3c protease prescission Search Results


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  • 99
    Millipore pre scission protease hrv 3c protease
    Pre Scission Protease Hrv 3c Protease, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pre scission protease hrv 3c protease/product/Millipore
    Average 99 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    pre scission protease hrv 3c protease - by Bioz Stars, 2020-09
    99/100 stars
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    99
    GE Healthcare prescission 3c protease
    Expression and purification of active Src kinases for in vitro kinase assays. (A) Schematic of the GST-PTP1B-His-Δ80Src construct (lacking the first 80 residues of rat full length Src) used to express active Src kinases in E. coli . The <t>3C</t> protease site to produce His-Src is indicated. (B) Coomassie stained SDS–PAGE gels showing the stages of a representative expression and purification of GST-PTP1B-His-Δ80N1-Src (asterisk; left panel) and its cleavage to yield His-Δ80N1-Src (arrow; middle panel). The right panel shows a comparison of purified His-Δ80C-, N1- and N2-Srcs (arrow). (C) Schematic showing the principles of an in vitro Src kinase assay in which GST-peptide substrates contain a tyrosine residue that can be phosphorylated by the Src kinase domain, and a proline rich sequence inserted at the position of PxxP to assess the effect of SH3 domain binding. The primary sequences of the n-Src loops of the C-, N1- and N2-Src SH3 domains are also depicted. (D) Primary sequences of the GST-peptide substrates used in this study. All substrates contain a phosphorylatable tyrosine residue (*). YP1 and YP2 contain canonical Class I and Class II C-Src SH3 domain binding sequences. YA is a mutant of YP1 in which the prolines have been substituted with alanine (underlined) and YL contains the SH2:kinase linker sequence.
    Prescission 3c Protease, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/prescission 3c protease/product/GE Healthcare
    Average 99 stars, based on 138 article reviews
    Price from $9.99 to $1999.99
    prescission 3c protease - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    99
    Millipore prescission protease site
    Expression and purification of active Src kinases for in vitro kinase assays. (A) Schematic of the GST-PTP1B-His-Δ80Src construct (lacking the first 80 residues of rat full length Src) used to express active Src kinases in E. coli . The <t>3C</t> protease site to produce His-Src is indicated. (B) Coomassie stained SDS–PAGE gels showing the stages of a representative expression and purification of GST-PTP1B-His-Δ80N1-Src (asterisk; left panel) and its cleavage to yield His-Δ80N1-Src (arrow; middle panel). The right panel shows a comparison of purified His-Δ80C-, N1- and N2-Srcs (arrow). (C) Schematic showing the principles of an in vitro Src kinase assay in which GST-peptide substrates contain a tyrosine residue that can be phosphorylated by the Src kinase domain, and a proline rich sequence inserted at the position of PxxP to assess the effect of SH3 domain binding. The primary sequences of the n-Src loops of the C-, N1- and N2-Src SH3 domains are also depicted. (D) Primary sequences of the GST-peptide substrates used in this study. All substrates contain a phosphorylatable tyrosine residue (*). YP1 and YP2 contain canonical Class I and Class II C-Src SH3 domain binding sequences. YA is a mutant of YP1 in which the prolines have been substituted with alanine (underlined) and YL contains the SH2:kinase linker sequence.
    Prescission Protease Site, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/prescission protease site/product/Millipore
    Average 99 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    prescission protease site - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    Expression and purification of active Src kinases for in vitro kinase assays. (A) Schematic of the GST-PTP1B-His-Δ80Src construct (lacking the first 80 residues of rat full length Src) used to express active Src kinases in E. coli . The 3C protease site to produce His-Src is indicated. (B) Coomassie stained SDS–PAGE gels showing the stages of a representative expression and purification of GST-PTP1B-His-Δ80N1-Src (asterisk; left panel) and its cleavage to yield His-Δ80N1-Src (arrow; middle panel). The right panel shows a comparison of purified His-Δ80C-, N1- and N2-Srcs (arrow). (C) Schematic showing the principles of an in vitro Src kinase assay in which GST-peptide substrates contain a tyrosine residue that can be phosphorylated by the Src kinase domain, and a proline rich sequence inserted at the position of PxxP to assess the effect of SH3 domain binding. The primary sequences of the n-Src loops of the C-, N1- and N2-Src SH3 domains are also depicted. (D) Primary sequences of the GST-peptide substrates used in this study. All substrates contain a phosphorylatable tyrosine residue (*). YP1 and YP2 contain canonical Class I and Class II C-Src SH3 domain binding sequences. YA is a mutant of YP1 in which the prolines have been substituted with alanine (underlined) and YL contains the SH2:kinase linker sequence.

