Structured Review

Abcam rabbit monoclonal eno1
Source, application and concentration of antibodies.
Rabbit Monoclonal Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit monoclonal eno1/product/Abcam
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rabbit monoclonal eno1 - by Bioz Stars, 2024-02
86/100 stars

Images

1) Product Images from "Helicase-like transcription factor (HLTF) -deleted CDX/TME model of colorectal cancer increased transcription of oxidative phosphorylation genes and diverted glycolysis to boost S-glutathionylation in lymphatic intravascular metastatic niches"

Article Title: Helicase-like transcription factor (HLTF) -deleted CDX/TME model of colorectal cancer increased transcription of oxidative phosphorylation genes and diverted glycolysis to boost S-glutathionylation in lymphatic intravascular metastatic niches

Journal: PLOS ONE

doi: 10.1371/journal.pone.0291023

Source, application and concentration of antibodies.
Figure Legend Snippet: Source, application and concentration of antibodies.

Techniques Used: Concentration Assay, Recombinant, Plasmid Preparation

Summary of site-specific S-glutathionylation identified by 2D-DIGE MALDI-TOF/TOF mass spectrometry. Pr-SSG in HLTF -/- CDX/TME.
Figure Legend Snippet: Summary of site-specific S-glutathionylation identified by 2D-DIGE MALDI-TOF/TOF mass spectrometry. Pr-SSG in HLTF -/- CDX/TME.

Techniques Used: Mass Spectrometry

eno1 rabbit monoclonal abcam wb  (Danaher Inc)


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    Structured Review

    Danaher Inc eno1 rabbit monoclonal abcam wb
    Eno1 Rabbit Monoclonal Abcam Wb, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/eno1 rabbit monoclonal abcam wb/product/Danaher Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    eno1 rabbit monoclonal abcam wb - by Bioz Stars, 2024-02
    86/100 stars

    Images


    Structured Review

    Abcam rabbit anti eno1 monoclonal antibody
    Photomicrographs showing <t>α-enolase</t> <t>(ENO1)</t> expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive <t>ENO1</t> expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).
    Rabbit Anti Eno1 Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti eno1 monoclonal antibody/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti eno1 monoclonal antibody - by Bioz Stars, 2024-02
    86/100 stars

    Images

    1) Product Images from "Diagnostic value of α-enolase expression and serum α-enolase autoantibody levels in lung cancer"

    Article Title: Diagnostic value of α-enolase expression and serum α-enolase autoantibody levels in lung cancer

    Journal: Jornal Brasileiro de Pneumologia

    doi: 10.1590/S1806-37562016000000241

    Photomicrographs showing α-enolase (ENO1) expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).
    Figure Legend Snippet: Photomicrographs showing α-enolase (ENO1) expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).

    Techniques Used: Expressing, Immunohistochemistry, Staining

    ROC curve showing the sensitivity and specificity of serum α-enolase antibody levels for the diagnosis of lung cancer.
    Figure Legend Snippet: ROC curve showing the sensitivity and specificity of serum α-enolase antibody levels for the diagnosis of lung cancer.

    Techniques Used:


    Structured Review

    Abcam rabbit monoclonal anti eno1
    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, <t>ENO1,</t> and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " width="250" height="auto" />
    Rabbit Monoclonal Anti Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal anti eno1/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit monoclonal anti eno1 - by Bioz Stars, 2024-02
    86/100 stars

    Images

    1) Product Images from "Integrative proteo-transcriptomic and immunophenotyping signatures of HIV-1 elite control phenotype: A cross-talk between glycolysis and HIF signaling"

    Article Title: Integrative proteo-transcriptomic and immunophenotyping signatures of HIV-1 elite control phenotype: A cross-talk between glycolysis and HIF signaling

    Journal: iScience

    doi: 10.1016/j.isci.2021.103607

    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, ENO1, and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " title="... Violin plots representing relative protein quantification of HIF-1α, ENO1, and ENO3 normalized to β-Actin from (H) using ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, ENO1, and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also Figure S2 .

    Techniques Used: Expressing, Functional Assay, Western Blot


    Figure Legend Snippet:

    Techniques Used: Software


    Structured Review

    Abcam anti eno1 rabbit monoclonal antibody
    Anti Eno1 Rabbit Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti eno1 rabbit monoclonal antibody/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti eno1 rabbit monoclonal antibody - by Bioz Stars, 2024-02
    86/100 stars

    Images


    Structured Review

    Abcam monoclonal rabbit anti eno1
    Monoclonal Rabbit Anti Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal rabbit anti eno1/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal rabbit anti eno1 - by Bioz Stars, 2024-02
    86/100 stars

    Images


    Structured Review

    Abcam rabbit anti eno1 monoclonal antibodies
    <t>ENO1</t> expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, <t>α-enolase;</t> AUC, area under the curve.
    Rabbit Anti Eno1 Monoclonal Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti eno1 monoclonal antibodies/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti eno1 monoclonal antibodies - by Bioz Stars, 2024-02
    86/100 stars

    Images

    1) Product Images from "α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis"

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    Journal: Oncology Letters

    doi: 10.3892/ol.2020.12003

    ENO1 expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, α-enolase; AUC, area under the curve.
    Figure Legend Snippet: ENO1 expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, α-enolase; AUC, area under the curve.

    Techniques Used: Expressing

     ENO1  expression in pathological tissues.
    Figure Legend Snippet: ENO1 expression in pathological tissues.

    Techniques Used: Expressing

    Comparison of the serum  anti-ENO1  antibody levels among the three groups of participants [P50 (P25-P75)].
    Figure Legend Snippet: Comparison of the serum anti-ENO1 antibody levels among the three groups of participants [P50 (P25-P75)].

