enolase 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc enolase 1
    Enolase 1, supplied by Cell Signaling Technology Inc, 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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    enolase 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc enolase 1
    Enolase 1, supplied by Cell Signaling Technology Inc, 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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    α enolase  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α enolase
    3-HT binds to the <t>α-enolase</t> protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.
    α Enolase, supplied by Cell Signaling Technology Inc, 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 "3-Hydroxytanshinone Inhibits the Activity of Hypoxia-Inducible Factor 1-α by Interfering with the Function of α-Enolase in the Glycolytic Pathway"

    Article Title: 3-Hydroxytanshinone Inhibits the Activity of Hypoxia-Inducible Factor 1-α by Interfering with the Function of α-Enolase in the Glycolytic Pathway

    Journal: Molecules

    doi: 10.3390/molecules29102218

    3-HT binds to the α-enolase protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.
    Figure Legend Snippet: 3-HT binds to the α-enolase protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.

    Techniques Used: Inhibition, Activity Assay, Silver Staining, Fast Protein Liquid Chromatography, Injection, SDS Page, Liquid Chromatography with Mass Spectroscopy, Purification, Concentration Assay, Membrane, Incubation, Blocking Assay, SPR Assay, Binding Assay, Enzymatic Assay

    3-HT inhibits the expression of HIF-1α by directly regulating the activity of α-enolase. ( A ) After transfection with siRNA against α-enolase for 2 days, HeLa cells were stimulated with CoCl 2 (200 μM) for 6 h. mRNA expression was measured using real-time PCR. * p < 0.05, *** p < 0.001 versus the control siRNA group. ( B ) After transfection with siRNA against α-enolase for 2 days, the cells were treated with CoCl 2 for 12 h and then lysed using NE-PER Nuclear and Cytoplasmic Extraction reagents. Protein samples were analyzed via Western blotting. Actin was used as the internal control. ( C ) Cells were transfected with siRNA against α-enolase for 2 days and treated with glucose and pyruvate in the presence of CoCl 2 (200 μM) for 6 h. The total RNA was harvested using TRIzol reagent. The mRNA expression was evaluated using real-time PCR. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05 versus the control siRNA group. ( D ) The effect of 3-HT on HIF-1α mRNA expression was measured using real-time PCR under conditions of CoCl 2 (200 μM) or 1% oxygen for 6 h in the presence of either glucose or pyruvate. ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05, ** p < 0.01, *** p < 0.001 versus the positive control. ( E ) The effects of 3-HT on HIF-1α protein expression were evaluated using Western blotting with glucose or pyruvate in the presence of CoCl 2 (200 μM). Actin was used as the internal control.
    Figure Legend Snippet: 3-HT inhibits the expression of HIF-1α by directly regulating the activity of α-enolase. ( A ) After transfection with siRNA against α-enolase for 2 days, HeLa cells were stimulated with CoCl 2 (200 μM) for 6 h. mRNA expression was measured using real-time PCR. * p < 0.05, *** p < 0.001 versus the control siRNA group. ( B ) After transfection with siRNA against α-enolase for 2 days, the cells were treated with CoCl 2 for 12 h and then lysed using NE-PER Nuclear and Cytoplasmic Extraction reagents. Protein samples were analyzed via Western blotting. Actin was used as the internal control. ( C ) Cells were transfected with siRNA against α-enolase for 2 days and treated with glucose and pyruvate in the presence of CoCl 2 (200 μM) for 6 h. The total RNA was harvested using TRIzol reagent. The mRNA expression was evaluated using real-time PCR. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05 versus the control siRNA group. ( D ) The effect of 3-HT on HIF-1α mRNA expression was measured using real-time PCR under conditions of CoCl 2 (200 μM) or 1% oxygen for 6 h in the presence of either glucose or pyruvate. ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05, ** p < 0.01, *** p < 0.001 versus the positive control. ( E ) The effects of 3-HT on HIF-1α protein expression were evaluated using Western blotting with glucose or pyruvate in the presence of CoCl 2 (200 μM). Actin was used as the internal control.

