k lactis gg799  (New England Biolabs)


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    K lactis GG799 Competent Cells
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    K lactis GG799 Competent Cells 5 rxns
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    c1001s
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    New England Biolabs k lactis gg799
    K lactis GG799 Competent Cells
    K lactis GG799 Competent Cells 5 rxns
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    Images

    1) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    2) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    3) Product Images from "A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis"

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.00542-19

    Gluc expression and glucose consumption during culturing of strains containing hybrid promoter-Gluc constructs. K. lactis GG799 cells harboring P GAP1 -Gluc, P ICL1 -Gluc, P 1000 -Gluc, P 350 -Gluc, and P 125 -Gluc expression constructs were grown in YDFM containing glucose in bioreactors. Shown are (A) luciferase activity (RLU/100,000) and cell growth (OD 600 ) relative to hours of culturing, and (B) glucose consumption (%) and cell growth (OD 600 ) relative to hours of culturing. P 1000 -Gluc showed constitutive Gluc expression higher than that of P ICL1 -Gluc or P GAP1 -Gluc. P 350 -Gluc showed Gluc expression only after glucose had been consumed from the culture medium. No Gluc expression was observed with P 125 -Gluc. ND represents the glucose detection limit (
    Figure Legend Snippet: Gluc expression and glucose consumption during culturing of strains containing hybrid promoter-Gluc constructs. K. lactis GG799 cells harboring P GAP1 -Gluc, P ICL1 -Gluc, P 1000 -Gluc, P 350 -Gluc, and P 125 -Gluc expression constructs were grown in YDFM containing glucose in bioreactors. Shown are (A) luciferase activity (RLU/100,000) and cell growth (OD 600 ) relative to hours of culturing, and (B) glucose consumption (%) and cell growth (OD 600 ) relative to hours of culturing. P 1000 -Gluc showed constitutive Gluc expression higher than that of P ICL1 -Gluc or P GAP1 -Gluc. P 350 -Gluc showed Gluc expression only after glucose had been consumed from the culture medium. No Gluc expression was observed with P 125 -Gluc. ND represents the glucose detection limit (

    Techniques Used: Expressing, Construct, Luciferase, Activity Assay

    Gaussia luciferase (A) or α- l -fucosidase (B) expression in K. lactis in response to different promoters and carbon sources. For each strain, the average protein production from five individual cultures, each inoculated with a single transformant, is shown. Cells were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C. Ethanol was added to “glucose + ethanol” cultures after 24 h. Protein production at 48 h was determined by normalizing the activity of the reporter protein (RLU for luciferase or OD 405 for α- l -fucosidase) to the corresponding cell density (OD 600 ) of each culture. Cultures of the wild-type K. lactis GG799 strain were used as negative controls. Error bars represent the standard deviation of the mean of five different cultures.
    Figure Legend Snippet: Gaussia luciferase (A) or α- l -fucosidase (B) expression in K. lactis in response to different promoters and carbon sources. For each strain, the average protein production from five individual cultures, each inoculated with a single transformant, is shown. Cells were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C. Ethanol was added to “glucose + ethanol” cultures after 24 h. Protein production at 48 h was determined by normalizing the activity of the reporter protein (RLU for luciferase or OD 405 for α- l -fucosidase) to the corresponding cell density (OD 600 ) of each culture. Cultures of the wild-type K. lactis GG799 strain were used as negative controls. Error bars represent the standard deviation of the mean of five different cultures.

