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α tubulin mab  (Proteintech)


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    Structured Review

    Proteintech α tubulin mab
    Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western <t>blotting,</t> <t>α-tubulin</t> and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.
    α Tubulin Mab, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 2889 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α tubulin mab/product/Proteintech
    Average 96 stars, based on 2889 article reviews
    α tubulin mab - by Bioz Stars, 2026-02
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    Images

    1) Product Images from "Rabeprazole attenuates fibrosis by modulating SMAD3 linker region phosphorylation"

    Article Title: Rabeprazole attenuates fibrosis by modulating SMAD3 linker region phosphorylation

    Journal: Biomedical Reports

    doi: 10.3892/br.2025.2098

    Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western blotting, α-tubulin and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.
    Figure Legend Snippet: Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western blotting, α-tubulin and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.

    Techniques Used: Phospho-proteomics, Translocation Assay, Western Blot, Isolation, Protein Extraction, Immunofluorescence



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    Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western <t>blotting,</t> <t>α-tubulin</t> and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.
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    Image Search Results


    Disruption of acrosome, nuclear, and manchette assembly in KI mouse sperm. a PAS (left) and PNA (right) staining of seminiferous tubules from WT and KI mice at different stages of spermatogenesis. Green arrowheads (PAS) and red arrowheads (PNA) indicate aberrant acrosomal morphology in KI spermatids. M: Metaphase. Scale bars, 10 μm. b Transmission electron microscopy (TEM) of sperm head development in WT and KI spermatids. Nu, nucleus; g, Golgi apparatus; av, proacrosomal vesicles; apx, acroplaxome; ac, acrosome. Red arrows indicate malformed acrosomes; blue asterisks denote abnormal nuclei. Scale bars, 1 μm. c Representative TEM images of manchette morphology during spermatid elongation in WT and KI mice. White double-headed arrows highlight the asymmetric manchette in KI spermatids. Abbreviations: Nu, nucleus; PR, perinuclear ring; M, manchette. Scale bars, 1 μm. d Immunofluorescence staining of tubulin in spermatozoa from adult WT and KI mice. Tubulin marks the manchette structure; DNA was counterstained with DAPI. Scale bars, 5 μm. e Quantification of manchette microtubule lengths from ( d ). For each group, 40 spermatozoa were randomly selected per mouse, and average values were calculated for every 10 sperms. Data are presented as mean ± SD. P -values were determined using a two-sided Student’s t -test. n = 36 per group

    Journal: Signal Transduction and Targeted Therapy

    Article Title: Targeting SKAP2 restores sperm motility and morphology through modulating mitochondrial organization and cytoskeletal remodeling

    doi: 10.1038/s41392-025-02513-3

    Figure Lengend Snippet: Disruption of acrosome, nuclear, and manchette assembly in KI mouse sperm. a PAS (left) and PNA (right) staining of seminiferous tubules from WT and KI mice at different stages of spermatogenesis. Green arrowheads (PAS) and red arrowheads (PNA) indicate aberrant acrosomal morphology in KI spermatids. M: Metaphase. Scale bars, 10 μm. b Transmission electron microscopy (TEM) of sperm head development in WT and KI spermatids. Nu, nucleus; g, Golgi apparatus; av, proacrosomal vesicles; apx, acroplaxome; ac, acrosome. Red arrows indicate malformed acrosomes; blue asterisks denote abnormal nuclei. Scale bars, 1 μm. c Representative TEM images of manchette morphology during spermatid elongation in WT and KI mice. White double-headed arrows highlight the asymmetric manchette in KI spermatids. Abbreviations: Nu, nucleus; PR, perinuclear ring; M, manchette. Scale bars, 1 μm. d Immunofluorescence staining of tubulin in spermatozoa from adult WT and KI mice. Tubulin marks the manchette structure; DNA was counterstained with DAPI. Scale bars, 5 μm. e Quantification of manchette microtubule lengths from ( d ). For each group, 40 spermatozoa were randomly selected per mouse, and average values were calculated for every 10 sperms. Data are presented as mean ± SD. P -values were determined using a two-sided Student’s t -test. n = 36 per group

    Article Snippet: We extend our gratitude to Bioss for the antibody of alpha Tubulin (bsm-33039M) and alpha Tubulin Antibody from MedChemExpress (Monmouth Junction, NJ, USA; Cat# HY- P86200 ).

