated by unpaired two‐tailed Student's t ‐test (B, F), one‐way ANOVA (E), and log‐rank test(G).

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: Identification of TMEM52B, upregulation of which in NPC is correlated with poor prognosis. A) Heatmap of the top 15 differentially expressed genes from RNA sequencing that were upregulated in various types of NPC cells. B) mRNA levels of TMEM52B by real‐time PCR in NPEC and NPC cells with β‐actin as the internal control. Data were represented as mean ± standard deviation (SD), n = 3, *** p < 0.001 versus NP‐69. C) Protein levels of TMEM52B by western blotting in NPEC and NPC cells, β‐tubulin was used as the internal control. D) Immunohistochemical staining of TMEM52B expression in NPC using a tissue microarray containing 132 human NPC tissues. Scale bar, 200 µm. E,F) TMEM52B expression was analyzed in NPC patients regarding tumor node metastasis (TNM) stage and recurrence using data in the NPC tissue microarray. G) Overall survival in NPC patients based on the expression of TMEM42B in the NPC tissue microarray, shown by Kaplan–Meier analysis. The median of TMEM52B levels was used to divide the high and low‐expression groups. H) TMEM52B was a biomarker for the overall survival of NPC as indicated by receiver operating curve (ROC) analysis. I,J) ROC curve analysis for TMEM52B as a diagnostic indicator in discriminating advanced stages (stages III and IV) from early stages (stages I and II), and to predict recurrence from no recurrence for NPC patients. P value calculated by unpaired two‐tailed Student's t ‐test (B, F), one‐way ANOVA (E), and log‐rank test(G).

Article Snippet: Western blotting was performed using the following antibodies: anti‐TMEM52B (NBP2‐49272, Novus), anti‐Flag (#14 793, Cell Signaling), anti‐Flag (F1804, Sigma‐Aldrich), anti‐N‐cadherin (sc‐7939, Santa Cruz Biotechnology), anti‐E‐cadherin (#3195, Cell Signaling), anti‐vimentin (sc‐7557, Santa Cruz Biotechnology), anti‐Twist (ab50887, Abcam), anti‐PGK1/2 (sc‐48342, Santa Cruz Biotechnology), anti‐PLEC‐1 (#12 254, Cell Signaling), anti‐phospho‐AKT (S473) (#4060, Cell Signaling), anti‐phospho‐AKT (T308) (#4056, Cell Signaling), anti‐AKT (pan) (#4691, Cell Signaling), and anti‐β‐tubulin (ab6046, Abcam).

Techniques: RNA Sequencing Assay, Real-time Polymerase Chain Reaction, Control, Standard Deviation, Western Blot, Immunohistochemical staining, Staining, Expressing, Microarray, Biomarker Assay, Diagnostic Assay, Two Tailed Test

Univariate and multivariate Cox regression analyses of TMEM52B for overall survival in NPC.

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: Univariate and multivariate Cox regression analyses of TMEM52B for overall survival in NPC.

Techniques: Expressing

TMEM52B knockdown inhibits NPC growth and metastasis in vitro and in vivo. A,B) Decreased mRNA and protein levels of TMEM52B in SUNE‐1 and S18 cells following siRNA transfection were shown by real‐time PCR and western blotting, β‐actin and β‐tubulin were used as the internal control, respectively C,D) The inhibitory effects on cell viability and proliferation after TMEM52B knockdown as shown by CCK‐8 and EdU assays in SUNE‐1 and S18 cells. Scale bar, 50 µm. E,F) Transwell assays to determine the suppressive effects of TMEM52B depletion on the migration and invasion of SUNE‐1 and S18 cells. Scale bar, 100 µm. G–K) SUEN‐1 cells pre‐infected with control or TMEM52B‐shRNA‐expressing lentivirus were subcutaneously inoculated into the flank of each BALB/c nude mouse ( n = 7 per group). The growth curves of tumors (G), tumor photographs (H); and tumor weights (I), in the nude mice were analyzed. The expression of TMEM52B (J) and Ki67 (K) in subcutaneous tumors was estimated using immunohistochemistry. Scale bar, 50 µm. Data were represented as mean ± SD in (A,C–F), n≥3, and mean ± standard error of the mean (SEM) in (G,I), * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test (A,D–F,I), and two‐way ANOVA (C, G).