    Techniques Used: Luciferase, Expressing, Activity Assay, Standard Deviation

    Gaussia luciferase expression using the P ICL1 -P GAP1 fusion promoters in response to different carbon sources. (A) Diagrams of promoters P ICL1 , P GAP1 , P 1000 , and P 350 . The region between nucleotides −690 and −811 upstream from the ICL1 translation start site contains two carbon source-responsive elements (CSRE; shown in dark gray). A series of promoters was created by fusing the regulatory portion of P ICL1 to progressively shorter regions of the P GAP1 promoter relative to the GAP1 translation start site (i.e., P 1000 , P 500 , P 450 , P 400 , P 350 , P 220 , P 125 , and P 74 ). Shown in panel A, P 350 contains 350 nucleotides immediately upstream of the GAP1 translation start site fused to the P ICL1 regulatory fragment. (B) Average protein production from 10 individual strains harboring each hybrid promoter fused to DNA encoding Gaussia luciferase (Gluc). Control strains where four biological replicates were analyzed are indicated by the # symbol. All cultures were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C, after which Gluc activity (RLU) was normalized to the cell density (OD 600 ) for each culture. Cultures of wild-type K. lactis GG799 cells were used as negative controls. Error bars represent the standard deviation from the mean.
    Figure Legend Snippet: Gaussia luciferase expression using the P ICL1 -P GAP1 fusion promoters in response to different carbon sources. (A) Diagrams of promoters P ICL1 , P GAP1 , P 1000 , and P 350 . The region between nucleotides −690 and −811 upstream from the ICL1 translation start site contains two carbon source-responsive elements (CSRE; shown in dark gray). A series of promoters was created by fusing the regulatory portion of P ICL1 to progressively shorter regions of the P GAP1 promoter relative to the GAP1 translation start site (i.e., P 1000 , P 500 , P 450 , P 400 , P 350 , P 220 , P 125 , and P 74 ). Shown in panel A, P 350 contains 350 nucleotides immediately upstream of the GAP1 translation start site fused to the P ICL1 regulatory fragment. (B) Average protein production from 10 individual strains harboring each hybrid promoter fused to DNA encoding Gaussia luciferase (Gluc). Control strains where four biological replicates were analyzed are indicated by the # symbol. All cultures were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C, after which Gluc activity (RLU) was normalized to the cell density (OD 600 ) for each culture. Cultures of wild-type K. lactis GG799 cells were used as negative controls. Error bars represent the standard deviation from the mean.

    Techniques Used: Luciferase, Expressing, Activity Assay, Standard Deviation

    4) Product Images from "A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis"

    Article Title: A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis

    Journal: Fems Yeast Research

    doi: 10.1111/j.1567-1364.2010.00703.x

    Secretion of human interferon Hy3 by protease-deficient strains. (a) Western blot analysis of recombinant Hy3 present in SCM derived from strain GG799 (wt) (± an expression vector) and each protease mutant. (b, c) Analysis of Hy3 secreted by the Kluyveromyces lactis Δ yps1 mutant grown to high cell density in a bioreactor. Hy3 secreted after 22.5 and 40.5 h of fermentation was visualized by SDS-PAGE separation of SCM and either Coomassie blue staining (b) or Western blotting (c). SCM from GG799 cells not expressing Hy3 was analyzed as a negative control. In all panels, arrows indicate intact Hy3 protein and M represents a molecular weight marker. In (a) and (c), the asterisk denotes a proteolytic product of Hy3.
    Figure Legend Snippet: Secretion of human interferon Hy3 by protease-deficient strains. (a) Western blot analysis of recombinant Hy3 present in SCM derived from strain GG799 (wt) (± an expression vector) and each protease mutant. (b, c) Analysis of Hy3 secreted by the Kluyveromyces lactis Δ yps1 mutant grown to high cell density in a bioreactor. Hy3 secreted after 22.5 and 40.5 h of fermentation was visualized by SDS-PAGE separation of SCM and either Coomassie blue staining (b) or Western blotting (c). SCM from GG799 cells not expressing Hy3 was analyzed as a negative control. In all panels, arrows indicate intact Hy3 protein and M represents a molecular weight marker. In (a) and (c), the asterisk denotes a proteolytic product of Hy3.

    Techniques Used: Western Blot, Recombinant, Derivative Assay, Expressing, Plasmid Preparation, Mutagenesis, SDS Page, Staining, Negative Control, Molecular Weight, Marker

    5) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    6) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    7) Product Images from "Establishing the Yeast Kluyveromyces lactis as an Expression Host for Production of the Saposin-Like Domain of the Aspartic Protease Cirsin"

    Article Title: Establishing the Yeast Kluyveromyces lactis as an Expression Host for Production of the Saposin-Like Domain of the Aspartic Protease Cirsin