    Techniques Used:

    Validation of the siRNA interference effect on ENO1 expression in liver cancer cells. (A) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (B) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (C) Western blot validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 protein in HepG2 cells in the si-1 and si-2 groups were significantly lower than those in the control group. (D) Western blot validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 protein in Huh7 cells in the si-1 and si-2 groups were significantly lower than those in the control group. **P<0.01; ****P<0.0001. siRNA, small interfering RNA; ENO1, α-enolase; si-1, siRNA interference group 1; si-2, siRNA interference group 2; RT-qPCR, reverse transcription-quantitative PCR.
    Figure Legend Snippet: Validation of the siRNA interference effect on ENO1 expression in liver cancer cells. (A) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (B) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (C) Western blot validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 protein in HepG2 cells in the si-1 and si-2 groups were significantly lower than those in the control group. (D) Western blot validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 protein in Huh7 cells in the si-1 and si-2 groups were significantly lower than those in the control group. **P<0.01; ****P<0.0001. siRNA, small interfering RNA; ENO1, α-enolase; si-1, siRNA interference group 1; si-2, siRNA interference group 2; RT-qPCR, reverse transcription-quantitative PCR.

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot, Small Interfering RNA, Real-time Polymerase Chain Reaction

    Effect of ENO1 siRNA on liver cancer cell proliferation. (A) HepG2 and (B) Huh7 cell proliferation was suppressed after ENO1 siRNA treatment. Results show that 72 h after transfection in the si-1 and si-2 groups, ENO1 siRNA treatment resulted in proliferation inhibition in HepG2 and Huh7 cells. In HepG2 cells, the differences in cell proliferation between the NC and the siRNA-treated groups were statistically significant (P<0.05 vs. si-2 group and P<0.01 vs. si-1 group). Cell proliferation in Huh7 cells was also significantly different. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; si-1, siRNA interference group 1; si-2, siRNA interference group 2; OD, optical density; NC, negative control.
    Figure Legend Snippet: Effect of ENO1 siRNA on liver cancer cell proliferation. (A) HepG2 and (B) Huh7 cell proliferation was suppressed after ENO1 siRNA treatment. Results show that 72 h after transfection in the si-1 and si-2 groups, ENO1 siRNA treatment resulted in proliferation inhibition in HepG2 and Huh7 cells. In HepG2 cells, the differences in cell proliferation between the NC and the siRNA-treated groups were statistically significant (P<0.05 vs. si-2 group and P<0.01 vs. si-1 group). Cell proliferation in Huh7 cells was also significantly different. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; si-1, siRNA interference group 1; si-2, siRNA interference group 2; OD, optical density; NC, negative control.

    Techniques Used: Transfection, Inhibition, Small Interfering RNA, Negative Control

    Effect of ENO1 siRNA on the migration ability of liver cancer cells. (A) Compared with that of the NC group, HepG2 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (B) Gap size was measured using ImageJ software and the ratio of gap size after ENO1 siRNA treatment in HepG2 cells was calculated based on the size of the wound at 0 h. (C) Compared with that of the NC group, Huh7 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (D) Gap size was measured with the ImageJ software and the ratio of gap size after ENO1 siRNA treatment in Huh7 cell was calculated based on the size of the wound at 0 h. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.
    Figure Legend Snippet: Effect of ENO1 siRNA on the migration ability of liver cancer cells. (A) Compared with that of the NC group, HepG2 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (B) Gap size was measured using ImageJ software and the ratio of gap size after ENO1 siRNA treatment in HepG2 cells was calculated based on the size of the wound at 0 h. (C) Compared with that of the NC group, Huh7 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (D) Gap size was measured with the ImageJ software and the ratio of gap size after ENO1 siRNA treatment in Huh7 cell was calculated based on the size of the wound at 0 h. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Techniques Used: Migration, Software, Small Interfering RNA, Negative Control

    Effect of ENO1 siRNA on the invasion and migration abilities of liver cancer cells. Compared with the NC group, the in vitro invasion and migration abilities of (A) HepG2 and (B) Huh7 cells after ENO1 siRNA treatment decreased in the si-1 and si-2 groups, and the differences were statistically significant. Numbers of (C) HepG2 and (D) Huh7 cells were measured with the ImageJ software after ENO1 siRNA treatment. *P<0.05; **P<0.01; ***P<0.001; ****P<0.0001. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.
    Figure Legend Snippet: Effect of ENO1 siRNA on the invasion and migration abilities of liver cancer cells. Compared with the NC group, the in vitro invasion and migration abilities of (A) HepG2 and (B) Huh7 cells after ENO1 siRNA treatment decreased in the si-1 and si-2 groups, and the differences were statistically significant. Numbers of (C) HepG2 and (D) Huh7 cells were measured with the ImageJ software after ENO1 siRNA treatment. *P<0.05; **P<0.01; ***P<0.001; ****P<0.0001. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Techniques Used: Migration, In Vitro, Software, Small Interfering RNA, Negative Control


    Structured Review

    Abcam rabbit anti eno1 monoclonal antibody
    cTnIAAb binds to <t>α-enolase</t> <t>(ENO1)</t> in myocardial cell membrane. a. The concentrated purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography was subjected to SDS-PAGE followed by Coomassie blue staining, which revealed one single band. b. The purified protein from BCG823 cell lysates specifically bound to <t>ENO1</t> mAb, but could not bind to cTnImAb1 again. Left : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could not interact with cTnImAb1 again. Middle : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could specifically bind to ENO1 mAb (51 KDa). Right : Western blotting showing that the non-reduced protein lysates from mouse cardiomyocytes interacted with cTnImAb1 at both 28 kDa and 51 kDa, while the reduced protein lysates interacted with cTnImAb1 only at 28 kDa. c. Immunoblot analysis showed that cTnImAb1 and anti-ENO1 pAb bound to the immunoprecipitation-purified endogenous dimeric ENO1 from cardiomyocytes. Far Left : Mouse cTnImAb1 strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse cTnImAb1 interacted with myocardial cTnI (lines 2 and 5, ~28 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Left : Mouse ENO1 pAb strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse ENO1 pAb interacted with myocardial ENOI (lines 2 and 5, ~47 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Right : Rabbit ENO1 mAb155955 interacted with ENO1 in the input protein sample (lines 2 and 5) as well as the immunoprecipitated endogenous ENO1 by rabbit ENO1 mAb155102 (lines 3 and 6). Rabbit ENO1 mAb155102 also bound to anti rabbit IgG (lines 4 and 7). Far Right : Mouse actin mAb interacted with the actin in the input protein sample (lines 2 and 5). All images are representative of at least 3 independent iterations. d. Identification of FLAG-tagged recombinant wild-type and C389A, C357A, C339A, C119A ENO1 protein expressed in 293 T cells. e. The reaction of recombinant ENO1 protein and 4 point-mutated ENO1 proteins with cTnImAb1 and Anti-ENO1 (non-reducing sample) respectively. Results shown are representative immunoblot analysis of three independent co-immunoprecipitation analysis. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Rabbit Anti Eno1 Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti eno1 monoclonal antibody/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti eno1 monoclonal antibody - by Bioz Stars, 2024-02
    86/100 stars

