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mouse piezo1 knockout neuro2a  (ATCC)


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    Structured Review

    ATCC mouse piezo1 knockout neuro2a
    (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in <t>N2A</t> <t>Piezo1</t> −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .
    Mouse Piezo1 Knockout Neuro2a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 4142 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+piezo1+knockout+neuro2a/pmc12951647-25-0-8?v=ATCC
    Average 99 stars, based on 4142 article reviews
    mouse piezo1 knockout neuro2a - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade"

    Article Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade

    Journal: Cell reports

    doi: 10.1016/j.celrep.2025.116878

    (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in N2A Piezo1 −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .
    Figure Legend Snippet: (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in N2A Piezo1 −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .

    Techniques Used: Patch Clamp, Transfection, MANN-WHITNEY, Cryo-EM Sample Prep

    (A) Lateral view of PEZO-1 isoform G highlighting the cap and central regions. Arrows indicate the spring linker. The cap width is denoted above the respective model. The pore-distal region of the blade is removed for ease of viewing. (B) Lateral view of PIEZO1 (PDB: 7WLT). Arrows indicate the spring linker. (C) Lateral view of PIEZO2 (PDB: 6KG7), whose spring linker is unresolved. (D) Top view of PEZO-1 isoform G showing a larger cap surface area. (E) Top view of PIEZO1. The cap area of PEZO-1G is shown as a dashed outline. (F) Top view of PIEZO2. The cap area of PEZO-1G is shown as a dashed outline. (G) PEZO-1 isoform G multiple hydrogen bonds (R2128–C1278′ , T2127–S1288′, D2123-K1289′, and N2118–E1689′), a salt bridge (K2144–E1689′), and a cation–π interaction (Y2125–K1289′) between the cap and THU7–THU8. (H) Single salt bridge in PIEZO1 (E2257–R1761′). (I) Absence of interactions in PIEZO2. See also .
    Figure Legend Snippet: (A) Lateral view of PEZO-1 isoform G highlighting the cap and central regions. Arrows indicate the spring linker. The cap width is denoted above the respective model. The pore-distal region of the blade is removed for ease of viewing. (B) Lateral view of PIEZO1 (PDB: 7WLT). Arrows indicate the spring linker. (C) Lateral view of PIEZO2 (PDB: 6KG7), whose spring linker is unresolved. (D) Top view of PEZO-1 isoform G showing a larger cap surface area. (E) Top view of PIEZO1. The cap area of PEZO-1G is shown as a dashed outline. (F) Top view of PIEZO2. The cap area of PEZO-1G is shown as a dashed outline. (G) PEZO-1 isoform G multiple hydrogen bonds (R2128–C1278′ , T2127–S1288′, D2123-K1289′, and N2118–E1689′), a salt bridge (K2144–E1689′), and a cation–π interaction (Y2125–K1289′) between the cap and THU7–THU8. (H) Single salt bridge in PIEZO1 (E2257–R1761′). (I) Absence of interactions in PIEZO2. See also .

    Techniques Used:

    (A) Ion conduction pathways of PEZO-1 isoforms G and K along the z axis. (B) HOLE profiles of the permeation pathways of PEZO-1G and PEZO-1K compared with available PIEZO1 conformations. Differences in the profile between PEZO-1G and PEZO-1K are indicated by asterisks. (C) Ion conduction pathways of the curved (PDB: 7WLT), intermediate (PDB: 8IXO), and flattened (PDB: 7WLU) conformations of PIEZO1. (D) Ribbon representations showing sites of constriction at the cap gate, transmembrane (TM), and neck regions of PEZO-1G and PIEZO1. Dashed and solid lines represent interactions and distances, respectively. See also .
    Figure Legend Snippet: (A) Ion conduction pathways of PEZO-1 isoforms G and K along the z axis. (B) HOLE profiles of the permeation pathways of PEZO-1G and PEZO-1K compared with available PIEZO1 conformations. Differences in the profile between PEZO-1G and PEZO-1K are indicated by asterisks. (C) Ion conduction pathways of the curved (PDB: 7WLT), intermediate (PDB: 8IXO), and flattened (PDB: 7WLU) conformations of PIEZO1. (D) Ribbon representations showing sites of constriction at the cap gate, transmembrane (TM), and neck regions of PEZO-1G and PIEZO1. Dashed and solid lines represent interactions and distances, respectively. See also .