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.03151-13

    Cirsin PSI fused to the α-MF leader sequence is efficiently integrated into the K. lactis genome and secreted into culture medium. (A) Schematic representation of the α-MF_PSI(His) 6 (top) and α-MF_PSI(N86S)(His) 6 (bottom) fusion proteins. Both sequences comprise the α-MF preprodomain sequence and a hexahistidine tag. The two putative N-glycosylation sites in the α-MF leader sequence (NGT and NTT) are indicated. A putative N-glycosylation site (NET) is present in the α-MF_PSI(His) 6 sequence, while in the construct α-MF_PSI(N86S)(His) 6 , this glycosylation site is mutated (N86S). (B) Confirmation by PCR of integration of the expression cassettes into the K. lactis genome. The numbers correspond to the selected clones and “c” to the amplification product using genomic DNA from untransformed K. lactis strain GG799 (negative control). (Top) α-MF_PSI(His) 6 . (Bottom) α-MF_PSI(N86S)(His) 6 . (C) Western blot analysis of recombinant cirsin PSI expression/secretion into culture media with an anti-His antibody. The numbers above the gels correspond to selected clones shown in panel B, and the lane marked with a c corresponds to the analysis of the culture medium of untransformed K. lactis GG799 cells (negative control). (Left) α-MF_PSI(His) 6 transformants. (Right) α-MF_PSI(N86S)(His) 6 transformants.
    Figure Legend Snippet: Cirsin PSI fused to the α-MF leader sequence is efficiently integrated into the K. lactis genome and secreted into culture medium. (A) Schematic representation of the α-MF_PSI(His) 6 (top) and α-MF_PSI(N86S)(His) 6 (bottom) fusion proteins. Both sequences comprise the α-MF preprodomain sequence and a hexahistidine tag. The two putative N-glycosylation sites in the α-MF leader sequence (NGT and NTT) are indicated. A putative N-glycosylation site (NET) is present in the α-MF_PSI(His) 6 sequence, while in the construct α-MF_PSI(N86S)(His) 6 , this glycosylation site is mutated (N86S). (B) Confirmation by PCR of integration of the expression cassettes into the K. lactis genome. The numbers correspond to the selected clones and “c” to the amplification product using genomic DNA from untransformed K. lactis strain GG799 (negative control). (Top) α-MF_PSI(His) 6 . (Bottom) α-MF_PSI(N86S)(His) 6 . (C) Western blot analysis of recombinant cirsin PSI expression/secretion into culture media with an anti-His antibody. The numbers above the gels correspond to selected clones shown in panel B, and the lane marked with a c corresponds to the analysis of the culture medium of untransformed K. lactis GG799 cells (negative control). (Left) α-MF_PSI(His) 6 transformants. (Right) α-MF_PSI(N86S)(His) 6 transformants.

    Techniques Used: Sequencing, Construct, Polymerase Chain Reaction, Expressing, Clone Assay, Amplification, Negative Control, Western Blot, Recombinant

    8) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    9) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    10) Product Images from "Characterization of a Nucleus-Encoded Chitinase from the Yeast Kluyveromyces lactis"

    Article Title: Characterization of a Nucleus-Encoded Chitinase from the Yeast Kluyveromyces lactis

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.71.6.2862-2869.2005

    (A) K. lactis Δ cts1 cells do not secrete KlCts1p. Proteins in spent culture medium from wild-type GG799 (WT) and Δ cts1 K. lactis cells were incubated with chitin beads. Bound proteins were eluted by boiling and were detected by α-ChBD
    Figure Legend Snippet: (A) K. lactis Δ cts1 cells do not secrete KlCts1p. Proteins in spent culture medium from wild-type GG799 (WT) and Δ cts1 K. lactis cells were incubated with chitin beads. Bound proteins were eluted by boiling and were detected by α-ChBD

    Techniques Used: Incubation

    Identification of a secreted 85-kDa K. lactis chitin-binding protein. Secreted proteins in 10 μl of K. lactis GG799 spent culture medium (after 96 h of growth) were separated by SDS-PAGE and screened for the presence of a chitin-binding domain
    Figure Legend Snippet: Identification of a secreted 85-kDa K. lactis chitin-binding protein. Secreted proteins in 10 μl of K. lactis GG799 spent culture medium (after 96 h of growth) were separated by SDS-PAGE and screened for the presence of a chitin-binding domain