    Images

    1) Product Images from "Cardiac troponin I autoantibody induces myocardial dysfunction by PTEN signaling activation"

    Article Title: Cardiac troponin I autoantibody induces myocardial dysfunction by PTEN signaling activation

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2019.08.045

    cTnIAAb binds to α-enolase (ENO1) in myocardial cell membrane. a. The concentrated purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography was subjected to SDS-PAGE followed by Coomassie blue staining, which revealed one single band. b. The purified protein from BCG823 cell lysates specifically bound to ENO1 mAb, but could not bind to cTnImAb1 again. Left : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could not interact with cTnImAb1 again. Middle : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could specifically bind to ENO1 mAb (51 KDa). Right : Western blotting showing that the non-reduced protein lysates from mouse cardiomyocytes interacted with cTnImAb1 at both 28 kDa and 51 kDa, while the reduced protein lysates interacted with cTnImAb1 only at 28 kDa. c. Immunoblot analysis showed that cTnImAb1 and anti-ENO1 pAb bound to the immunoprecipitation-purified endogenous dimeric ENO1 from cardiomyocytes. Far Left : Mouse cTnImAb1 strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse cTnImAb1 interacted with myocardial cTnI (lines 2 and 5, ~28 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Left : Mouse ENO1 pAb strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse ENO1 pAb interacted with myocardial ENOI (lines 2 and 5, ~47 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Right : Rabbit ENO1 mAb155955 interacted with ENO1 in the input protein sample (lines 2 and 5) as well as the immunoprecipitated endogenous ENO1 by rabbit ENO1 mAb155102 (lines 3 and 6). Rabbit ENO1 mAb155102 also bound to anti rabbit IgG (lines 4 and 7). Far Right : Mouse actin mAb interacted with the actin in the input protein sample (lines 2 and 5). All images are representative of at least 3 independent iterations. d. Identification of FLAG-tagged recombinant wild-type and C389A, C357A, C339A, C119A ENO1 protein expressed in 293 T cells. e. The reaction of recombinant ENO1 protein and 4 point-mutated ENO1 proteins with cTnImAb1 and Anti-ENO1 (non-reducing sample) respectively. Results shown are representative immunoblot analysis of three independent co-immunoprecipitation analysis. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: cTnIAAb binds to α-enolase (ENO1) in myocardial cell membrane. a. The concentrated purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography was subjected to SDS-PAGE followed by Coomassie blue staining, which revealed one single band. b. The purified protein from BCG823 cell lysates specifically bound to ENO1 mAb, but could not bind to cTnImAb1 again. Left : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could not interact with cTnImAb1 again. Middle : Western blotting showing that the purified protein from BCG823 cell lysates through cTnImAb1-dextran affinity chromatography could specifically bind to ENO1 mAb (51 KDa). Right : Western blotting showing that the non-reduced protein lysates from mouse cardiomyocytes interacted with cTnImAb1 at both 28 kDa and 51 kDa, while the reduced protein lysates interacted with cTnImAb1 only at 28 kDa. c. Immunoblot analysis showed that cTnImAb1 and anti-ENO1 pAb bound to the immunoprecipitation-purified endogenous dimeric ENO1 from cardiomyocytes. Far Left : Mouse cTnImAb1 strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse cTnImAb1 interacted with myocardial cTnI (lines 2 and 5, ~28 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Left : Mouse ENO1 pAb strongly interacted with the unreduced ENO1 dimer (line 6, ~98 kDa) immunoprecipitated by rabbit ENO1 mAb155102, while it weakly interacted with the reduced endogenous ENO1 (line 3, ~47 kDa). Mouse ENO1 pAb interacted with myocardial ENOI (lines 2 and 5, ~47 kDa) as well as the unreduced input protein sample (line 2, ~98 kDa). Right : Rabbit ENO1 mAb155955 interacted with ENO1 in the input protein sample (lines 2 and 5) as well as the immunoprecipitated endogenous ENO1 by rabbit ENO1 mAb155102 (lines 3 and 6). Rabbit ENO1 mAb155102 also bound to anti rabbit IgG (lines 4 and 7). Far Right : Mouse actin mAb interacted with the actin in the input protein sample (lines 2 and 5). All images are representative of at least 3 independent iterations. d. Identification of FLAG-tagged recombinant wild-type and C389A, C357A, C339A, C119A ENO1 protein expressed in 293 T cells. e. The reaction of recombinant ENO1 protein and 4 point-mutated ENO1 proteins with cTnImAb1 and Anti-ENO1 (non-reducing sample) respectively. Results shown are representative immunoblot analysis of three independent co-immunoprecipitation analysis. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Purification, Affinity Chromatography, SDS Page, Staining, Western Blot, Immunoprecipitation, Recombinant