    Journal: Febs Letters

    Article Title: The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src

    doi: 10.1016/j.febslet.2015.05.033

    Figure Lengend Snippet: Expression and purification of active Src kinases for in vitro kinase assays. (A) Schematic of the GST-PTP1B-His-Δ80Src construct (lacking the first 80 residues of rat full length Src) used to express active Src kinases in E. coli . The 3C protease site to produce His-Src is indicated. (B) Coomassie stained SDS–PAGE gels showing the stages of a representative expression and purification of GST-PTP1B-His-Δ80N1-Src (asterisk; left panel) and its cleavage to yield His-Δ80N1-Src (arrow; middle panel). The right panel shows a comparison of purified His-Δ80C-, N1- and N2-Srcs (arrow). (C) Schematic showing the principles of an in vitro Src kinase assay in which GST-peptide substrates contain a tyrosine residue that can be phosphorylated by the Src kinase domain, and a proline rich sequence inserted at the position of PxxP to assess the effect of SH3 domain binding. The primary sequences of the n-Src loops of the C-, N1- and N2-Src SH3 domains are also depicted. (D) Primary sequences of the GST-peptide substrates used in this study. All substrates contain a phosphorylatable tyrosine residue (*). YP1 and YP2 contain canonical Class I and Class II C-Src SH3 domain binding sequences. YA is a mutant of YP1 in which the prolines have been substituted with alanine (underlined) and YL contains the SH2:kinase linker sequence.

    Article Snippet: Following purification with glutathione resin (Genscript), the His-tagged kinases were cleaved from GST-PTP1B by incubation with PreScission 3C protease (GE Healthcare) at 4 °C overnight.

    Techniques: Expressing, Purification, In Vitro, Construct, Staining, SDS Page, Kinase Assay, Sequencing, Binding Assay, Mutagenesis

    MALDI-TOF MS data of peptides modified by NisB wt (blue) or NisB S88P/D234N (green). (a) CS5D; (b) CS5A; (c) N-terminal part of BDA, which was released by HRV-3C protease from cell surface; (d) N-terminal part of BDD, which was released by HRV-3C protease from cell surface; (e) nisin T2D ; (f) nisin T2E ; (g) nisin(1–22) K12D ; (h) nisin(1–22) K12E ; (i) nisin(1–22) G14D ; (m) nisin(1–22) G14E .

    Journal: ACS Synthetic Biology

    Article Title: High-Throughput Screening for Substrate Specificity-Adapted Mutants of the Nisin Dehydratase NisB

    doi: 10.1021/acssynbio.0c00130

    Figure Lengend Snippet: MALDI-TOF MS data of peptides modified by NisB wt (blue) or NisB S88P/D234N (green). (a) CS5D; (b) CS5A; (c) N-terminal part of BDA, which was released by HRV-3C protease from cell surface; (d) N-terminal part of BDD, which was released by HRV-3C protease from cell surface; (e) nisin T2D ; (f) nisin T2E ; (g) nisin(1–22) K12D ; (h) nisin(1–22) K12E ; (i) nisin(1–22) G14D ; (m) nisin(1–22) G14E .

    Article Snippet: The produced proteins containing the HRV 3C protease recognition sequence (PreScission protease; GE Healthcare) to release the N-terminal part of proteins from the L. lactis cell surface.

    Techniques: Modification