    Techniques Used: Expressing, Activity Assay, Transfection, Real-time Polymerase Chain Reaction, Extraction, Western Blot, Negative Control, Positive Control

    A proposed mechanism detailing the inhibition of α-enolase, which is regulated by AMPK phosphorylation, leading to the attenuation of HIF-1α in HeLa cells by 3-HT.
    Figure Legend Snippet: A proposed mechanism detailing the inhibition of α-enolase, which is regulated by AMPK phosphorylation, leading to the attenuation of HIF-1α in HeLa cells by 3-HT.

    Techniques Used: Inhibition

    neuronspecific enolase nse  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc neuronspecific enolase nse
    Neuronspecific Enolase Nse, supplied by Cell Signaling Technology Inc, 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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    neuron specific enolase nse  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc neuron specific enolase nse
    Neuron Specific Enolase Nse, supplied by Cell Signaling Technology Inc, 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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    enolase 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc enolase 1
    Enolase 1, supplied by Cell Signaling Technology Inc, 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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    alpha enolase  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc alpha enolase
    The ALDH family is collectively important in melanoma. Western blot <t>showing</t> <t>ALDH1A1,</t> 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. <t>Alpha-enolase</t> served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
    Alpha Enolase, supplied by Cell Signaling Technology Inc, 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 "Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent"

    Article Title: Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent

    Journal: Molecular cancer therapeutics

    doi: 10.1158/1535-7163.MCT-19-0360

    The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
    Figure Legend Snippet: The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).

    Techniques Used: Western Blot, Expressing, Over Expression, MTS Assay, Negative Control, Inhibition

    alpha enolase  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc alpha enolase
    The ALDH family is collectively important in melanoma. Western blot <t>showing</t> <t>ALDH1A1,</t> 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. <t>Alpha-enolase</t> served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
    Alpha Enolase, supplied by Cell Signaling Technology Inc, 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 "Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent"

    Article Title: Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent

    Journal: Molecular cancer therapeutics

    doi: 10.1158/1535-7163.MCT-19-0360

    The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
    Figure Legend Snippet: The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).

    Techniques Used: Western Blot, Expressing, Over Expression, MTS Assay, Negative Control, Inhibition

    anti enolase 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti enolase 1
    Anti Enolase 1, supplied by Cell Signaling Technology Inc, 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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    enolase 1  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc enolase 1
    Enolase 1, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc enolase 1
    Enolase 1, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc α enolase
    3-HT binds to the <t>α-enolase</t> protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.
    α Enolase, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc neuronspecific enolase nse
    3-HT binds to the <t>α-enolase</t> protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.
    Neuronspecific Enolase Nse, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc neuron specific enolase nse
    3-HT binds to the <t>α-enolase</t> protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.
    Neuron Specific Enolase Nse, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc alpha enolase
    The ALDH family is collectively important in melanoma. Western blot <t>showing</t> <t>ALDH1A1,</t> 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. <t>Alpha-enolase</t> served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
    Alpha Enolase, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc anti enolase 1
    The ALDH family is collectively important in melanoma. Western blot <t>showing</t> <t>ALDH1A1,</t> 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. <t>Alpha-enolase</t> served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).
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    3-HT binds to the α-enolase protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.