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: TMEM52B knockdown inhibits NPC growth and metastasis in vitro and in vivo. A,B) Decreased mRNA and protein levels of TMEM52B in SUNE‐1 and S18 cells following siRNA transfection were shown by real‐time PCR and western blotting, β‐actin and β‐tubulin were used as the internal control, respectively C,D) The inhibitory effects on cell viability and proliferation after TMEM52B knockdown as shown by CCK‐8 and EdU assays in SUNE‐1 and S18 cells. Scale bar, 50 µm. E,F) Transwell assays to determine the suppressive effects of TMEM52B depletion on the migration and invasion of SUNE‐1 and S18 cells. Scale bar, 100 µm. G–K) SUEN‐1 cells pre‐infected with control or TMEM52B‐shRNA‐expressing lentivirus were subcutaneously inoculated into the flank of each BALB/c nude mouse ( n = 7 per group). The growth curves of tumors (G), tumor photographs (H); and tumor weights (I), in the nude mice were analyzed. The expression of TMEM52B (J) and Ki67 (K) in subcutaneous tumors was estimated using immunohistochemistry. Scale bar, 50 µm. Data were represented as mean ± SD in (A,C–F), n≥3, and mean ± standard error of the mean (SEM) in (G,I), * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test (A,D–F,I), and two‐way ANOVA (C, G).

Techniques: Knockdown, In Vitro, In Vivo, Transfection, Real-time Polymerase Chain Reaction, Western Blot, Control, CCK-8 Assay, Migration, Infection, shRNA, Expressing, Immunohistochemistry, Two Tailed Test

Overexpression of TMEM52B‐P18 and TMEM52B‐P20 isoforms similarly promotes NPC growth in vitro and in vivo. A) The aligned amino acid sequences of TMEM52‐B‐P18 and TMEM52B‐P20 isoforms. B,C) The increased mRNA and protein levels of TMEM52B isoforms in HONE‐1 and HK‐1 cells following infection with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus, analyzed by real‐time PCR and western blotting with β‐actin and β‐tubulin as the internal control, respectively. D,E) The role of TMEM52B isoforms in promoting cell viability and proliferation after TMEM52B overexpression were shown using CCK‐8 and EdU assays in HONE‐1 and HK‐1 cells. Scale bar, 50 µm. F–J. HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus were subcutaneously inoculated into the flank of each BALB/c nude mouse ( n = 5 per group). The growth curves of F) tumors, G) tumor photographs, and H) tumor weights are shown. The expression of I) TMEM52B and J) Ki67 in subcutaneous tumors was estimated using immunohistochemistry. Scale bar, 50 µm. Data were represented as mean ± SD in (B, D, E), n≥3, and mean ± SEM in (F,H), * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t ‐test (B,E,H), and two‐way ANOVA (D,F).

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: Overexpression of TMEM52B‐P18 and TMEM52B‐P20 isoforms similarly promotes NPC growth in vitro and in vivo. A) The aligned amino acid sequences of TMEM52‐B‐P18 and TMEM52B‐P20 isoforms. B,C) The increased mRNA and protein levels of TMEM52B isoforms in HONE‐1 and HK‐1 cells following infection with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus, analyzed by real‐time PCR and western blotting with β‐actin and β‐tubulin as the internal control, respectively. D,E) The role of TMEM52B isoforms in promoting cell viability and proliferation after TMEM52B overexpression were shown using CCK‐8 and EdU assays in HONE‐1 and HK‐1 cells. Scale bar, 50 µm. F–J. HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus were subcutaneously inoculated into the flank of each BALB/c nude mouse ( n = 5 per group). The growth curves of F) tumors, G) tumor photographs, and H) tumor weights are shown. The expression of I) TMEM52B and J) Ki67 in subcutaneous tumors was estimated using immunohistochemistry. Scale bar, 50 µm. Data were represented as mean ± SD in (B, D, E), n≥3, and mean ± SEM in (F,H), * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t ‐test (B,E,H), and two‐way ANOVA (D,F).

