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porcine brain arp2 3 complex  (Cytoskeleton Inc)


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    Structured Review

    Cytoskeleton Inc porcine brain arp2 3 complex
    Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by 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 inhibited actin growth (row labeled 2000 nM).
    Porcine Brain Arp2 3 Complex, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 96/100, based on 177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/porcine brain arp2 3 complex/product/Cytoskeleton Inc
    Average 96 stars, based on 177 article reviews
    porcine brain arp2 3 complex - by Bioz Stars, 2026-03
    96/100 stars

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    1) Product Images from "Biochemical Functions of the Membrane-Binding Domain of CARMIL"

    Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

    Journal: bioRxiv

    doi: 10.64898/2026.01.05.697744

    Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by 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 inhibited actin growth (row labeled 2000 nM).
    Figure Legend Snippet: Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by 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 inhibited actin growth (row labeled 2000 nM).

    Techniques Used: Generated, Labeling

    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-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.
    Figure Legend Snippet: 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-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.

    Techniques Used:

    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.
    Figure Legend Snippet: 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.

    Techniques Used: Binding Assay



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    Image Search Results


    Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by 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 inhibited actin growth (row labeled 2000 nM).

    Journal: bioRxiv

    Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

    doi: 10.64898/2026.01.05.697744

    Figure Lengend Snippet: Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by 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 inhibited actin growth (row labeled 2000 nM).

    Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

    Techniques: Generated, Labeling

    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-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.

    Journal: bioRxiv

    Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

    doi: 10.64898/2026.01.05.697744

    Figure Lengend Snippet: 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-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.

    Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

    Techniques:

    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.

    Journal: bioRxiv

    Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

    doi: 10.64898/2026.01.05.697744

    Figure Lengend Snippet: 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.

    Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

    Techniques: Binding Assay