    Techniques: Disruption, Staining, Transmission Assay, Electron Microscopy, Immunofluorescence

    Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western blotting, α-tubulin and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.

    Journal: Biomedical Reports

    Article Title: Rabeprazole attenuates fibrosis by modulating SMAD3 linker region phosphorylation

    doi: 10.3892/br.2025.2098

    Figure Lengend Snippet: Rabeprazole modulates SMAD3 phosphorylation and nuclear translocation. (A) GES-1 and AGS cells were treated with or without rabeprazole for 1 h, and the phosphorylation of SMAD3 linker was detected by immunoblotting. (B-E) The band intensities were quantified and analyzed by one sample t-test. Data are shown as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001, n=3. (F) Left panel: The subcellular fraction was isolated using nuclear and cytoplasmic protein extraction kit according to manufacturer's instructions. The SMAD3 level was detected by western blotting, α-tubulin and lamin A/C were used as cytosolic and nuclear internal controls. Right panel: IF analysis of SMAD3 in AGS cells treated with or without rabeprazole for 1 h. Scale bar, 100 µm. SMAD3, SMAD family member 3; IF, immunofluorescence; phospho, phosphorylated.

    Article Snippet: Antibodies including α-SMA specific monoclonal antibody (mAb) (cat. no. 67735-1-Ig), FN mAb (cat. no. 66042-1-Ig), vimentin polyclonal antibody (pAb) (cat. no. 10366-1-AP), collagen type I (Col1a1) mAb (cat. no. 67288-1-Ig), SMAD3 mAb (cat. no. 66516-1-Ig), lamin A/C pAb (cat. no. 10298-1-AP) and α-tubulin mAb (cat. no. 66031-1-Ig) were purchased from Proteintech Group, Inc. TIF1γ mouse mAb (cat. no. YM1108), SMAD3 (phospho Ser204) rabbit pAb (cat. no. YP0363), SMAD3 (phospho Ser213) rabbit pAb (cat. no. YP0364), SMAD3 (phospho Thr179) rabbit pAb (cat. no. YP0745) and SMAD3 (phospho Ser208) rabbit pAb (cat. no. YP0746) were purchased from Immunoway Biotechnology Co., Ltd.; peroxidase affiniPureTM goat anti-rabbit IgG (H+L) (cat. no. 111-035-003) and peroxidase-conjugated affiniPure goat anti-mouse IgG (H+L) (cat. no. 115-035-003) were obtained from Jackson ImmunoResearch Laboratories, Inc.

    Techniques: Phospho-proteomics, Translocation Assay, Western Blot, Isolation, Protein Extraction, Immunofluorescence