Techniques: Over Expression, In Vitro, In Vivo, Infection, Control, Expressing, Real-time Polymerase Chain Reaction, Western Blot, CCK-8 Assay, Immunohistochemistry, Two Tailed Test

Overexpressing TMEM52B‐P18 and TMEM52B‐P20 isoforms differentially promotes NPC metastasis in vitro and in vivo. A,B) Transwell assays to determine the effects of TMEM52B isoforms after TMEM52B overexpression on accelerating the migration and invasion of HONE‐1 and HK‐1 cells. Scale bar, 100 µm. C) Representative images showed different cell morphology of HONE‐1 cells overexpressing TMEM52B isoforms versus controls. Scale bar, 200 µm. D) Protein levels of E‐cadherin, N‐cadherin, vimentin, and twist in cells overexpressing TMEM52B‐P18, or TMEM52B‐P20 and in controls were analyzed by western blotting using whole lysates extracted from HONE‐1 and HK‐1 cells, β‐tubulin was used as the loading control. E) Photographs of pulmonary tumors generated by HONE‐1 cells transfected with LV‐oeCtrl ( n = 7), LV‐TMEM52B‐P18 ( n = 8) or LV‐TMEM52B‐P20 ( n = 8). F) Body weight curves of nude mice injected with LV‐oeCtrl, LV‐TMEM52B‐P18, or LV‐TMEM52B‐P20 HONE‐1 cells. G. Survival curves of nude mice inoculated with LV‐oeCtrl, LV‐TMEM52B‐P18, or LV‐TMEM52B‐P20 HONE‐1 cells. Data were represented as mean ± SD, n = 5, in (A,B) and mean ± SEM in (F); ns, no significance; ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t ‐test (A,B), two‐way F) ANOVA, and G) log‐rank test.

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: Overexpressing TMEM52B‐P18 and TMEM52B‐P20 isoforms differentially promotes NPC metastasis in vitro and in vivo. A,B) Transwell assays to determine the effects of TMEM52B isoforms after TMEM52B overexpression on accelerating the migration and invasion of HONE‐1 and HK‐1 cells. Scale bar, 100 µm. C) Representative images showed different cell morphology of HONE‐1 cells overexpressing TMEM52B isoforms versus controls. Scale bar, 200 µm. D) Protein levels of E‐cadherin, N‐cadherin, vimentin, and twist in cells overexpressing TMEM52B‐P18, or TMEM52B‐P20 and in controls were analyzed by western blotting using whole lysates extracted from HONE‐1 and HK‐1 cells, β‐tubulin was used as the loading control. E) Photographs of pulmonary tumors generated by HONE‐1 cells transfected with LV‐oeCtrl ( n = 7), LV‐TMEM52B‐P18 ( n = 8) or LV‐TMEM52B‐P20 ( n = 8). F) Body weight curves of nude mice injected with LV‐oeCtrl, LV‐TMEM52B‐P18, or LV‐TMEM52B‐P20 HONE‐1 cells. G. Survival curves of nude mice inoculated with LV‐oeCtrl, LV‐TMEM52B‐P18, or LV‐TMEM52B‐P20 HONE‐1 cells. Data were represented as mean ± SD, n = 5, in (A,B) and mean ± SEM in (F); ns, no significance; ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t ‐test (A,B), two‐way F) ANOVA, and G) log‐rank test.

Techniques: In Vitro, In Vivo, Over Expression, Migration, Western Blot, Control, Generated, Transfection, Injection, Two Tailed Test

