96 well strep tactinxt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences 96 well strep tactinxt coated microplates
    96 Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96 well strep tactinxt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences 96 well strep tactinxt coated microplates
    96 Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96 well strep tactinxt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences 96 well strep tactinxt coated microplates
    96 Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    well strep tactinxt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences well strep tactinxt coated microplates
    Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    microplates  (IBA Lifesciences)


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    IBA Lifesciences microplates
    Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96 well strep tactin xt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences 96 well strep tactin xt coated microplates
    96 Well Strep Tactin Xt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    strep tactin xt  (IBA Lifesciences)


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    IBA Lifesciences strep tactin xt
    Isothiazoles are irreversible SARM1 inhibitors. ( A <t>)</t> <t>SAM-TIR</t> protein immobilized to <t>Strep-Tactin</t> ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.
    Strep Tactin Xt, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/strep tactin xt/product/IBA Lifesciences
    Average 93 stars, based on 1 article reviews
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    1) Product Images from "Pharmacological SARM1 inhibition protects axon structure and function in paclitaxel-induced peripheral neuropathy"

    Article Title: Pharmacological SARM1 inhibition protects axon structure and function in paclitaxel-induced peripheral neuropathy

    Journal: Brain

    doi: 10.1093/brain/awab184

    Isothiazoles are irreversible SARM1 inhibitors. ( A ) SAM-TIR protein immobilized to Strep-Tactin ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.
    Figure Legend Snippet: Isothiazoles are irreversible SARM1 inhibitors. ( A ) SAM-TIR protein immobilized to Strep-Tactin ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.

    Techniques Used: Activity Assay, Inhibition

    strep tactin xt  (IBA Lifesciences)


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    IBA Lifesciences strep tactin xt
    Strep Tactin Xt, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    strep tactin xt  (IBA Lifesciences)


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    IBA Lifesciences strep tactin xt
    ( A ) The permeation pathway formed by tetrameric hDERL1, as determined by HOLE , is shown in the red surface in a cartoon representation of hDERL1 with the protomer close to observers shown as transparent model. ( B ) The intersecting surface of the central tunnel of hDERL1 viewed from the lumen side of the ER membrane. The critical residues at the central tunnel and the interface between protomers are shown in a stick model rendered by elements. The distances between P66 residues at diagonal were measured are and shown in dashed lines. ( C ) The intersecting surface of the central tunnel of hDERL1 viewed parallel to the ER membrane at two angles, with the radius for inner pathway calculated by HOLE shown in the right panel. The Mol. A1 and Mol. B1 were removed for a clear observation in left and middle panels, respectively. ( D ) The substructure in hDERL1 channel. The hDERL1 tetramer is shown in a surface model and sliced perpendicular to the membrane surface. Part of the cap of clipping surfaces was set to transparent to show the composition of lumenal leaf and cytoplasmic leaf. ( E ) NHK dislocation by hDERL1. Left: Immunoblot of lysates of cells expressing NHK (control) and coexpressing NHK with hDERL1-strep [wild type (WT) and mutants]. Right: Immunoblots of <t>Strep-Tactin</t> <t>magnetic</t> beads precipitated material from cells expressing NHK (control) and coexpressing NHK with hDERL1-strep (wild type and mutants).
    Strep Tactin Xt, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1"

    Article Title: The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1

    Journal: Science Advances

    doi: 10.1126/sciadv.abe8591

    ( A ) The permeation pathway formed by tetrameric hDERL1, as determined by HOLE , is shown in the red surface in a cartoon representation of hDERL1 with the protomer close to observers shown as transparent model. ( B ) The intersecting surface of the central tunnel of hDERL1 viewed from the lumen side of the ER membrane. The critical residues at the central tunnel and the interface between protomers are shown in a stick model rendered by elements. The distances between P66 residues at diagonal were measured are and shown in dashed lines. ( C ) The intersecting surface of the central tunnel of hDERL1 viewed parallel to the ER membrane at two angles, with the radius for inner pathway calculated by HOLE shown in the right panel. The Mol. A1 and Mol. B1 were removed for a clear observation in left and middle panels, respectively. ( D ) The substructure in hDERL1 channel. The hDERL1 tetramer is shown in a surface model and sliced perpendicular to the membrane surface. Part of the cap of clipping surfaces was set to transparent to show the composition of lumenal leaf and cytoplasmic leaf. ( E ) NHK dislocation by hDERL1. Left: Immunoblot of lysates of cells expressing NHK (control) and coexpressing NHK with hDERL1-strep [wild type (WT) and mutants]. Right: Immunoblots of Strep-Tactin magnetic beads precipitated material from cells expressing NHK (control) and coexpressing NHK with hDERL1-strep (wild type and mutants).
    Figure Legend Snippet: ( A ) The permeation pathway formed by tetrameric hDERL1, as determined by HOLE , is shown in the red surface in a cartoon representation of hDERL1 with the protomer close to observers shown as transparent model. ( B ) The intersecting surface of the central tunnel of hDERL1 viewed from the lumen side of the ER membrane. The critical residues at the central tunnel and the interface between protomers are shown in a stick model rendered by elements. The distances between P66 residues at diagonal were measured are and shown in dashed lines. ( C ) The intersecting surface of the central tunnel of hDERL1 viewed parallel to the ER membrane at two angles, with the radius for inner pathway calculated by HOLE shown in the right panel. The Mol. A1 and Mol. B1 were removed for a clear observation in left and middle panels, respectively. ( D ) The substructure in hDERL1 channel. The hDERL1 tetramer is shown in a surface model and sliced perpendicular to the membrane surface. Part of the cap of clipping surfaces was set to transparent to show the composition of lumenal leaf and cytoplasmic leaf. ( E ) NHK dislocation by hDERL1. Left: Immunoblot of lysates of cells expressing NHK (control) and coexpressing NHK with hDERL1-strep [wild type (WT) and mutants]. Right: Immunoblots of Strep-Tactin magnetic beads precipitated material from cells expressing NHK (control) and coexpressing NHK with hDERL1-strep (wild type and mutants).

