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porcine brain arp2 3 complex  (Cytoskeleton Inc)


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    Cytoskeleton Inc porcine brain arp2 3 complex
    Actin filament network assembly on lipid-coated beads with CP, V-1, and CBR126. Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by the addition of 100 <t>nM</t> <t>Arp2/3</t> complex, 5 μM profilin-actin, and 50 nM CP for 30 min ( top row ). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead ( second row ). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations of CBR126 inhibited actin growth (row labeled 2000 nM). CP, capping protein; CBR, CP-binding region.
    Porcine Brain Arp2 3 Complex, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 96/100, based on 221 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/arp2+3+protein+complex/pmc13208823-226-0-5?v=Cytoskeleton+Inc
    Average 96 stars, based on 221 article reviews
    porcine brain arp2 3 complex - by Bioz Stars, 2026-07
    96/100 stars

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    1) Product Images from "CARMIL membrane-binding domain regulates capping protein and actin assembly"

    Article Title: CARMIL membrane-binding domain regulates capping protein and actin assembly

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2026.111484

    Actin filament network assembly on lipid-coated beads with CP, V-1, and CBR126. Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by the addition of 100 nM Arp2/3 complex, 5 μM profilin-actin, and 50 nM CP for 30 min ( top row ). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead ( second row ). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations of CBR126 inhibited actin growth (row labeled 2000 nM). CP, capping protein; CBR, CP-binding region.
    Figure Legend Snippet: Actin filament network assembly on lipid-coated beads with CP, V-1, and CBR126. Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by the addition of 100 nM Arp2/3 complex, 5 μM profilin-actin, and 50 nM CP for 30 min ( top row ). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead ( second row ). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations of CBR126 inhibited actin growth (row labeled 2000 nM). CP, capping protein; CBR, CP-binding region.

    Techniques Used: Generated, Labeling, Binding Assay

    Membrane-binding domain (MB) effects on CP activity. A , His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 μM profilin-actin, 50 nM CP, and 500 nM V-1 (30-min time points) but to a lesser extent than His-CBR126 wt. B - E , three data sets are plotted as different colors and shapes . The data analyzed are from experiments with an optimal concentration of His-CBR, one that produced the highest numbers of beads with asymmetric actin growth for each data set. The horizontal black bar is the median, and p values are calculated from a Mann-Whitney nonparametric analysis. The following parameters were measured and plotted: B , the area of brightest fluorescence near the bead surface; C , circularity of the region of brightest fluorescence near the bead surface; D , the total area of fluorescence, including the diffuse cloud surrounding the beads, and E , the total fluorescence of the actin network. CP, capping protein; CBR, CP-binding region.
    Figure Legend Snippet: Membrane-binding domain (MB) effects on CP activity. A , His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 μM profilin-actin, 50 nM CP, and 500 nM V-1 (30-min time points) but to a lesser extent than His-CBR126 wt. B - E , three data sets are plotted as different colors and shapes . The data analyzed are from experiments with an optimal concentration of His-CBR, one that produced the highest numbers of beads with asymmetric actin growth for each data set. The horizontal black bar is the median, and p values are calculated from a Mann-Whitney nonparametric analysis. The following parameters were measured and plotted: B , the area of brightest fluorescence near the bead surface; C , circularity of the region of brightest fluorescence near the bead surface; D , the total area of fluorescence, including the diffuse cloud surrounding the beads, and E , the total fluorescence of the actin network. CP, capping protein; CBR, CP-binding region.

    Techniques Used: Membrane, Binding Assay, Activity Assay, Concentration Assay, Produced, MANN-WHITNEY, Fluorescence

    Model of regulatory cycles for CP actin capping. 1 , CP bound to V-1 in the cytoplasm is inactive. 2 , CP/V-1 binding to CARMIL promotes V-1 dissociation. 3 , Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5 , Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose/leaky” capper. 6 , Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface. CP, capping protein.
    Figure Legend Snippet: Model of regulatory cycles for CP actin capping. 1 , CP bound to V-1 in the cytoplasm is inactive. 2 , CP/V-1 binding to CARMIL promotes V-1 dissociation. 3 , Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5 , Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose/leaky” capper. 6 , Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface. CP, capping protein.