    Techniques Used: Binding Assay, SDS Page

    Enzymatic properties of secreted KlCts1p. (A) Substrate preferences of KlCts1p and ScCts1p. Spent culture media from cultures of K. lactis GG799 and S. cerevisiae BY4741 cells were incubated with 50 μM 4MU-GlcNAc 3 (Tri) (black bars) and with 50
    Figure Legend Snippet: Enzymatic properties of secreted KlCts1p. (A) Substrate preferences of KlCts1p and ScCts1p. Spent culture media from cultures of K. lactis GG799 and S. cerevisiae BY4741 cells were incubated with 50 μM 4MU-GlcNAc 3 (Tri) (black bars) and with 50

    Techniques Used: Incubation

    11) Product Images from "Kluyveromyces lactis LAC4 Promoter Variants That Lack Function in Bacteria but Retain Full Function in K. lactis"

    Article Title: Kluyveromyces lactis LAC4 Promoter Variants That Lack Function in Bacteria but Retain Full Function in K. lactis

    Journal:

    doi: 10.1128/AEM.71.11.7092-7098.2005

    Activity of secreted enterokinase in the spent culture medium of K. lactis cells containing integrated pKLAC1-EK L . Seven K. lactis strains harboring pKLAC1-EK L and wild-type GG799 cells were grown in YPGal medium for 48 h. Cleared spent culture
    Figure Legend Snippet: Activity of secreted enterokinase in the spent culture medium of K. lactis cells containing integrated pKLAC1-EK L . Seven K. lactis strains harboring pKLAC1-EK L and wild-type GG799 cells were grown in YPGal medium for 48 h. Cleared spent culture

    Techniques Used: Activity Assay

    12) Product Images from "Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis"

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    Journal: Brazilian Journal of Microbiology

    doi: 10.1016/j.bjm.2017.10.001

    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    Figure Legend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Techniques Used: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    Related Articles

    Clone Assay:

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. K. lactis GG799 (New England Biolabs, US) was used as a host system for protein expression, while Escherichia coli DH5α was used as a host system for gene cloning. .. The pGEM-T Easy (Promega, Madison, WI, USA) and pKLAC2 vectors were used for gene cloning in E. coli and for gene expression in K. lactis , respectively.

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. K. lactis GG799 (New England Biolabs, US) was used as a host system for protein expression, while Escherichia coli DH5α was used as a host system for gene cloning. .. The pGEM-T Easy (Promega, Madison, WI, USA) and pKLAC2 vectors were used for gene cloning in E. coli and for gene expression in K. lactis , respectively.

    Selection:

    Article Title: A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis
    Article Snippet: .. Construction of protease-deficient strains After its assembly by PCR, 2 μg of a gene disruption DNA fragment was introduced into K. lactis GG799 competent cells as described by the manufacturer (New England Biolabs) followed by selection of transformants by growth on YCB agar medium supplemented with 5 mM acetamide for no more than 3 days at 30 °C. .. Successful disruption of a target chromosomal locus was assessed by whole-cell PCR (see previous section).

    Construct:

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. Expression of the endoglucanase gene from A. fumigatus DBiNU-1 in K. lactis GG799 The expression vector pKLAC2-Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The expression vector pKLAC2- Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Purification:

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis
    Article Snippet: .. For expression in yeast, a purified linearized expression cassette (0.1 μg) was introduced into K. lactis GG799 competent cells, as described by the manufacturer (New England Biolabs). .. Transformants were selected by growth on nitrogen-free yeast carbon base (YCB) agar medium (New England Biolabs) supplemented with 5 mM acetamide for 3 to 4 days at 30°C.

    Expressing:

    Article Title: Establishing the Yeast Kluyveromyces lactis as an Expression Host for Production of the Saposin-Like Domain of the Aspartic Protease Cirsin
    Article Snippet: .. The K. lactis GG799 commercial strain (New England BioLabs) was used as the host for PSI expression. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The transformation of the expression cassette into K. lactis GG799 was performed using lithium acetate with the heat shock method. .. To integrate the cloned endoglucanase gene into the LAC4 locus of the K. lactis chromosome, the expression cassette pKLAC2-Cel7 was linearized with Bst XI before transformation.