RNA sequencing reveals that TMEM52B affects AKT signaling. A) Volcano plots of RNA sequencing analysis of HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus (|log2fold change| > 1 and Q value < 0.01, green indicates downregulated genes; red indicates upregulated genes). B,C) Metascape enrichment analysis showing groups of several categories based on gene functional relevance; a network was constructed based on relevance and similarity. Different colors represent different categories. D) The top 20 enriched biological processes of differentially expressed genes in LV‐TMEM52B‐P18/LV‐oeCtrl and LV‐TMEM52B‐P20/LV‐oeCtrl HONE‐1 cells. E) Heat map showing the expression of PI3K‐Akt signaling pathway‐related genes by HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus (blue indicates downregulated genes; red indicates upregulated genes). F) Real‐time PCR analysis of mRNA levels of AKT and TMEM52B in HONE‐1 or HK‐1 cells overexpressing TMEM52B isoforms and SUNE‐1 or S18 cells silencing TMEM52B, β‐actin was used as the internal control. G,H) Phosphorylated levels of AKT at S473 and T308 sites in LV‐oeCtrl, LV‐TMEM52B‐P18 or LV‐TMEM52B‐P20 HONE‐1 and HK‐1 cells (G), as well as LV‐shCtrl or LV‐shTMEM52B infected SUNE‐1 and S18 cells (H), by western blotting with β‐tubulin as the loading control. Data were represented as mean ±SD, n≥3; ns, no significance; * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: RNA sequencing reveals that TMEM52B affects AKT signaling. A) Volcano plots of RNA sequencing analysis of HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus (|log2fold change| > 1 and Q value < 0.01, green indicates downregulated genes; red indicates upregulated genes). B,C) Metascape enrichment analysis showing groups of several categories based on gene functional relevance; a network was constructed based on relevance and similarity. Different colors represent different categories. D) The top 20 enriched biological processes of differentially expressed genes in LV‐TMEM52B‐P18/LV‐oeCtrl and LV‐TMEM52B‐P20/LV‐oeCtrl HONE‐1 cells. E) Heat map showing the expression of PI3K‐Akt signaling pathway‐related genes by HONE‐1 cells pre‐infected with control, TMEM52B‐P18‐expressing, or TMEM52B‐P20‐expressing lentivirus (blue indicates downregulated genes; red indicates upregulated genes). F) Real‐time PCR analysis of mRNA levels of AKT and TMEM52B in HONE‐1 or HK‐1 cells overexpressing TMEM52B isoforms and SUNE‐1 or S18 cells silencing TMEM52B, β‐actin was used as the internal control. G,H) Phosphorylated levels of AKT at S473 and T308 sites in LV‐oeCtrl, LV‐TMEM52B‐P18 or LV‐TMEM52B‐P20 HONE‐1 and HK‐1 cells (G), as well as LV‐shCtrl or LV‐shTMEM52B infected SUNE‐1 and S18 cells (H), by western blotting with β‐tubulin as the loading control. Data were represented as mean ±SD, n≥3; ns, no significance; * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Techniques: RNA Sequencing Assay, Infection, Control, Expressing, Functional Assay, Construct, Real-time Polymerase Chain Reaction, Western Blot, Two Tailed Test

TMEM52B isoforms interact with PGK1 to promote NPC growth. A) Both TMEM52B isoforms interact with PGK1. Cell lysates from HONE‐1 cells overexpressing TMEM52B‐P18 or TMEM52B‐P20 and control cells were immunoprecipitated with anti‐Flag, followed by western blotting with anti‐PGK1 or anti‐Flag antibody on the precipitates and lysates, as indicated. B) Reciprocal immunoprecipitation (IP) was performed on cell lysates from HONE‐1 cells overexpressing TMEM52B‐P18 or TMEM52B‐P20 and control cells, by precipitating with anti‐PGK1, followed by western blotting with anti‐TMEM52B or anti‐PGK1 antibody on the precipitates and lysates, as indicated. C) The effects of TMEM52B‐P18 and TMEM52B‐P20 on the phosphorylation of AKT depend on PGK1. HONE‐1 cells were transfected with siRNA control or PGK1 siRNA sequences, followed by the transfection of control, TMEM52B‐P18 or TMEM52B‐P20 plasmids. Western blotting was performed to estimate the phosphorylation of AKT at S473 and T308 sites with β‐tubulin as the loading control. D) Cell viability and proliferation of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression, assessed by CCK‐8. E) Cloning of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression. F,G) Cell migration and invasion of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression, assessed by transwell assays. Scale bar, 100 µm. Data were represented as mean ±SD, n ≥ 3; ns, no significance; * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test (E‐G) and two‐way ANOVA (D).