    Techniques Used: Binding Assay



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    Actin filament network assembly on lipid-coated beads with CP, V-1, and CBR126. Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by the addition of 100 nM Arp2/3 complex, 5 μM profilin-actin, and 50 nM CP for 30 min ( top row ). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead ( second row ). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations of CBR126 inhibited actin growth (row labeled 2000 nM). CP, capping protein; CBR, CP-binding region.

    Journal: The Journal of Biological Chemistry

    Article Title: CARMIL membrane-binding domain regulates capping protein and actin assembly

    doi: 10.1016/j.jbc.2026.111484

    Figure Lengend Snippet: Actin filament network assembly on lipid-coated beads with CP, V-1, and CBR126. Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by the addition of 100 nM Arp2/3 complex, 5 μM profilin-actin, and 50 nM CP for 30 min ( top row ). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead ( second row ). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations of CBR126 inhibited actin growth (row labeled 2000 nM). CP, capping protein; CBR, CP-binding region.

    Article Snippet: Porcine brain Arp2/3 complex from cytoskeleton (Cat. No. RP01P) was reconstituted per manufacturer instructions and used within 1 month.

    Techniques: Generated, Labeling, Binding Assay

    Membrane-binding domain (MB) effects on CP activity. A , His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 μM profilin-actin, 50 nM CP, and 500 nM V-1 (30-min time points) but to a lesser extent than His-CBR126 wt. B - E , three data sets are plotted as different colors and shapes . The data analyzed are from experiments with an optimal concentration of His-CBR, one that produced the highest numbers of beads with asymmetric actin growth for each data set. The horizontal black bar is the median, and p values are calculated from a Mann-Whitney nonparametric analysis. The following parameters were measured and plotted: B , the area of brightest fluorescence near the bead surface; C , circularity of the region of brightest fluorescence near the bead surface; D , the total area of fluorescence, including the diffuse cloud surrounding the beads, and E , the total fluorescence of the actin network. CP, capping protein; CBR, CP-binding region.

    Journal: The Journal of Biological Chemistry

    Article Title: CARMIL membrane-binding domain regulates capping protein and actin assembly

    doi: 10.1016/j.jbc.2026.111484

    Figure Lengend Snippet: Membrane-binding domain (MB) effects on CP activity. A , His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 μM profilin-actin, 50 nM CP, and 500 nM V-1 (30-min time points) but to a lesser extent than His-CBR126 wt. B - E , three data sets are plotted as different colors and shapes . The data analyzed are from experiments with an optimal concentration of His-CBR, one that produced the highest numbers of beads with asymmetric actin growth for each data set. The horizontal black bar is the median, and p values are calculated from a Mann-Whitney nonparametric analysis. The following parameters were measured and plotted: B , the area of brightest fluorescence near the bead surface; C , circularity of the region of brightest fluorescence near the bead surface; D , the total area of fluorescence, including the diffuse cloud surrounding the beads, and E , the total fluorescence of the actin network. CP, capping protein; CBR, CP-binding region.

    Article Snippet: Porcine brain Arp2/3 complex from cytoskeleton (Cat. No. RP01P) was reconstituted per manufacturer instructions and used within 1 month.

    Techniques: Membrane, Binding Assay, Activity Assay, Concentration Assay, Produced, MANN-WHITNEY, Fluorescence

    Model of regulatory cycles for CP actin capping. 1 , CP bound to V-1 in the cytoplasm is inactive. 2 , CP/V-1 binding to CARMIL promotes V-1 dissociation. 3 , Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5 , Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose/leaky” capper. 6 , Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface. CP, capping protein.

    Journal: The Journal of Biological Chemistry

    Article Title: CARMIL membrane-binding domain regulates capping protein and actin assembly

    doi: 10.1016/j.jbc.2026.111484

    Figure Lengend Snippet: Model of regulatory cycles for CP actin capping. 1 , CP bound to V-1 in the cytoplasm is inactive. 2 , CP/V-1 binding to CARMIL promotes V-1 dissociation. 3 , Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5 , Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose/leaky” capper. 6 , Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface. CP, capping protein.

    Article Snippet: Porcine brain Arp2/3 complex from cytoskeleton (Cat. No. RP01P) was reconstituted per manufacturer instructions and used within 1 month.

    Techniques: Binding Assay