    Techniques Used:

    (A) (Top) Lateral view of PEZO-1G highlighting the beam relative to the pore and its interactions with the proximal and distal blade, close to the N and C terminus, respectively (bottom). (B) Comparison of the beam in PEZO-1G and PEZO-1K with those of the curved, intermediate, and flattened conformations of PIEZO1, as well as PIEZO2. These beams are also depicted as simplified line schematics. An angle illustrating the relative orientation of the beam of PEZO-1G to the beam of PIEZO1 in the curved state is shown. (C) Electrostatic potential surface of the beam-THU7 of PEZO-1G, PEZO1-K, PIEZO1, and PIEZO2. Positively charged regions are shown in blue, and negatively charged regions are shown in red. (D) Lateral view of PEZO-1 isoform G with the cytoplasmic latch-plug denoted in the dashed box. (E) Comparison of the PEZO-1G, PIEZO1 (curved), and PIEZO2 cytoplasmic latch-plugs, highlighting key residues located within this region. See also and .
    Figure Legend Snippet: (A) (Top) Lateral view of PEZO-1G highlighting the beam relative to the pore and its interactions with the proximal and distal blade, close to the N and C terminus, respectively (bottom). (B) Comparison of the beam in PEZO-1G and PEZO-1K with those of the curved, intermediate, and flattened conformations of PIEZO1, as well as PIEZO2. These beams are also depicted as simplified line schematics. An angle illustrating the relative orientation of the beam of PEZO-1G to the beam of PIEZO1 in the curved state is shown. (C) Electrostatic potential surface of the beam-THU7 of PEZO-1G, PEZO1-K, PIEZO1, and PIEZO2. Positively charged regions are shown in blue, and negatively charged regions are shown in red. (D) Lateral view of PEZO-1 isoform G with the cytoplasmic latch-plug denoted in the dashed box. (E) Comparison of the PEZO-1G, PIEZO1 (curved), and PIEZO2 cytoplasmic latch-plugs, highlighting key residues located within this region. See also and .

    Techniques Used: Comparison



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    99
    ATCC mouse piezo1 knockout neuro2a
    (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in <t>N2A</t> <t>Piezo1</t> −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .
    Mouse Piezo1 Knockout Neuro2a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+piezo1+knockout+neuro2a/pmc12951647-25-0-8?v=ATCC
    Average 99 stars, based on 1 article reviews
    mouse piezo1 knockout neuro2a - by Bioz Stars, 2026-07
    99/100 stars
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    (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in N2A Piezo1 −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .

    Journal: Cell reports

    Article Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade

    doi: 10.1016/j.celrep.2025.116878

    Figure Lengend Snippet: (A) Gene diagrams of pezo-1 G, K, and L isoforms, according to WormBase ( wormweb.org v. WS297), made with Exon-Intron Graphic Maker. Beginning rectangles and triangles denote the 5′ and 3′ UTRs, respectively; rectangles denote exons, and lines denote introns. (B) Schematic representation of monomer topology for PEZO-1 isoforms. Filled lines denote resolved regions, dashed lines denote unresolved regions. (C) Representative whole-cell patch-clamp recordings of mechanically activated currents in N2A Piezo1 −/− cells transfected with pezo-1 G, K, or L isoform. (D) Current densities evoked by maximal mechanical displacement. Bars are mean ± SEM. n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.139). (E) Boxplot showing the displacement threshold required to elicit mechanocurrents. Boxplots show the median (bisecting line), as well as the minimum and maximum values (whiskers). n.s. not significant by Kolmogorov-Smirnov and Mann-Whitney test ( p = 0.901). (F) Boxplot of inactivation time constants evoked by maximal displacement. Kolmogorov-Smirnov and Mann-Whitney tests ( p = 0.002). ** p = 0.139 by Kolmogorov-Smirnov and Mann-Whitney test. (G–I) Cryo-EM density maps of PEZO-1 isoforms G (turquoise; PDB: 9ZIS, EMD: 74281), K (aluminum, PDB: 9ZIT, EMD: 74283), and L (red; EMD: 74433), viewed from the top, side, and bottom. See also - ; .

    Article Snippet: Mouse: Piezo1 -knockout Neuro2a (N2A Piezo1−/− ) , ATCC , CAT#CCL-131.

    Techniques: Patch Clamp, Transfection, MANN-WHITNEY, Cryo-EM Sample Prep

    (A) Lateral view of PEZO-1 isoform G highlighting the cap and central regions. Arrows indicate the spring linker. The cap width is denoted above the respective model. The pore-distal region of the blade is removed for ease of viewing. (B) Lateral view of PIEZO1 (PDB: 7WLT). Arrows indicate the spring linker. (C) Lateral view of PIEZO2 (PDB: 6KG7), whose spring linker is unresolved. (D) Top view of PEZO-1 isoform G showing a larger cap surface area. (E) Top view of PIEZO1. The cap area of PEZO-1G is shown as a dashed outline. (F) Top view of PIEZO2. The cap area of PEZO-1G is shown as a dashed outline. (G) PEZO-1 isoform G multiple hydrogen bonds (R2128–C1278′ , T2127–S1288′, D2123-K1289′, and N2118–E1689′), a salt bridge (K2144–E1689′), and a cation–π interaction (Y2125–K1289′) between the cap and THU7–THU8. (H) Single salt bridge in PIEZO1 (E2257–R1761′). (I) Absence of interactions in PIEZO2. See also .