    cTnImAb1 upregulates the expression of ENO1 and induces cardiomyocyte apoptosis, while silencing ENO1 attenuates cTnImAb1–induced cardiomyocyte apoptosis. a & b. cTnImAb1 treatment (0, 25, 50, or 100 μg/ml) for 48 h induced cardiomyocyte apoptosis in a dose-dependent manner as revealed by flow cytometry. a , representative images. b , quantification of 3 independent experiments. * p = .000 (ANOVA analysis). c. cTnImAb1 treatment for 48 h at indicated doses increased Bax, cleaved Caspase3, and caspase8/p18 expression, and decreased Bcl2 expression in a dose-dependent manner as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images of 3 independent experiments. d&e. cTnImAb1 treatment (50 μg/ml) for indicated times induced cardiomyocyte apoptosis in a time-dependent manner as revealed by flow cytometry. d , representative images. e , quantification of 3 independent experiments, * p = .000 (ANOVA analysis). f. cTnImAb1 treatment (50 μg/ml) for indicated times increased Bax, cleaved Caspase3, and caspase8/p18 expression, and decreased Bcl2 expression in a dose-dependent manner as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images of 3 independent experiments. g-i. cTnImAb1 treatment (50 μg/ml) for 48 h increased ENO1 expression of primary cultured cardiomyocytes ( i ) compared with mouse IgG ( g ) and cTnTmAb ( h ) treatments as revealed by immunohistochemistry. Bar = 50 μm. j&k. cTnImAb1 treatment (50 μg/ml) for 48 h increased ENO1 expression compared with mouse IgG treatments as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images ( j ) and quantification by ImageJ-mediated densitometry analysis ( k ) of 3 independent experiments. * p = .000 ( t -test). l&m. Silencing ENO1 attenuated cTnImAb1 (50 μg/ml)-induced cardiomyocyte apoptosis compared with mock-siRNA group. l , Annexin V-PI staining was used for flow cytometric analysis. Representative images are shown. m , Quantification of Annexin-V/PI staining from 3 independent experiments. 24 h * p = .008, 48 h * p = .000 ( t -test). n&o. RNAi-mediated silencing of Eno1 in primary cultured cardiomyocytes significantly reduced the cTnImAb1 (50 μg/ml)-induced cardiomyocyte apoptosis by increasing Bax expression and decreasing Bcl2 expression compared with mock-siRNA group. Representative immunoblot images are shown in n . ImageJ-based quantification of ENO1 (*ENO1-siRNA p = .000, Mock-siRNA p = .000), Bax (*ENO1-siRNA p = .000, Mock-siRNA p = .000), and Bcl2 (*ENO1-siRNA p = .003, Mock-siRNA p = .020) protein expression is shown in o. (ANOVA analysis).
    Figure Legend Snippet: cTnImAb1 upregulates the expression of ENO1 and induces cardiomyocyte apoptosis, while silencing ENO1 attenuates cTnImAb1–induced cardiomyocyte apoptosis. a & b. cTnImAb1 treatment (0, 25, 50, or 100 μg/ml) for 48 h induced cardiomyocyte apoptosis in a dose-dependent manner as revealed by flow cytometry. a , representative images. b , quantification of 3 independent experiments. * p = .000 (ANOVA analysis). c. cTnImAb1 treatment for 48 h at indicated doses increased Bax, cleaved Caspase3, and caspase8/p18 expression, and decreased Bcl2 expression in a dose-dependent manner as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images of 3 independent experiments. d&e. cTnImAb1 treatment (50 μg/ml) for indicated times induced cardiomyocyte apoptosis in a time-dependent manner as revealed by flow cytometry. d , representative images. e , quantification of 3 independent experiments, * p = .000 (ANOVA analysis). f. cTnImAb1 treatment (50 μg/ml) for indicated times increased Bax, cleaved Caspase3, and caspase8/p18 expression, and decreased Bcl2 expression in a dose-dependent manner as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images of 3 independent experiments. g-i. cTnImAb1 treatment (50 μg/ml) for 48 h increased ENO1 expression of primary cultured cardiomyocytes ( i ) compared with mouse IgG ( g ) and cTnTmAb ( h ) treatments as revealed by immunohistochemistry. Bar = 50 μm. j&k. cTnImAb1 treatment (50 μg/ml) for 48 h increased ENO1 expression compared with mouse IgG treatments as revealed by immunoblot analysis. β-actin served as a loading control. Shown are representative images ( j ) and quantification by ImageJ-mediated densitometry analysis ( k ) of 3 independent experiments. * p = .000 ( t -test). l&m. Silencing ENO1 attenuated cTnImAb1 (50 μg/ml)-induced cardiomyocyte apoptosis compared with mock-siRNA group. l , Annexin V-PI staining was used for flow cytometric analysis. Representative images are shown. m , Quantification of Annexin-V/PI staining from 3 independent experiments. 24 h * p = .008, 48 h * p = .000 ( t -test). n&o. RNAi-mediated silencing of Eno1 in primary cultured cardiomyocytes significantly reduced the cTnImAb1 (50 μg/ml)-induced cardiomyocyte apoptosis by increasing Bax expression and decreasing Bcl2 expression compared with mock-siRNA group. Representative immunoblot images are shown in n . ImageJ-based quantification of ENO1 (*ENO1-siRNA p = .000, Mock-siRNA p = .000), Bax (*ENO1-siRNA p = .000, Mock-siRNA p = .000), and Bcl2 (*ENO1-siRNA p = .003, Mock-siRNA p = .020) protein expression is shown in o. (ANOVA analysis).