    Journal: Molecules

    Article Title: 3-Hydroxytanshinone Inhibits the Activity of Hypoxia-Inducible Factor 1-α by Interfering with the Function of α-Enolase in the Glycolytic Pathway

    doi: 10.3390/molecules29102218

    Figure Lengend Snippet: 3-HT binds to the α-enolase protein, resulting in the inhibition of its enzymatic activity. ( A ) Silver staining of biotinyl-3-HT. For fast protein liquid chromatography, biotinyl-3-HT was injected into a 1 mL streptavidin column. After washing, 30 mg of protein was injected. After further washing, each 0.5 mL fraction was eluted. SDS-PAGE was performed using a 15% gel with 25 μL loading, followed by silver staining and LC-MS/MS. ( B ) Dotting assay of 3-HT. Purified enolase protein was prepared. Each concentration of enolase was spotted onto a nitrocellulose membrane, which was then incubated at 4 °C for 15 min. After washing twice with TBST, a 5% bovine serum albumin (BSA) in TBST was used as a blocking buffer for 2 h. The enolase dots were then treated with either anti-biotin compounds or anti-enolase antibodies in 5% BSA for 4 h. Following three washes, anti-biotin-HRP or anti-goat-HRP was applied as a secondary antibody with 5% BSA for 2 h. ( C ) Surface plasmon resonance (SPR) analysis of 3-HT binding to α-enolase. Biotinyl-3-HT was immobilized on a chip, and enolase was injected into the flow cells. ( D ) Enolase enzymatic assay for 3-HT. Purified α-enolase was mixed with DMSO or 3-HT. The reaction was detected at 340 nm over 10 min at 30-s intervals using a multifunctional microplate reader.

    Article Snippet: Antibodies against p-AMPK, AMPK, and α-enolase were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Inhibition, Activity Assay, Silver Staining, Fast Protein Liquid Chromatography, Injection, SDS Page, Liquid Chromatography with Mass Spectroscopy, Purification, Concentration Assay, Membrane, Incubation, Blocking Assay, SPR Assay, Binding Assay, Enzymatic Assay

    3-HT inhibits the expression of HIF-1α by directly regulating the activity of α-enolase. ( A ) After transfection with siRNA against α-enolase for 2 days, HeLa cells were stimulated with CoCl 2 (200 μM) for 6 h. mRNA expression was measured using real-time PCR. * p < 0.05, *** p < 0.001 versus the control siRNA group. ( B ) After transfection with siRNA against α-enolase for 2 days, the cells were treated with CoCl 2 for 12 h and then lysed using NE-PER Nuclear and Cytoplasmic Extraction reagents. Protein samples were analyzed via Western blotting. Actin was used as the internal control. ( C ) Cells were transfected with siRNA against α-enolase for 2 days and treated with glucose and pyruvate in the presence of CoCl 2 (200 μM) for 6 h. The total RNA was harvested using TRIzol reagent. The mRNA expression was evaluated using real-time PCR. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05 versus the control siRNA group. ( D ) The effect of 3-HT on HIF-1α mRNA expression was measured using real-time PCR under conditions of CoCl 2 (200 μM) or 1% oxygen for 6 h in the presence of either glucose or pyruvate. ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05, ** p < 0.01, *** p < 0.001 versus the positive control. ( E ) The effects of 3-HT on HIF-1α protein expression were evaluated using Western blotting with glucose or pyruvate in the presence of CoCl 2 (200 μM). Actin was used as the internal control.

    Journal: Molecules

    Article Title: 3-Hydroxytanshinone Inhibits the Activity of Hypoxia-Inducible Factor 1-α by Interfering with the Function of α-Enolase in the Glycolytic Pathway