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: TMEM52B isoforms interact with PGK1 to promote NPC growth. A) Both TMEM52B isoforms interact with PGK1. Cell lysates from HONE‐1 cells overexpressing TMEM52B‐P18 or TMEM52B‐P20 and control cells were immunoprecipitated with anti‐Flag, followed by western blotting with anti‐PGK1 or anti‐Flag antibody on the precipitates and lysates, as indicated. B) Reciprocal immunoprecipitation (IP) was performed on cell lysates from HONE‐1 cells overexpressing TMEM52B‐P18 or TMEM52B‐P20 and control cells, by precipitating with anti‐PGK1, followed by western blotting with anti‐TMEM52B or anti‐PGK1 antibody on the precipitates and lysates, as indicated. C) The effects of TMEM52B‐P18 and TMEM52B‐P20 on the phosphorylation of AKT depend on PGK1. HONE‐1 cells were transfected with siRNA control or PGK1 siRNA sequences, followed by the transfection of control, TMEM52B‐P18 or TMEM52B‐P20 plasmids. Western blotting was performed to estimate the phosphorylation of AKT at S473 and T308 sites with β‐tubulin as the loading control. D) Cell viability and proliferation of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression, assessed by CCK‐8. E) Cloning of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression. F,G) Cell migration and invasion of HONE‐1 cells with PGK1 silencing followed by TMEM52B‐P18 or TMEM52B‐P20 overexpression, assessed by transwell assays. Scale bar, 100 µm. Data were represented as mean ±SD, n ≥ 3; ns, no significance; * p < 0.05, ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test (E‐G) and two‐way ANOVA (D).

Techniques: Control, Immunoprecipitation, Western Blot, Transfection, Over Expression, CCK-8 Assay, Clone Assay, Migration, Two Tailed Test

Plasma membrane‐associated TMEM52B‐P20 markedly promotes NPC metastasis. A) Schematic diagram of P20 mutants. B) Western blotting to determine the influence of TMEM52B‐P20 mutants on the protein levels of E‐cadherin, N‐cadherin, and vimentin in HONE‐1 cells. C,D) The effects of TMEM52B‐P20 mutants that dissociated TMEM52B‐P20 from the plasma membrane on the migratory (C) and invasive (D) capabilities of HONE‐1 cells, assessed by transwell assays. Scale bar, 100 µm. E) TMEM52B interacts with cell membrane protein. Cell lysates from HONE‐1 cells transfected with control, TMEM52B‐P18, TMEM52B‐P20, or TMEM52B‐P20 mutant plasmids were immunoprecipitated with anti‐GFP to pull down TMEM52B‐P18 and TMEM52B‐P20, followed by western blotting with anti‐E‐cadherin or anti‐GFP antibody on the precipitates and lysates, as indicated. F) Co‐localization of E‐cadherin with GFP‐P20 but not GFP‐P18 or GFP‐P20 mutants by immunostaining analysis. Scale bar, 10 µm. G) TMEM52B‐P20 increases the ubiquitination level of E‐cadherin. Cell lysates from HONE‐1 cells transfected with Flag‐E‐cadherin, HA‐Ub, and TMEM52B plasmids were immunoprecipitated with anti‐Flag to pull down ubiquitinated E‐cadherin, followed by western blotting with anti‐Flag, anti‐GFP or anti‐HA antibody on the precipitates and lysates, as indicated. H) TMEM52B‐P20 promotes the interaction of E‐cadherin with NEDD4. Cell lysates from HONE‐1 cells transfected with GFP‐E‐cadherin, HA‐NEDD4, and TMEM52B plasmids were immunoprecipitated with anti‐GFP to pull down HA‐NEDD4, followed by western blotting with anti‐Flag, anti‐GFP or anti‐HA antibody on the precipitates and lysates, as indicated. Data were represented as mean ±SD, n = 5, ** p <0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: Plasma membrane‐associated TMEM52B‐P20 markedly promotes NPC metastasis. A) Schematic diagram of P20 mutants. B) Western blotting to determine the influence of TMEM52B‐P20 mutants on the protein levels of E‐cadherin, N‐cadherin, and vimentin in HONE‐1 cells. C,D) The effects of TMEM52B‐P20 mutants that dissociated TMEM52B‐P20 from the plasma membrane on the migratory (C) and invasive (D) capabilities of HONE‐1 cells, assessed by transwell assays. Scale bar, 100 µm. E) TMEM52B interacts with cell membrane protein. Cell lysates from HONE‐1 cells transfected with control, TMEM52B‐P18, TMEM52B‐P20, or TMEM52B‐P20 mutant plasmids were immunoprecipitated with anti‐GFP to pull down TMEM52B‐P18 and TMEM52B‐P20, followed by western blotting with anti‐E‐cadherin or anti‐GFP antibody on the precipitates and lysates, as indicated. F) Co‐localization of E‐cadherin with GFP‐P20 but not GFP‐P18 or GFP‐P20 mutants by immunostaining analysis. Scale bar, 10 µm. G) TMEM52B‐P20 increases the ubiquitination level of E‐cadherin. Cell lysates from HONE‐1 cells transfected with Flag‐E‐cadherin, HA‐Ub, and TMEM52B plasmids were immunoprecipitated with anti‐Flag to pull down ubiquitinated E‐cadherin, followed by western blotting with anti‐Flag, anti‐GFP or anti‐HA antibody on the precipitates and lysates, as indicated. H) TMEM52B‐P20 promotes the interaction of E‐cadherin with NEDD4. Cell lysates from HONE‐1 cells transfected with GFP‐E‐cadherin, HA‐NEDD4, and TMEM52B plasmids were immunoprecipitated with anti‐GFP to pull down HA‐NEDD4, followed by western blotting with anti‐Flag, anti‐GFP or anti‐HA antibody on the precipitates and lysates, as indicated. Data were represented as mean ±SD, n = 5, ** p <0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Techniques: Membrane, Western Blot, Transfection, Control, Mutagenesis, Immunoprecipitation, Immunostaining, Two Tailed Test