    Techniques Used: Expressing, Flow Cytometry, Western Blot, Cell Culture, Immunohistochemistry, Staining

    cTnImAb1 treatment increases ENO1 expression followed by activation of PTEN and suppression of Akt signaling in mouse hearts. a. Heat map from PathScan® Akt Signaling Antibody Array kit analysis showing changes in 16 phosphorylated proteins. b & c. Statistical analysis of heat map data in a and volcano plot showing that cTnImAb1 treatment significantly increased PTEN Ser380 phosphorylation in the mouse heart. 1. PTEN Ser380, *p = .023, ( t -test). 2. GSK-3b Ser9, * p = .038, ( t -test). 3. PTEN Ser380, * p = .031 ( t -test). d&e. Immunoblot analysis showed that cTnImAb1 treatment significantly increased ENO1 expression and PTEN Ser380 phosphorylation but suppressed Akt Thr308 phosphorylation. β-actin served as a loading control. e is the statistical analysis of d . ENO1 * p = .002, pPTEN/PTEN/Actin, * p = .003, pAkt/Akt/Actin, * p = .003. (ANOVA analysis). f-h. cTnImAb1 treatment (50 μg/ml) induced changes in ENO1 expression and phosphorylation of PTEN Ser380 and Akt Thr308 at different time points in cultured cardiomyoyctes. cTnImAb1 increased the p-Ser380-PTEN/total PTEN ratio at 8 h but decreased the pThr308-AKT/total Akt ratio at 8–12 h. Mouse IgG treatment did not alter pSer380 PTEN but significantly increased the pThr308-Akt/total Akt ratio at 24–36 h. f shows representative blot images of three independent experiments. g and h represent ImageJ-based densitometry analysis of relative changes in p-Ser380-PTEN/total PTEN ratio ( G, 8 h * p = .020, 12 h * p = .024, t -test) and pThr308-AKT/total Akt ( H , 12 h * p = .018, 24 h * p = .001, 36 h * p = .001, t -test). i-l. Knockdown of ENO1 significantly suppressed cTnImAb1–induced alteration in PTEN/Akt signaling. Cultured cardiomyocytes were transfected with siRNA targeting Eno1 and then subjected to cTnImAb1 treatment (50 μg/ml) for 4–48 h as indicated. Mock-siRNA was used as a control. Depletion of Eno1 suppressed the p-PTEN Ser380/total PTEN ratio and increased the pAkt-Thr308/total Akt ratio at 4, 8, and 12 h, respectively. i shows representative blot images of three independent experiments. j represents ImageJ-based densitometry analysis of relative changes in ENO1 protein levels ( J ,48 h * p = .000, t -test). k and l represent ImageJ-based densitometry analysis of relative changes in p-Ser380-PTEN/total PTEN ratio ( k, 48 h * p = .000, t -test) and pThr308-AKT/total Akt ( l, 6 h * p = .000, 12 h * p = .000, t -test).
    Figure Legend Snippet: cTnImAb1 treatment increases ENO1 expression followed by activation of PTEN and suppression of Akt signaling in mouse hearts. a. Heat map from PathScan® Akt Signaling Antibody Array kit analysis showing changes in 16 phosphorylated proteins. b & c. Statistical analysis of heat map data in a and volcano plot showing that cTnImAb1 treatment significantly increased PTEN Ser380 phosphorylation in the mouse heart. 1. PTEN Ser380, *p = .023, ( t -test). 2. GSK-3b Ser9, * p = .038, ( t -test). 3. PTEN Ser380, * p = .031 ( t -test). d&e. Immunoblot analysis showed that cTnImAb1 treatment significantly increased ENO1 expression and PTEN Ser380 phosphorylation but suppressed Akt Thr308 phosphorylation. β-actin served as a loading control. e is the statistical analysis of d . ENO1 * p = .002, pPTEN/PTEN/Actin, * p = .003, pAkt/Akt/Actin, * p = .003. (ANOVA analysis). f-h. cTnImAb1 treatment (50 μg/ml) induced changes in ENO1 expression and phosphorylation of PTEN Ser380 and Akt Thr308 at different time points in cultured cardiomyoyctes. cTnImAb1 increased the p-Ser380-PTEN/total PTEN ratio at 8 h but decreased the pThr308-AKT/total Akt ratio at 8–12 h. Mouse IgG treatment did not alter pSer380 PTEN but significantly increased the pThr308-Akt/total Akt ratio at 24–36 h. f shows representative blot images of three independent experiments. g and h represent ImageJ-based densitometry analysis of relative changes in p-Ser380-PTEN/total PTEN ratio ( G, 8 h * p = .020, 12 h * p = .024, t -test) and pThr308-AKT/total Akt ( H , 12 h * p = .018, 24 h * p = .001, 36 h * p = .001, t -test). i-l. Knockdown of ENO1 significantly suppressed cTnImAb1–induced alteration in PTEN/Akt signaling. Cultured cardiomyocytes were transfected with siRNA targeting Eno1 and then subjected to cTnImAb1 treatment (50 μg/ml) for 4–48 h as indicated. Mock-siRNA was used as a control. Depletion of Eno1 suppressed the p-PTEN Ser380/total PTEN ratio and increased the pAkt-Thr308/total Akt ratio at 4, 8, and 12 h, respectively. i shows representative blot images of three independent experiments. j represents ImageJ-based densitometry analysis of relative changes in ENO1 protein levels ( J ,48 h * p = .000, t -test). k and l represent ImageJ-based densitometry analysis of relative changes in p-Ser380-PTEN/total PTEN ratio ( k, 48 h * p = .000, t -test) and pThr308-AKT/total Akt ( l, 6 h * p = .000, 12 h * p = .000, t -test).

    Techniques Used: Expressing, Activation Assay, Ab Array, Western Blot, Cell Culture, Transfection

    Graphical mechanism summary: Human cTnIAAb interacts with ENO1 present in the myocardial membrane and induces apoptosis of cultured cardiomyocytes. Human cTnIAAb can trigger cardiomyocyte apoptosis via binding membrane ENO1, increasing ENO1 expression, promoting phosphorylation of PTEN Ser380, and suppressing Akt activity in the mouse model of cTnImAb-induced myocardial injury. This induces the pro-apoptotic Bax and suppresses the anti-apoptotic Bcl2 expression resulting in cardiomyocyte apoptosis.
    Figure Legend Snippet: Graphical mechanism summary: Human cTnIAAb interacts with ENO1 present in the myocardial membrane and induces apoptosis of cultured cardiomyocytes. Human cTnIAAb can trigger cardiomyocyte apoptosis via binding membrane ENO1, increasing ENO1 expression, promoting phosphorylation of PTEN Ser380, and suppressing Akt activity in the mouse model of cTnImAb-induced myocardial injury. This induces the pro-apoptotic Bax and suppresses the anti-apoptotic Bcl2 expression resulting in cardiomyocyte apoptosis.

