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recombinant sm eno protein  (Thermo Fisher)


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    Structured Review

    Thermo Fisher recombinant sm eno protein
    ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). <t>Recombinant</t> Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.
    Recombinant Sm Eno Protein, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+sm+eno+protein/pmc04676649-263-22-43?v=Thermo+Fisher
    Average 95 stars, based on 1 article reviews
    recombinant sm eno protein - by Bioz Stars, 2026-08
    95/100 stars

    Images

    1) Product Images from "Schistosomes Enhance Plasminogen Activation: The Role of Tegumental Enolase"

    Article Title: Schistosomes Enhance Plasminogen Activation: The Role of Tegumental Enolase

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1005335

    ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). Recombinant Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.
    Figure Legend Snippet: ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). Recombinant Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.

    Techniques Used: Expressing, Staining, SDS Page, Bacteria, Western Blot, Recombinant, Purification, Affinity Chromatography, Migration, Generated, Activity Assay, Concentration Assay, Control



    Similar Products

    recombinant sm eno protein  (Thermo Fisher)
    95
    Thermo Fisher recombinant sm eno protein
    ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). <t>Recombinant</t> Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.
    Recombinant Sm Eno Protein, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+sm+eno+protein/pmc04676649-263-22-43?v=Thermo+Fisher
    Average 95 stars, based on 1 article reviews
    recombinant sm eno protein - by Bioz Stars, 2026-08
    95/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). Recombinant Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.

    Journal: PLoS Pathogens

    Article Title: Schistosomes Enhance Plasminogen Activation: The Role of Tegumental Enolase

    doi: 10.1371/journal.ppat.1005335

    Figure Lengend Snippet: ( A ) Heterologous expression of r Sm Eno in E . coli BL21 Star (DE3). Coomassie-stained gel showing SDS-PAGE resolution of lysates of E . coli bacteria harboring pTrcHisB:: Sm Eno before (Gel, left lane) or 4 hours after (Gel, right lane) protein expression induction. The arrow indicates r Sm Eno in the induced lane. In western blot analysis of these lysates probed with monoclonal anti-His tag antibody, a prominent ~50 kDa protein ( Sm Eno) is detected (Western Blot, anti-His, arrow). Recombinant Sm Eno protein was purified from bacterial lysate by immobilized metal affinity chromatography. A single ~50 kDa pure protein ( Sm Eno) is resolved following Coomassie brilliant blue staining of an SDS-PAGE gel and this protein binds anti-ENO antibody, as determined by western blot analysis (right lane, arrow). Positions of migration of molecular mass markers are indicated on the left (kDa). Michaelis-Menten kinetic curve generated using PGA as substrate ( B , catalyzing the forward reaction) or using PEP as substrate ( C , catalyzing the reverse reaction). The apparent Km and Vmax values shown represent the mean +/- SD of three independent experiments. ( D ) Recombinant Sm Eno activity in a buffer system covering the pH range 5.5–9.5. Enzymatic activity is maximal at pH 7.5. ( E ) Impact of divalent ion (Mg 2+ or Ca 2+ , as indicated) concentration on mean r Sm Eno activity (± SD). The highest activity value (at 100 mM Mg 2+ ) was set at 100% and relative activities were calculated and are presented. Significant differences relative to equivalent measurements containing Ca 2+ are denoted by *** for p <0.001. EDTA is Ethylenediaminetetraacetic acid. ( F ) r Sm Eno activity in the presence of increasing concentrations of NaF (white bars) compared to its activity in the absence of inhibitors (set at 100%, black bar). Significant differences relative to the untreated control are denoted by *** for p <0.001. ( G ) Influence of increasing concentrations of mefloquine (MFQ) on r Sm Eno activity (left bars) or on schistosomula lysate enolase activity (right bars). Activity measured in the absence of MFQ was set at 100% and relative activities were calculated. Significant differences relative to the untreated control are denoted by * for p<0.05 and ** for p<0.01. In E-F, bars represent mean relative activity ± SD, n = 3.

    Article Snippet: Four hours later, bacteria were harvested by centrifugation and the cell pellet was resuspended in Bug Buster Lysis buffer (Life Technologies) and recombinant Sm Eno protein (r Sm Eno) was purified by affinity chromatography on a Ni-NTA Sepharose column following the manufacturer’s instructions (Life Technologies).

    Techniques: Expressing, Staining, SDS Page, Bacteria, Western Blot, Recombinant, Purification, Affinity Chromatography, Migration, Generated, Activity Assay, Concentration Assay, Control