TMEM52B enhances drug resistance in NPC cells. A) HNE‐1, SUNE‐1 and S18 cells were transfected with small interfering RNA, and after 48 hours the cells were passed and treated with different concentrations of DDP. Cell survival rate was calculated and cell survival curve was drawn. B) HONE‐1, HK‐1 and S18 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20, and after 48 hours the cells were passed and treated with different concentrations of DDP. Cell survival rate was calculated and cell survival curve was drawn. C) HONE‐1 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20, and treated with different concentrations of AKT phosphorylation inhibitor. Cell lysates were detected by western blotting with anti‐Flag, anti‐pAKT S473 or anti‐pAKT T308. D) HONE‐1 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20. 48 hours later the cells were passed and treated with different concentrations of DDP and 20 µm AKTi. Cell survival rate was calculated and cell survival curve was drawn. E‐H. Cell migration and invasion of HONE‐1 cells transfected with TMEM52B‐P18 or TMEM52B‐P20 followed by AKTi treatment, assessed by transwell assays. Scale bar, 100 µm. Data were represented as mean ±SD, n = 6; ns, no significance; ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Journal: Advanced Science

Article Title: TMEM52B Isoforms P18 and P20 Differentially Promote the Oncogenesis and Metastasis of Nasopharyngeal Carcinoma

doi: 10.1002/advs.202402457

Figure Lengend Snippet: TMEM52B enhances drug resistance in NPC cells. A) HNE‐1, SUNE‐1 and S18 cells were transfected with small interfering RNA, and after 48 hours the cells were passed and treated with different concentrations of DDP. Cell survival rate was calculated and cell survival curve was drawn. B) HONE‐1, HK‐1 and S18 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20, and after 48 hours the cells were passed and treated with different concentrations of DDP. Cell survival rate was calculated and cell survival curve was drawn. C) HONE‐1 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20, and treated with different concentrations of AKT phosphorylation inhibitor. Cell lysates were detected by western blotting with anti‐Flag, anti‐pAKT S473 or anti‐pAKT T308. D) HONE‐1 cells were transfected with TMEM52B‐P18 or TMEM52B‐P20. 48 hours later the cells were passed and treated with different concentrations of DDP and 20 µm AKTi. Cell survival rate was calculated and cell survival curve was drawn. E‐H. Cell migration and invasion of HONE‐1 cells transfected with TMEM52B‐P18 or TMEM52B‐P20 followed by AKTi treatment, assessed by transwell assays. Scale bar, 100 µm. Data were represented as mean ±SD, n = 6; ns, no significance; ** p < 0.01, *** p < 0.001. P value calculated by unpaired two‐tailed Student's t test.