    Techniques Used: Cell Culture, Binding Assay, Expressing, Activity Assay


    Structured Review

    Abcam rabbit monoclonal anti eno1 antibody
    (A) Both PFK and <t>ENO1</t> enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).
    Rabbit Monoclonal Anti Eno1 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis"

    Article Title: p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

    Journal: Molecular cell

    doi: 10.1016/j.molcel.2018.04.011

    (A) Both PFK and ENO1 enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).
    Figure Legend Snippet: (A) Both PFK and ENO1 enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).

    Techniques Used: Cell Culture, Colorimetric Assay

    Key Resources Table
    Figure Legend Snippet: Key Resources Table

    Techniques Used: Recombinant, shRNA, Clone Assay, Synthesized, Activity Assay, Mutagenesis, Mass Spectrometry, Western Blot, Sequencing, Software


    Structured Review

    Abcam rabbit anti eno1 monoclonal antibody
    Rabbit Anti Eno1 Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit monoclonal eno1
    Source, application and concentration of antibodies.
    Rabbit Monoclonal Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Danaher Inc eno1 rabbit monoclonal abcam wb
    Source, application and concentration of antibodies.
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    Abcam rabbit anti eno1 monoclonal antibody
    Photomicrographs showing <t>α-enolase</t> <t>(ENO1)</t> expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive <t>ENO1</t> expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).
    Rabbit Anti Eno1 Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit monoclonal anti eno1
    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, <t>ENO1,</t> and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " width="250" height="auto" />
    Rabbit Monoclonal Anti Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti eno1 rabbit monoclonal antibody
    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, <t>ENO1,</t> and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " width="250" height="auto" />
    Anti Eno1 Rabbit Monoclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam monoclonal rabbit anti eno1
    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, <t>ENO1,</t> and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " width="250" height="auto" />
    Monoclonal Rabbit Anti Eno1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit anti eno1 monoclonal antibodies
    <t>ENO1</t> expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, <t>α-enolase;</t> AUC, area under the curve.
    Rabbit Anti Eno1 Monoclonal Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit monoclonal anti eno1 antibody
    (A) Both PFK and <t>ENO1</t> enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).
    Rabbit Monoclonal Anti Eno1 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Source, application and concentration of antibodies.

    Journal: PLOS ONE

    Article Title: Helicase-like transcription factor (HLTF) -deleted CDX/TME model of colorectal cancer increased transcription of oxidative phosphorylation genes and diverted glycolysis to boost S-glutathionylation in lymphatic intravascular metastatic niches

    doi: 10.1371/journal.pone.0291023

    Figure Lengend Snippet: Source, application and concentration of antibodies.

    Article Snippet: Rabbit polyclonal HLTF antibody (NBP1-83256) Novus Biologicals (1:100) Rabbit polyclonal CYTB (55090-1-AP) ThermoFisher Scientific (1:50) Rabbit polyclonal PGAM1 (16126-1-AP) ThermoFisher Scientific (1:50) Rabbit polyclonal ANXA1 (71–3400) ThermoFisher Scientific (1:20) Rabbit monoclonal γH2AX-phospho S139 (ab81299) Abcam (1:50) Rabbit monoclonal ENO1 (ab227978) Abcam (1:2,000) Rabbit recombinant monoclonal mouse-specific PDPN (MA5-29742) ThermoFisher Scientific (1:500) , IHC-P: Vector Laboratories RTU Biotinylated Goat Anti-rabbit IgG (H+L) (BP-9100-50).

    Techniques: Concentration Assay, Recombinant, Plasmid Preparation

    Summary of site-specific S-glutathionylation identified by 2D-DIGE MALDI-TOF/TOF mass spectrometry. Pr-SSG in HLTF -/- CDX/TME.

    Journal: PLOS ONE

    Article Title: Helicase-like transcription factor (HLTF) -deleted CDX/TME model of colorectal cancer increased transcription of oxidative phosphorylation genes and diverted glycolysis to boost S-glutathionylation in lymphatic intravascular metastatic niches

    doi: 10.1371/journal.pone.0291023

    Figure Lengend Snippet: Summary of site-specific S-glutathionylation identified by 2D-DIGE MALDI-TOF/TOF mass spectrometry. Pr-SSG in HLTF -/- CDX/TME.

    Article Snippet: Rabbit polyclonal HLTF antibody (NBP1-83256) Novus Biologicals (1:100) Rabbit polyclonal CYTB (55090-1-AP) ThermoFisher Scientific (1:50) Rabbit polyclonal PGAM1 (16126-1-AP) ThermoFisher Scientific (1:50) Rabbit polyclonal ANXA1 (71–3400) ThermoFisher Scientific (1:20) Rabbit monoclonal γH2AX-phospho S139 (ab81299) Abcam (1:50) Rabbit monoclonal ENO1 (ab227978) Abcam (1:2,000) Rabbit recombinant monoclonal mouse-specific PDPN (MA5-29742) ThermoFisher Scientific (1:500) , IHC-P: Vector Laboratories RTU Biotinylated Goat Anti-rabbit IgG (H+L) (BP-9100-50).

    Techniques: Mass Spectrometry

    Photomicrographs showing α-enolase (ENO1) expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).

    Journal: Jornal Brasileiro de Pneumologia

    Article Title: Diagnostic value of α-enolase expression and serum α-enolase autoantibody levels in lung cancer

    doi: 10.1590/S1806-37562016000000241

    Figure Lengend Snippet: Photomicrographs showing α-enolase (ENO1) expression in lung tissue samples (immunohistochemistry using the streptavidin-peroxidase staining method). Positive signs are visualized as yellow or brownish yellow granules. In A and B, adenocarcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In C and D, squamous cell carcinoma tissue samples showing positive ENO1 expression (magnification, ×400 and ×100, respectively). In E and F, pulmonary inflammatory pseudotumor tissue samples showing negative ENO1 expression (magnification, ×400 and ×100, respectively).