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. K. lactis GG799 (New England Biolabs, US) was used as a host system for protein expression, while Escherichia coli DH5α was used as a host system for gene cloning. .. The pGEM-T Easy (Promega, Madison, WI, USA) and pKLAC2 vectors were used for gene cloning in E. coli and for gene expression in K. lactis , respectively.

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. Expression of the endoglucanase gene from A. fumigatus DBiNU-1 in K. lactis GG799 The expression vector pKLAC2-Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The expression vector pKLAC2- Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. K. lactis GG799 (New England Biolabs, US) was used as a host system for protein expression, while Escherichia coli DH5α was used as a host system for gene cloning. .. The pGEM-T Easy (Promega, Madison, WI, USA) and pKLAC2 vectors were used for gene cloning in E. coli and for gene expression in K. lactis , respectively.

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis
    Article Snippet: .. For expression in yeast, a purified linearized expression cassette (0.1 μg) was introduced into K. lactis GG799 competent cells, as described by the manufacturer (New England Biolabs). .. Transformants were selected by growth on nitrogen-free yeast carbon base (YCB) agar medium (New England Biolabs) supplemented with 5 mM acetamide for 3 to 4 days at 30°C.

    Transformation Assay:

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The transformation of the expression cassette into K. lactis GG799 was performed using lithium acetate with the heat shock method. .. To integrate the cloned endoglucanase gene into the LAC4 locus of the K. lactis chromosome, the expression cassette pKLAC2-Cel7 was linearized with Bst XI before transformation.

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. Expression of the endoglucanase gene from A. fumigatus DBiNU-1 in K. lactis GG799 The expression vector pKLAC2-Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The expression vector pKLAC2- Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Polymerase Cycling Assembly:

    Article Title: A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis
    Article Snippet: .. Construction of protease-deficient strains After its assembly by PCR, 2 μg of a gene disruption DNA fragment was introduced into K. lactis GG799 competent cells as described by the manufacturer (New England Biolabs) followed by selection of transformants by growth on YCB agar medium supplemented with 5 mM acetamide for no more than 3 days at 30 °C. .. Successful disruption of a target chromosomal locus was assessed by whole-cell PCR (see previous section).

    Plasmid Preparation:

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. Expression of the endoglucanase gene from A. fumigatus DBiNU-1 in K. lactis GG799 The expression vector pKLAC2-Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
    Article Snippet: .. The expression vector pKLAC2- Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section. ..

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    New England Biolabs k lactis gg799
    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. <t>lactis</t> <t>GG799;</t> 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.
    K Lactis Gg799, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Journal: Brazilian Journal of Microbiology

    Article Title: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis

    doi: 10.1016/j.bjm.2017.10.001

    Figure Lengend Snippet: SDS-PAGE and zymogram analysis of the endoglucanase (A) and the purified recombinant endoglucanase (B) from A. fumigatus DBiNU-1. The protein samples (30 μg) were loaded on the gel and subjected to electrophoresis. (A) M, protein marker; 1, the cell-free supernatant from K. lactis GG799; 2, the cell-free supernatant from K. lactis harboring pKLAC2- Cel7 ; 3, zymogram analysis of the endoglucanase after Congo red staining. (B) M, protein marker; 1, crude recombinant endoglucanase; 2, purified recombinant endoglucanase.

    Article Snippet: Expression of the endoglucanase gene from A. fumigatus DBiNU-1 in K. lactis GG799 The expression vector pKLAC2-Cel7 was constructed and transformed into K. lactis GG799, and the transformants were selected using YCB agar medium, as described in the Materials and methods section.