    Journal: Cell reports

    Article Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade

    doi: 10.1016/j.celrep.2025.116878

    Figure Lengend Snippet: (A) Lateral view of PEZO-1 isoform G highlighting the cap and central regions. Arrows indicate the spring linker. The cap width is denoted above the respective model. The pore-distal region of the blade is removed for ease of viewing. (B) Lateral view of PIEZO1 (PDB: 7WLT). Arrows indicate the spring linker. (C) Lateral view of PIEZO2 (PDB: 6KG7), whose spring linker is unresolved. (D) Top view of PEZO-1 isoform G showing a larger cap surface area. (E) Top view of PIEZO1. The cap area of PEZO-1G is shown as a dashed outline. (F) Top view of PIEZO2. The cap area of PEZO-1G is shown as a dashed outline. (G) PEZO-1 isoform G multiple hydrogen bonds (R2128–C1278′ , T2127–S1288′, D2123-K1289′, and N2118–E1689′), a salt bridge (K2144–E1689′), and a cation–π interaction (Y2125–K1289′) between the cap and THU7–THU8. (H) Single salt bridge in PIEZO1 (E2257–R1761′). (I) Absence of interactions in PIEZO2. See also .

    Article Snippet: Mouse: Piezo1 -knockout Neuro2a (N2A Piezo1−/− ) , ATCC , CAT#CCL-131.

    Techniques:

    (A) Ion conduction pathways of PEZO-1 isoforms G and K along the z axis. (B) HOLE profiles of the permeation pathways of PEZO-1G and PEZO-1K compared with available PIEZO1 conformations. Differences in the profile between PEZO-1G and PEZO-1K are indicated by asterisks. (C) Ion conduction pathways of the curved (PDB: 7WLT), intermediate (PDB: 8IXO), and flattened (PDB: 7WLU) conformations of PIEZO1. (D) Ribbon representations showing sites of constriction at the cap gate, transmembrane (TM), and neck regions of PEZO-1G and PIEZO1. Dashed and solid lines represent interactions and distances, respectively. See also .

    Journal: Cell reports

    Article Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade

    doi: 10.1016/j.celrep.2025.116878

    Figure Lengend Snippet: (A) Ion conduction pathways of PEZO-1 isoforms G and K along the z axis. (B) HOLE profiles of the permeation pathways of PEZO-1G and PEZO-1K compared with available PIEZO1 conformations. Differences in the profile between PEZO-1G and PEZO-1K are indicated by asterisks. (C) Ion conduction pathways of the curved (PDB: 7WLT), intermediate (PDB: 8IXO), and flattened (PDB: 7WLU) conformations of PIEZO1. (D) Ribbon representations showing sites of constriction at the cap gate, transmembrane (TM), and neck regions of PEZO-1G and PIEZO1. Dashed and solid lines represent interactions and distances, respectively. See also .

    Article Snippet: Mouse: Piezo1 -knockout Neuro2a (N2A Piezo1−/− ) , ATCC , CAT#CCL-131.

    Techniques:

    (A) (Top) Lateral view of PEZO-1G highlighting the beam relative to the pore and its interactions with the proximal and distal blade, close to the N and C terminus, respectively (bottom). (B) Comparison of the beam in PEZO-1G and PEZO-1K with those of the curved, intermediate, and flattened conformations of PIEZO1, as well as PIEZO2. These beams are also depicted as simplified line schematics. An angle illustrating the relative orientation of the beam of PEZO-1G to the beam of PIEZO1 in the curved state is shown. (C) Electrostatic potential surface of the beam-THU7 of PEZO-1G, PEZO1-K, PIEZO1, and PIEZO2. Positively charged regions are shown in blue, and negatively charged regions are shown in red. (D) Lateral view of PEZO-1 isoform G with the cytoplasmic latch-plug denoted in the dashed box. (E) Comparison of the PEZO-1G, PIEZO1 (curved), and PIEZO2 cytoplasmic latch-plugs, highlighting key residues located within this region. See also and .

    Journal: Cell reports

    Article Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade

    doi: 10.1016/j.celrep.2025.116878

    Figure Lengend Snippet: (A) (Top) Lateral view of PEZO-1G highlighting the beam relative to the pore and its interactions with the proximal and distal blade, close to the N and C terminus, respectively (bottom). (B) Comparison of the beam in PEZO-1G and PEZO-1K with those of the curved, intermediate, and flattened conformations of PIEZO1, as well as PIEZO2. These beams are also depicted as simplified line schematics. An angle illustrating the relative orientation of the beam of PEZO-1G to the beam of PIEZO1 in the curved state is shown. (C) Electrostatic potential surface of the beam-THU7 of PEZO-1G, PEZO1-K, PIEZO1, and PIEZO2. Positively charged regions are shown in blue, and negatively charged regions are shown in red. (D) Lateral view of PEZO-1 isoform G with the cytoplasmic latch-plug denoted in the dashed box. (E) Comparison of the PEZO-1G, PIEZO1 (curved), and PIEZO2 cytoplasmic latch-plugs, highlighting key residues located within this region. See also and .

    Article Snippet: Mouse: Piezo1 -knockout Neuro2a (N2A Piezo1−/− ) , ATCC , CAT#CCL-131.

    Techniques: Comparison