    Article Snippet: The reagents used were rabbit anti-ENO1 monoclonal antibody (Abcam Biotechnology Co. Ltd., Cambridge, UK), an immunohistochemistry reagent kit (Maixin, Fuzhou, China) and an ENO1 antibody ELISA reagent kit (HuaAn, Hangzhou, China).

    Techniques: Expressing, Immunohistochemistry, Staining

    ROC curve showing the sensitivity and specificity of serum α-enolase antibody levels for the diagnosis of lung cancer.

    Journal: Jornal Brasileiro de Pneumologia

    Article Title: Diagnostic value of α-enolase expression and serum α-enolase autoantibody levels in lung cancer

    doi: 10.1590/S1806-37562016000000241

    Figure Lengend Snippet: ROC curve showing the sensitivity and specificity of serum α-enolase antibody levels for the diagnosis of lung cancer.

    Article Snippet: The reagents used were rabbit anti-ENO1 monoclonal antibody (Abcam Biotechnology Co. Ltd., Cambridge, UK), an immunohistochemistry reagent kit (Maixin, Fuzhou, China) and an ENO1 antibody ELISA reagent kit (HuaAn, Hangzhou, China).

    Techniques:

    Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, ENO1, and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also <xref ref-type=Figure S2 . " width="100%" height="100%">

    Journal: iScience

    Article Title: Integrative proteo-transcriptomic and immunophenotyping signatures of HIV-1 elite control phenotype: A cross-talk between glycolysis and HIF signaling

    doi: 10.1016/j.isci.2021.103607

    Figure Lengend Snippet: Proteo-transcriptomic integration confirms HIF signaling and glycolysis as unique features of the male EC phenotype Proteo-transcriptomic analysis in HC (n = 9 ), EC (n = 9 ), and VP (n = 9 ). (A) Upset plot describing the number of features detected by each of the sparse partial least squares models. (B) Schematic representation of the derivation of EC-specific proteins. (C) PCA plot representing sample clustering with respect to EC-specific proteins. The first two principal components capturing maximum of variance were used. Data ellipses were drawn at the level of 0.9. (D) Heatmap visualizing quantile normalized and Z-scaled expression pattern of EC-specific proteins. Column annotation represents the cohorts and the different groups used for pairwise comparison. Proteins are hierarchically clustered based on Euclidean distance. (E) Functional analysis results of proteins belonging to cluster 1 in (D). Size of the bubble and the color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (F) Functional analysis results of the proteins belonging to cluster 2 in (D). The bubble size and color gradient are relative to number of features in each pathway and adjusted p value of the enrichment test, respectively. (G) Schematic representation of the proteins belonging to pathways in (F). Circular nodes in red represents upregulated proteins in EC, in relation to HC, and gray color denotes non-significant expression levels. (H) Western blot analysis of HIF target genes identified in (G) for male HC (n = 9 ), and EC (n = 9 ). (I) Violin plots representing relative protein quantification of HIF-1α, ENO1, and ENO3 normalized to β-Actin from (H) using unpaired t test (significance level, p < 0.05) represented with violin plot with mean. See also Figure S2 .

    Article Snippet: Rabbit monoclonal anti-ENO1 [EPR10863(B)] , Abcam , Cat#ab155102.

    Techniques: Expressing, Functional Assay, Western Blot

    Journal: iScience

    Article Title: Integrative proteo-transcriptomic and immunophenotyping signatures of HIV-1 elite control phenotype: A cross-talk between glycolysis and HIF signaling

    doi: 10.1016/j.isci.2021.103607

    Figure Lengend Snippet:

    Article Snippet: Rabbit monoclonal anti-ENO1 [EPR10863(B)] , Abcam , Cat#ab155102.

    Techniques: Software

    ENO1 expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, α-enolase; AUC, area under the curve.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: ENO1 expression in liver cancer tissue and peripheral blood of patients with liver cancer. (A) ENO1 expression in liver cancer tissues (×100). (B) ENO1 was not expressed in benign liver lesions (×100). (C) Serum anti-ENO1 antibody levels in patients with liver cancer were higher than those in patients with benign liver lesions and healthy controls. (D) ENO1 expression in liver cancer tissues (×400). (E) ENO1 was not expressed in benign liver lesion (×400). (F) Receiver operating characteristic curve analysis for liver cancer diagnosis using anti-ENO1 antibody levels. The AUC was 0.741, the sensitivity was 64.3% and the specificity was 85.5%. The red dot represents the cut-off value. **P<0.01; ****P<0.0001 ENO1, α-enolase; AUC, area under the curve.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Expressing

     ENO1  expression in pathological tissues.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: ENO1 expression in pathological tissues.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Expressing

    Comparison of the serum  anti-ENO1  antibody levels among the three groups of participants [P50 (P25-P75)].

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: Comparison of the serum anti-ENO1 antibody levels among the three groups of participants [P50 (P25-P75)].

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques:

    Validation of the siRNA interference effect on ENO1 expression in liver cancer cells. (A) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (B) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (C) Western blot validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 protein in HepG2 cells in the si-1 and si-2 groups were significantly lower than those in the control group. (D) Western blot validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 protein in Huh7 cells in the si-1 and si-2 groups were significantly lower than those in the control group. **P<0.01; ****P<0.0001. siRNA, small interfering RNA; ENO1, α-enolase; si-1, siRNA interference group 1; si-2, siRNA interference group 2; RT-qPCR, reverse transcription-quantitative PCR.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: Validation of the siRNA interference effect on ENO1 expression in liver cancer cells. (A) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (B) RT-qPCR validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 gene in the si-1 and si-2 groups were lower than those in the control group. (C) Western blot validation of the effect of siRNA interference on ENO1 expression in HepG2 cells. The results showed that the relative expression levels of the ENO1 protein in HepG2 cells in the si-1 and si-2 groups were significantly lower than those in the control group. (D) Western blot validation of the effect of siRNA interference on ENO1 expression in Huh7 cells. The results showed that the relative expression levels of the ENO1 protein in Huh7 cells in the si-1 and si-2 groups were significantly lower than those in the control group. **P<0.01; ****P<0.0001. siRNA, small interfering RNA; ENO1, α-enolase; si-1, siRNA interference group 1; si-2, siRNA interference group 2; RT-qPCR, reverse transcription-quantitative PCR.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, Small Interfering RNA, Real-time Polymerase Chain Reaction

