cn04 a Search Results


rho rac cdc42 activator i  (Cytoskeleton Inc)
96
Cytoskeleton Inc rho rac cdc42 activator i
Mitochondrial elongation occurs downstream of rac1 (A–C) Effect of Rac1 (Rac Inhibitor III; 2 μM) and Rho (Rho inhibitor I, 10 μM) inhibition on mammosphere attachment to fibronectin-coated plates (1 h) (A), formation of F-actin structures (B), and mitochondrial structure (C). Each point represents an independent experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. One-way ANOVA (A), two-way ANOVA (B and C). Representative images in . (D–F) Actin polymerization and mitochondria in mammospheres treated with a Rac activator <t>(Rho/Rac/Cdc42</t> Activator I, 10 μM, 1 h). Quantification of 3 independent experiments for F-actin (E) and for mitochondrial length (F). Each point represents an individual experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. two-sided t test (D), two-way ANOVA (E). Representative images of F-actin (phalloidin, red) and mitochondria (TOM20, cyan) in MDA-MB-231 mammospheres are shown in (F). Scale bars, 10 μm.
Rho Rac Cdc42 Activator I, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cn04+a/Rho+Rac+Cdc42+Activator+I/pmc12997302-363-86-91
Average 96 stars, based on 1 article reviews
rho rac cdc42 activator i - by Bioz Stars, 2026-11
96/100 stars
  Buy from Supplier

Image Search Results


Mitochondrial elongation occurs downstream of rac1 (A–C) Effect of Rac1 (Rac Inhibitor III; 2 μM) and Rho (Rho inhibitor I, 10 μM) inhibition on mammosphere attachment to fibronectin-coated plates (1 h) (A), formation of F-actin structures (B), and mitochondrial structure (C). Each point represents an independent experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. One-way ANOVA (A), two-way ANOVA (B and C). Representative images in . (D–F) Actin polymerization and mitochondria in mammospheres treated with a Rac activator (Rho/Rac/Cdc42 Activator I, 10 μM, 1 h). Quantification of 3 independent experiments for F-actin (E) and for mitochondrial length (F). Each point represents an individual experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. two-sided t test (D), two-way ANOVA (E). Representative images of F-actin (phalloidin, red) and mitochondria (TOM20, cyan) in MDA-MB-231 mammospheres are shown in (F). Scale bars, 10 μm.

Journal: iScience

Article Title: Extracellular matrix signals promote actin-dependent mitochondrial elongation and activity

doi: 10.1016/j.isci.2026.115171

Figure Lengend Snippet: Mitochondrial elongation occurs downstream of rac1 (A–C) Effect of Rac1 (Rac Inhibitor III; 2 μM) and Rho (Rho inhibitor I, 10 μM) inhibition on mammosphere attachment to fibronectin-coated plates (1 h) (A), formation of F-actin structures (B), and mitochondrial structure (C). Each point represents an independent experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. One-way ANOVA (A), two-way ANOVA (B and C). Representative images in . (D–F) Actin polymerization and mitochondria in mammospheres treated with a Rac activator (Rho/Rac/Cdc42 Activator I, 10 μM, 1 h). Quantification of 3 independent experiments for F-actin (E) and for mitochondrial length (F). Each point represents an individual experiment. Bars show the average ±SD. ∗∗∗ p < 0.001. two-sided t test (D), two-way ANOVA (E). Representative images of F-actin (phalloidin, red) and mitochondria (TOM20, cyan) in MDA-MB-231 mammospheres are shown in (F). Scale bars, 10 μm.

Article Snippet: The following proteins were manipulated using chemical inhibitors/activators: F-Actin depolymerization, Cytochalasin D (0.1 μg/mL Sigma Aldrich #C8273); FAK, small-molecule inhibitor PF-573228 (10 μM; Sigma Aldrich #PZ0117); Src kinase, Src Inhibitor-1 (10 μM; Sigma Aldrich #S2075); Rho GTPase, Rho Inhibitor I (C3 Transferase from Clostridium botulinum covalently linked to a cell-penetrating moiety; 10 μM; Cytoskeleton, Inc #CT04-A); Rac GTPase, Rac Inhibitor III (2 μM; MilliporeSigma #55351310 MG); Arp 2/3 complex, CK-666 (10 μM; Sigma Aldrich #182515); Formin, FH2 domain inhibitor SMIFH2 (2 μM; Sigma-Aldrich #344092); Rac activation, Rho/Rac/Cdc42 Activator I (10 μM; Cytoskeleton, Inc #CN04-A).

Techniques: Inhibition