Techniques: Transfection, Small Interfering RNA, Western Blot, Migration, Two Tailed Test

Journal:

Article Title: Extracellular Polysaccharides of Rhodococcus rhodochrous S-2 Stimulate the Degradation of Aromatic Components in Crude Oil by Indigenous Marine Bacteria

doi: 10.1128/AEM.68.5.2337-2343.2002

Figure Lengend Snippet: 16S rDNA sequences most closely related to the major bacterial populations detected by DGGE shown in Fig. Fig.4 4 and

Article Snippet: Cultures were withdrawn on days 5, 10, and 15 for DNA extraction. table ft1 table-wrap mode="anchored" t5 TABLE 2. caption a7 Figure Band Closest sequence Accession no. % Identity 4 A5-15 Alcanivorax vorkumensis DSM11573 {"type":"entrez-nucleotide","attrs":{"text":"AF062642","term_id":"4218925","term_text":"AF062642"}} AF062642 100 B5-15 Cycloclasticus pugetii PS-1 {"type":"entrez-nucleotide","attrs":{"text":"U12624","term_id":"639913","term_text":"U12624"}} U12624 100 C5-15 α- Proteobacteria strain KT0221 {"type":"entrez-nucleotide","attrs":{"text":"AF235122","term_id":"9255825","term_text":"AF235122"}} AF235122 100 D5 Cycloclasticus oligotrophus {"type":"entrez-nucleotide","attrs":{"text":"AF148215","term_id":"4927280","term_text":"AF148215"}} AF148215 96 E5 Uncultured bacteria {"type":"entrez-nucleotide","attrs":{"text":"AF268243","term_id":"14090551","term_text":"AF268243"}} AF268243 100 F10 Marinobacter sp. strain MR-6 {"type":"entrez-nucleotide","attrs":{"text":"AF264687","term_id":"8101084","term_text":"AF264687"}} AF264687 99 G Sphingomonas paucimobilis ATCC 29837 {"type":"entrez-nucleotide","attrs":{"text":"U37337","term_id":"1051189","term_text":"U37337"}} U37337 100 5 1 Sphingomonas parapaucimobilis IFO15100 {"type":"entrez-nucleotide","attrs":{"text":"D13724","term_id":"456230","term_text":"D13724"}} D13724 96 5B-1 Sphingomonas sp. strain K101 {"type":"entrez-nucleotide","attrs":{"text":"AJ009706","term_id":"6911689","term_text":"AJ009706"}} AJ009706 99 5B-2 Sphingomonas paucimobilis {"type":"entrez-nucleotide","attrs":{"text":"U20776","term_id":"134034037","term_text":"U20776"}} U20776 97 11B-1 Alteromonas distincta {"type":"entrez-nucleotide","attrs":{"text":"AF043742","term_id":"6652557","term_text":"AF043742"}} AF043742 98 12B-1 Alteromonas distincta {"type":"entrez-nucleotide","attrs":{"text":"AF043742","term_id":"6652557","term_text":"AF043742"}} AF043742 97 14B-1 Cycloclasticus oligotrophus {"type":"entrez-nucleotide","attrs":{"text":"AF148215","term_id":"4927280","term_text":"AF148215"}} AF148215 96 Open in a separate window 16S rDNA sequences most closely related to the major bacterial populations detected by DGGE shown in Fig. and Effects of synthetic surfactants on degradation of AF by marine bacteria.

Techniques: Sequencing

Review

Structured Review

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