    Techniques: SDS Page, Purification, Recombinant, Electrophoresis, Marker, Staining

    Gluc expression and glucose consumption during culturing of strains containing hybrid promoter-Gluc constructs. K. lactis GG799 cells harboring P GAP1 -Gluc, P ICL1 -Gluc, P 1000 -Gluc, P 350 -Gluc, and P 125 -Gluc expression constructs were grown in YDFM containing glucose in bioreactors. Shown are (A) luciferase activity (RLU/100,000) and cell growth (OD 600 ) relative to hours of culturing, and (B) glucose consumption (%) and cell growth (OD 600 ) relative to hours of culturing. P 1000 -Gluc showed constitutive Gluc expression higher than that of P ICL1 -Gluc or P GAP1 -Gluc. P 350 -Gluc showed Gluc expression only after glucose had been consumed from the culture medium. No Gluc expression was observed with P 125 -Gluc. ND represents the glucose detection limit (

    Journal: Applied and Environmental Microbiology

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis

    doi: 10.1128/AEM.00542-19

    Figure Lengend Snippet: Gluc expression and glucose consumption during culturing of strains containing hybrid promoter-Gluc constructs. K. lactis GG799 cells harboring P GAP1 -Gluc, P ICL1 -Gluc, P 1000 -Gluc, P 350 -Gluc, and P 125 -Gluc expression constructs were grown in YDFM containing glucose in bioreactors. Shown are (A) luciferase activity (RLU/100,000) and cell growth (OD 600 ) relative to hours of culturing, and (B) glucose consumption (%) and cell growth (OD 600 ) relative to hours of culturing. P 1000 -Gluc showed constitutive Gluc expression higher than that of P ICL1 -Gluc or P GAP1 -Gluc. P 350 -Gluc showed Gluc expression only after glucose had been consumed from the culture medium. No Gluc expression was observed with P 125 -Gluc. ND represents the glucose detection limit (

    Article Snippet: For expression in yeast, a purified linearized expression cassette (0.1 μg) was introduced into K. lactis GG799 competent cells, as described by the manufacturer (New England Biolabs).

    Techniques: Expressing, Construct, Luciferase, Activity Assay

    Gaussia luciferase (A) or α- l -fucosidase (B) expression in K. lactis in response to different promoters and carbon sources. For each strain, the average protein production from five individual cultures, each inoculated with a single transformant, is shown. Cells were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C. Ethanol was added to “glucose + ethanol” cultures after 24 h. Protein production at 48 h was determined by normalizing the activity of the reporter protein (RLU for luciferase or OD 405 for α- l -fucosidase) to the corresponding cell density (OD 600 ) of each culture. Cultures of the wild-type K. lactis GG799 strain were used as negative controls. Error bars represent the standard deviation of the mean of five different cultures.

    Journal: Applied and Environmental Microbiology

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis

    doi: 10.1128/AEM.00542-19

    Figure Lengend Snippet: Gaussia luciferase (A) or α- l -fucosidase (B) expression in K. lactis in response to different promoters and carbon sources. For each strain, the average protein production from five individual cultures, each inoculated with a single transformant, is shown. Cells were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C. Ethanol was added to “glucose + ethanol” cultures after 24 h. Protein production at 48 h was determined by normalizing the activity of the reporter protein (RLU for luciferase or OD 405 for α- l -fucosidase) to the corresponding cell density (OD 600 ) of each culture. Cultures of the wild-type K. lactis GG799 strain were used as negative controls. Error bars represent the standard deviation of the mean of five different cultures.

    Article Snippet: For expression in yeast, a purified linearized expression cassette (0.1 μg) was introduced into K. lactis GG799 competent cells, as described by the manufacturer (New England Biolabs).

    Techniques: Luciferase, Expressing, Activity Assay, Standard Deviation

    Gaussia luciferase expression using the P ICL1 -P GAP1 fusion promoters in response to different carbon sources. (A) Diagrams of promoters P ICL1 , P GAP1 , P 1000 , and P 350 . The region between nucleotides −690 and −811 upstream from the ICL1 translation start site contains two carbon source-responsive elements (CSRE; shown in dark gray). A series of promoters was created by fusing the regulatory portion of P ICL1 to progressively shorter regions of the P GAP1 promoter relative to the GAP1 translation start site (i.e., P 1000 , P 500 , P 450 , P 400 , P 350 , P 220 , P 125 , and P 74 ). Shown in panel A, P 350 contains 350 nucleotides immediately upstream of the GAP1 translation start site fused to the P ICL1 regulatory fragment. (B) Average protein production from 10 individual strains harboring each hybrid promoter fused to DNA encoding Gaussia luciferase (Gluc). Control strains where four biological replicates were analyzed are indicated by the # symbol. All cultures were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C, after which Gluc activity (RLU) was normalized to the cell density (OD 600 ) for each culture. Cultures of wild-type K. lactis GG799 cells were used as negative controls. Error bars represent the standard deviation from the mean.