    doi: 10.3390/molecules29102218

    Figure Lengend Snippet: 3-HT inhibits the expression of HIF-1α by directly regulating the activity of α-enolase. ( A ) After transfection with siRNA against α-enolase for 2 days, HeLa cells were stimulated with CoCl 2 (200 μM) for 6 h. mRNA expression was measured using real-time PCR. * p < 0.05, *** p < 0.001 versus the control siRNA group. ( B ) After transfection with siRNA against α-enolase for 2 days, the cells were treated with CoCl 2 for 12 h and then lysed using NE-PER Nuclear and Cytoplasmic Extraction reagents. Protein samples were analyzed via Western blotting. Actin was used as the internal control. ( C ) Cells were transfected with siRNA against α-enolase for 2 days and treated with glucose and pyruvate in the presence of CoCl 2 (200 μM) for 6 h. The total RNA was harvested using TRIzol reagent. The mRNA expression was evaluated using real-time PCR. # p < 0.05, ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05 versus the control siRNA group. ( D ) The effect of 3-HT on HIF-1α mRNA expression was measured using real-time PCR under conditions of CoCl 2 (200 μM) or 1% oxygen for 6 h in the presence of either glucose or pyruvate. ## p < 0.01, ### p < 0.001 versus the negative control; * p < 0.05, ** p < 0.01, *** p < 0.001 versus the positive control. ( E ) The effects of 3-HT on HIF-1α protein expression were evaluated using Western blotting with glucose or pyruvate in the presence of CoCl 2 (200 μM). Actin was used as the internal control.

    Article Snippet: Antibodies against p-AMPK, AMPK, and α-enolase were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Expressing, Activity Assay, Transfection, Real-time Polymerase Chain Reaction, Extraction, Western Blot, Negative Control, Positive Control

    A proposed mechanism detailing the inhibition of α-enolase, which is regulated by AMPK phosphorylation, leading to the attenuation of HIF-1α in HeLa cells by 3-HT.

    Journal: Molecules

    Article Title: 3-Hydroxytanshinone Inhibits the Activity of Hypoxia-Inducible Factor 1-α by Interfering with the Function of α-Enolase in the Glycolytic Pathway

    doi: 10.3390/molecules29102218

    Figure Lengend Snippet: A proposed mechanism detailing the inhibition of α-enolase, which is regulated by AMPK phosphorylation, leading to the attenuation of HIF-1α in HeLa cells by 3-HT.

    Article Snippet: Antibodies against p-AMPK, AMPK, and α-enolase were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Inhibition

    The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).

    Journal: Molecular cancer therapeutics

    Article Title: Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent

    doi: 10.1158/1535-7163.MCT-19-0360

    Figure Lengend Snippet: The ALDH family is collectively important in melanoma. Western blot showing ALDH1A1, 2, and 3A1 expression levels in normal human fibroblasts (FF2441), melanocytes (NHEM), radial growth phase (RGP), vertical growth phase (VGP), and metastatic melanoma cell lines. ALDH expression in general increased during disease progression and was not dependent on BRAF mutational status. Alpha-enolase served as the loading control (A). Data from the TCGA database showing slightly better survival with ALDH1A1 and 2 overexpression (B) and worse survival with ALDH3A1 overexpression (C) in patients with melanoma. The data are available through the UCSC Xena Cancer Browser. Individual siRNA knockdown of ALDH1A1, 2, and 3A1 did not significantly reduce the survival of UACC 903 cells after 72 hours in an MTS assay. siRNA to BRAF and ALDH18A1 served as positive controls. Scrambled siRNA served as the negative control (D). siRNA knockdown of ALDH1A1, 2, 3A1, 18A1, and BRAF in UACC 903 cells was confirmed via Western blot. Alpha-enolase served as loading control (E). Pharmacologic inhibition of ALDH1A1, 2, and 3A1 using ALDH isoform–specific inhibitors (Cpd 3, CVT10216, and CB7, respectively), and the multi-ALDH isoform inhibitor, DEAB, revealed multi-ALDH isoform inhibition was most effective in inhibiting UACC 903 cell survival (F).

    Article Snippet: Blots were probed with antibodies according to each supplier’s recommendations: antibodies to cleaved PARP and LC3B from Cell Signaling Technology; alpha-enolase, ALDH1A1, 2, 3A1, 18A1, BRAF, and secondary antibodies conjugated with horseradish peroxidase from Santa Cruz Biotechnology.

    Techniques: Western Blot, Expressing, Over Expression, MTS Assay, Negative Control, Inhibition