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cdc42 purified proteins  (Cytoskeleton Inc)


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    Structured Review

    Cytoskeleton Inc cdc42 purified proteins
    A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or <t>CDC42</t> with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.
    Cdc42 Purified Proteins, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 90/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cdc42 purified proteins/product/Cytoskeleton Inc
    Average 90 stars, based on 21 article reviews
    cdc42 purified proteins - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "A Rac-specific competitive inhibitor of guanine nucleotide binding reduces metastasis in triple-negative breast cancer"

    Article Title: A Rac-specific competitive inhibitor of guanine nucleotide binding reduces metastasis in triple-negative breast cancer

    Journal: Cell Reports Medicine

    doi: 10.1016/j.xcrm.2025.102233

    A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or CDC42 with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.
    Figure Legend Snippet: A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or CDC42 with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.

    Techniques Used: Activation Assay, SPR Assay, Binding Assay, Purification, Fluorescence, Control, Western Blot, Expressing



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    cdc42 purified proteins  (Cytoskeleton Inc)
    90
    Cytoskeleton Inc cdc42 purified proteins
    A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or <t>CDC42</t> with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.
    Cdc42 Purified Proteins, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cdc42 purified proteins/product/Cytoskeleton Inc
    Average 90 stars, based on 1 article reviews
    cdc42 purified proteins - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or CDC42 with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.

    Journal: Cell Reports Medicine

    Article Title: A Rac-specific competitive inhibitor of guanine nucleotide binding reduces metastasis in triple-negative breast cancer

    doi: 10.1016/j.xcrm.2025.102233

    Figure Lengend Snippet: A41 selectively impairs RAC protein activation (A) Representative surface plasmon resonance (SPR) sensograms of binding of immobilized RHOA or CDC42 with indicated increasing concentrations of A41 ( N > 3). (B) Effect of A41 on GEF-stimulated RAC2, RHOG, RHOA, and CDC42 nucleotide exchange. Purified small G proteins were pre-loaded with GDP and then nucleotide exchange was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM) ( N = 3). K obs is expressed as mean ± SEM. ∗ p < 0.001 vs. control. (C) Effect of A41 on RAC1 G30S activation. RAC1 G30S activation was monitored by the increase in fluorescence following mant-GTP binding in the absence and presence of A41 (5 μM). The GEF TRIO was used to induce nucleotide exchange ( N = 3). Data are expressed as mean ± SEM. (D) Immunoblot analysis and associated quantification of RAC-GTP level and total RAC expression in NIH-3T3 fibroblasts expressing RAC wild-type (RAC1 WT) or RAC1 oncomutants (RAC1 P29S and RAC1b) in the absence (Ctrl) and presence of A41 (10 μM). RAC activation was measured as the ratio of RAC-GTP to total RAC and expressed relative to Ctrl condition. Data are presented as mean ± SEM. ∗∗∗ p < 0.001 vs. controls.

    Article Snippet: RAC1, RHOA and CDC42 purified proteins (respectively RH01, RC01 and CD01, Cytoskeleton) were diluted to 5 μg/mL in Na + acetate buffer (pH 5.0) and injected into sensor chip CM5 (GE Healthcare) in a Biacore T200 (GE Healthcare) that was activated with NHS/EDC buffer.

    Techniques: Activation Assay, SPR Assay, Binding Assay, Purification, Fluorescence, Control, Western Blot, Expressing