    Effect of ENO1 siRNA on liver cancer cell proliferation. (A) HepG2 and (B) Huh7 cell proliferation was suppressed after ENO1 siRNA treatment. Results show that 72 h after transfection in the si-1 and si-2 groups, ENO1 siRNA treatment resulted in proliferation inhibition in HepG2 and Huh7 cells. In HepG2 cells, the differences in cell proliferation between the NC and the siRNA-treated groups were statistically significant (P<0.05 vs. si-2 group and P<0.01 vs. si-1 group). Cell proliferation in Huh7 cells was also significantly different. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; si-1, siRNA interference group 1; si-2, siRNA interference group 2; OD, optical density; NC, negative control.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: Effect of ENO1 siRNA on liver cancer cell proliferation. (A) HepG2 and (B) Huh7 cell proliferation was suppressed after ENO1 siRNA treatment. Results show that 72 h after transfection in the si-1 and si-2 groups, ENO1 siRNA treatment resulted in proliferation inhibition in HepG2 and Huh7 cells. In HepG2 cells, the differences in cell proliferation between the NC and the siRNA-treated groups were statistically significant (P<0.05 vs. si-2 group and P<0.01 vs. si-1 group). Cell proliferation in Huh7 cells was also significantly different. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; si-1, siRNA interference group 1; si-2, siRNA interference group 2; OD, optical density; NC, negative control.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Transfection, Inhibition, Small Interfering RNA, Negative Control

    Effect of ENO1 siRNA on the migration ability of liver cancer cells. (A) Compared with that of the NC group, HepG2 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (B) Gap size was measured using ImageJ software and the ratio of gap size after ENO1 siRNA treatment in HepG2 cells was calculated based on the size of the wound at 0 h. (C) Compared with that of the NC group, Huh7 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (D) Gap size was measured with the ImageJ software and the ratio of gap size after ENO1 siRNA treatment in Huh7 cell was calculated based on the size of the wound at 0 h. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: Effect of ENO1 siRNA on the migration ability of liver cancer cells. (A) Compared with that of the NC group, HepG2 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (B) Gap size was measured using ImageJ software and the ratio of gap size after ENO1 siRNA treatment in HepG2 cells was calculated based on the size of the wound at 0 h. (C) Compared with that of the NC group, Huh7 cell migration after ENO1 siRNA treatment became slower in the si-1 and si-2 groups, and the difference was statistically significant at 48 h after treatment. (D) Gap size was measured with the ImageJ software and the ratio of gap size after ENO1 siRNA treatment in Huh7 cell was calculated based on the size of the wound at 0 h. *P<0.05; **P<0.01. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Migration, Software, Small Interfering RNA, Negative Control

    Effect of ENO1 siRNA on the invasion and migration abilities of liver cancer cells. Compared with the NC group, the in vitro invasion and migration abilities of (A) HepG2 and (B) Huh7 cells after ENO1 siRNA treatment decreased in the si-1 and si-2 groups, and the differences were statistically significant. Numbers of (C) HepG2 and (D) Huh7 cells were measured with the ImageJ software after ENO1 siRNA treatment. *P<0.05; **P<0.01; ***P<0.001; ****P<0.0001. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Journal: Oncology Letters

    Article Title: α-enolase is highly expressed in liver cancer and promotes cancer cell invasion and metastasis

    doi: 10.3892/ol.2020.12003

    Figure Lengend Snippet: Effect of ENO1 siRNA on the invasion and migration abilities of liver cancer cells. Compared with the NC group, the in vitro invasion and migration abilities of (A) HepG2 and (B) Huh7 cells after ENO1 siRNA treatment decreased in the si-1 and si-2 groups, and the differences were statistically significant. Numbers of (C) HepG2 and (D) Huh7 cells were measured with the ImageJ software after ENO1 siRNA treatment. *P<0.05; **P<0.01; ***P<0.001; ****P<0.0001. ENO1, α-enolase; siRNA, small interfering RNA; NC, negative control; si-1, siRNA interference group 1; si-2, siRNA interference group 2.

    Article Snippet: Rabbit anti-ENO1 monoclonal antibodies were purchased from Abcam (cat. no. ab85086) for use in immunohistochemistry and western blotting.

    Techniques: Migration, In Vitro, Software, Small Interfering RNA, Negative Control

    (A) Both PFK and ENO1 enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).

    Journal: Molecular cell

    Article Title: p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

    doi: 10.1016/j.molcel.2018.04.011

    Figure Lengend Snippet: (A) Both PFK and ENO1 enzymes display reduced activities in p300 KO HCT116 cells. WT and p300 KO HCT116 cells were cultured in complete medium. The activities of PFK and ENO1 from total cell lysates were measured using colorimetric assay kits (n=3, *p<0.05, values are expressed as mean ±SEM).

    Article Snippet: Rabbit monoclonal anti-ENO1 antibody (clone {"type":"entrez-protein","attrs":{"text":"EPR10864","term_id":"523376409","term_text":"EPR10864"}} EPR10864 (B)) , Abcam , Cat# ab155955.

    Techniques: Cell Culture, Colorimetric Assay

    Key Resources Table

    Journal: Molecular cell

    Article Title: p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

    doi: 10.1016/j.molcel.2018.04.011

    Figure Lengend Snippet: Key Resources Table

    Article Snippet: Rabbit monoclonal anti-ENO1 antibody (clone {"type":"entrez-protein","attrs":{"text":"EPR10864","term_id":"523376409","term_text":"EPR10864"}} EPR10864 (B)) , Abcam , Cat# ab155955.

    Techniques: Recombinant, shRNA, Clone Assay, Synthesized, Activity Assay, Mutagenesis, Mass Spectrometry, Western Blot, Sequencing, Software