    Techniques Used: Western Blot, Expressing, Magnetic Beads

    96 well strep tactinxt coated microplates  (IBA Lifesciences)


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    IBA Lifesciences 96 well strep tactinxt coated microplates
    96 Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    IBA Lifesciences 96 well strep tactinxt coated microplates
    96 Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    IBA Lifesciences well strep tactinxt coated microplates
    Well Strep Tactinxt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    IBA Lifesciences microplates
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    IBA Lifesciences 96 well strep tactin xt coated microplates
    96 Well Strep Tactin Xt Coated Microplates, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/96 well strep tactin xt coated microplates/product/IBA Lifesciences
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    IBA Lifesciences strep tactin xt
    Isothiazoles are irreversible SARM1 inhibitors. ( A <t>)</t> <t>SAM-TIR</t> protein immobilized to <t>Strep-Tactin</t> ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.
    Strep Tactin Xt, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/strep tactin xt/product/IBA Lifesciences
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    Isothiazoles are irreversible SARM1 inhibitors. ( A ) SAM-TIR protein immobilized to Strep-Tactin ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.

    Journal: Brain

    Article Title: Pharmacological SARM1 inhibition protects axon structure and function in paclitaxel-induced peripheral neuropathy

    doi: 10.1093/brain/awab184

    Figure Lengend Snippet: Isothiazoles are irreversible SARM1 inhibitors. ( A ) SAM-TIR protein immobilized to Strep-Tactin ® XT plates was treated with DSRM-3716, compound 4 or compound 9 for 2 h and enzymatic activity was measured either immediately ( t = 0), or plates were rinsed and assayed after 10 min ( t = 10) or 60 min ( t = 60) post removal of the compounds. Substantial loss of inhibition was observed with the reversible SARM1 inhibitor DSRM-3716 ( left ). In contrast, inhibition with compound 4 ( middle ) and compound 9 ( right ) was completely maintained after 60 min in the absence of compound, consistent with irreversible inhibition of the enzyme. ( B ) DRG mouse cultures were treated for 3 h with 10 µM of the reversible SARM1 inhibitor DSRM-3716 or 10 µM each of compounds 4, 9 and 10. Compounds were removed from the cultures and a subset of cultures had DSRM-3716 replaced immediately after rinsing (continuous). Axons were subjected to axotomy and examined at the times indicated below the bars (in hours). Whereas protection by DSRM-3716 was completely lost by compound removal at the 16-h time point, compounds, 4, 9 and 10 maintained axonal protection at 72 h. ANOVA with Holm–Sidak post hoc F (11,36) = 10.49, P < 0.0001, mean ± SEM; control n = 4. ns, not significant; ** P < 0.01; **** P < 0.0001. ( C ) DRG mouse cultures were exposed to a 3-h pulse of 10-µM compound 4 or 10-µM compound 9 and compounds were removed from the cultures. The interval between removal of the compound and axotomy defines the chase interval. At the completion of the chase interval indicated below the bars, axons were subjected to axotomy and axonal protection was examined after 16 h. Almost complete axonal protection was maintained after a chase period of 24 h. The extent of axonal protection progressively decreased with longer intervals between compound removal and axotomy. Two-way ANOVA with Holm–Sidak post hoc F (3,24) = 71.81, P < 0.0001, mean ± SEM; n = 4. * P < 0.05; ** P < 0.01; **** P < 0.0001.

    Article Snippet: A modified version of this assay was used to incubate SAM-TIR lysate to Strep-Tactin ® XT-coated plates (IBA) to capture the Strep-tag moiety in the recombinant SARM1 construct.

    Techniques: Activity Assay, Inhibition