    Journal: Applied and Environmental Microbiology

    Article Title: A Novel Regulated Hybrid Promoter That Permits Autoinduction of Heterologous Protein Expression in Kluyveromyces lactis

    doi: 10.1128/AEM.00542-19

    Figure Lengend Snippet: Gaussia luciferase expression using the P ICL1 -P GAP1 fusion promoters in response to different carbon sources. (A) Diagrams of promoters P ICL1 , P GAP1 , P 1000 , and P 350 . The region between nucleotides −690 and −811 upstream from the ICL1 translation start site contains two carbon source-responsive elements (CSRE; shown in dark gray). A series of promoters was created by fusing the regulatory portion of P ICL1 to progressively shorter regions of the P GAP1 promoter relative to the GAP1 translation start site (i.e., P 1000 , P 500 , P 450 , P 400 , P 350 , P 220 , P 125 , and P 74 ). Shown in panel A, P 350 contains 350 nucleotides immediately upstream of the GAP1 translation start site fused to the P ICL1 regulatory fragment. (B) Average protein production from 10 individual strains harboring each hybrid promoter fused to DNA encoding Gaussia luciferase (Gluc). Control strains where four biological replicates were analyzed are indicated by the # symbol. All cultures were grown in deep-well plates containing YEP medium supplemented with different carbon sources for 48 h at 30°C, after which Gluc activity (RLU) was normalized to the cell density (OD 600 ) for each culture. Cultures of wild-type K. lactis GG799 cells were used as negative controls. Error bars represent the standard deviation from the mean.

    Article Snippet: For expression in yeast, a purified linearized expression cassette (0.1 μg) was introduced into K. lactis GG799 competent cells, as described by the manufacturer (New England Biolabs).

    Techniques: Luciferase, Expressing, Activity Assay, Standard Deviation

    Secretion of human interferon Hy3 by protease-deficient strains. (a) Western blot analysis of recombinant Hy3 present in SCM derived from strain GG799 (wt) (± an expression vector) and each protease mutant. (b, c) Analysis of Hy3 secreted by the Kluyveromyces lactis Δ yps1 mutant grown to high cell density in a bioreactor. Hy3 secreted after 22.5 and 40.5 h of fermentation was visualized by SDS-PAGE separation of SCM and either Coomassie blue staining (b) or Western blotting (c). SCM from GG799 cells not expressing Hy3 was analyzed as a negative control. In all panels, arrows indicate intact Hy3 protein and M represents a molecular weight marker. In (a) and (c), the asterisk denotes a proteolytic product of Hy3.

    Journal: Fems Yeast Research

    Article Title: A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis

    doi: 10.1111/j.1567-1364.2010.00703.x

    Figure Lengend Snippet: Secretion of human interferon Hy3 by protease-deficient strains. (a) Western blot analysis of recombinant Hy3 present in SCM derived from strain GG799 (wt) (± an expression vector) and each protease mutant. (b, c) Analysis of Hy3 secreted by the Kluyveromyces lactis Δ yps1 mutant grown to high cell density in a bioreactor. Hy3 secreted after 22.5 and 40.5 h of fermentation was visualized by SDS-PAGE separation of SCM and either Coomassie blue staining (b) or Western blotting (c). SCM from GG799 cells not expressing Hy3 was analyzed as a negative control. In all panels, arrows indicate intact Hy3 protein and M represents a molecular weight marker. In (a) and (c), the asterisk denotes a proteolytic product of Hy3.

    Article Snippet: Construction of protease-deficient strains After its assembly by PCR, 2 μg of a gene disruption DNA fragment was introduced into K. lactis GG799 competent cells as described by the manufacturer (New England Biolabs) followed by selection of transformants by growth on YCB agar medium supplemented with 5 mM acetamide for no more than 3 days at 30 °C.

    Techniques: Western Blot, Recombinant, Derivative Assay, Expressing, Plasmid Preparation, Mutagenesis, SDS Page, Staining, Negative Control, Molecular Weight, Marker