    DHA increases sensitivity to ferroptosis by modulating cellular oxidative stress (A–E) Western blot and quantifications of the GPX4, ACSL4, FSP1, DHODH, β-actin, and α-tubulin expression in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h. (F) GSH levels in N27 cells treated with different doses of DHA (0, 1.5 μM, 12.5 μM) for 12 h were detected, n = 6 wells from one representative of two independent experiments. (G) Western blot and quantifications of the 4-HNE and β-actin expression in N27 cells treated with different doses of DHA (0, 1.5, 12.5, and 25 μM) for 12 h. (H) N27 cells were treated with different doses of DHA (0, 1.5, and 12.5 μM) for 12 h and lipid ROS was detected by C11-BODIPY using flow cytometry. Representative histograms for fluorescence of oxidized C11-BODIPY and the ratio of the MFI of oxidized to reduced C11-BODIPY are shown. (I) TEM of N27 cells treated with DHA (12.5 μM) for 12 h. Red arrows indicate shrunken mitochondria. Scale bars: upper panel = 2 μm; lower panel = 500 nm, as indicated. (J) The average fluorescence intensity of FerroOrange in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, n = 5 wells from one representative of two independent experiments. (K) The iron levels detected by ICP-MS in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, n = 5 wells from one representative of two independent experiments. (L) Cell viability of N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) in the absence or presence of DFO (50 μM) for 48 h, n = 6 wells from one representative of two independent experiments. (M) Cell viability of N27 cells treated with DHA (12.5 μM) in the absence or presence of DFO (50 μM) for 48 h, n = 6 wells from one representative of two independent experiments. (N) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. (O) N27 cells were treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h and detected by CellROX Green using flow cytometry. Representative histograms for fluorescence of CellROX Green and the average fluorescence are shown, n = 6 wells from one representative of two independent experiments. (P) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM), RSL-3 (100 nM), and NAC (1 mM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. (Q) Cell viability of N27 cells treated with NAC and DHA (1.5 μM) and RSL-3 (100 nM) for 48 h, n = 6 wells from one representative of two independent experiments. (R) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM), RSL-3 (100 nM), and DFO (50 μM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. Data are means ± SEM, n = 3 wells from one representative of two independent experiments unless specified. One-way ANOVA was performed.

    Journal: iScience

    Article Title: HMOX1 drives dihydroartemisinin-sensitized ferroptosis antagonized by mitochondrial fusion

    doi: 10.1016/j.isci.2025.114382

    Figure Lengend Snippet: DHA increases sensitivity to ferroptosis by modulating cellular oxidative stress (A–E) Western blot and quantifications of the GPX4, ACSL4, FSP1, DHODH, β-actin, and α-tubulin expression in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h. (F) GSH levels in N27 cells treated with different doses of DHA (0, 1.5 μM, 12.5 μM) for 12 h were detected, n = 6 wells from one representative of two independent experiments. (G) Western blot and quantifications of the 4-HNE and β-actin expression in N27 cells treated with different doses of DHA (0, 1.5, 12.5, and 25 μM) for 12 h. (H) N27 cells were treated with different doses of DHA (0, 1.5, and 12.5 μM) for 12 h and lipid ROS was detected by C11-BODIPY using flow cytometry. Representative histograms for fluorescence of oxidized C11-BODIPY and the ratio of the MFI of oxidized to reduced C11-BODIPY are shown. (I) TEM of N27 cells treated with DHA (12.5 μM) for 12 h. Red arrows indicate shrunken mitochondria. Scale bars: upper panel = 2 μm; lower panel = 500 nm, as indicated. (J) The average fluorescence intensity of FerroOrange in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, n = 5 wells from one representative of two independent experiments. (K) The iron levels detected by ICP-MS in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, n = 5 wells from one representative of two independent experiments. (L) Cell viability of N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) in the absence or presence of DFO (50 μM) for 48 h, n = 6 wells from one representative of two independent experiments. (M) Cell viability of N27 cells treated with DHA (12.5 μM) in the absence or presence of DFO (50 μM) for 48 h, n = 6 wells from one representative of two independent experiments. (N) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. (O) N27 cells were treated with DHA (1.5 μM) and RSL-3 (100 nM) for 12 h and detected by CellROX Green using flow cytometry. Representative histograms for fluorescence of CellROX Green and the average fluorescence are shown, n = 6 wells from one representative of two independent experiments. (P) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM), RSL-3 (100 nM), and NAC (1 mM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. (Q) Cell viability of N27 cells treated with NAC and DHA (1.5 μM) and RSL-3 (100 nM) for 48 h, n = 6 wells from one representative of two independent experiments. (R) The representative images of H 2 DCFDA staining in N27 cells treated with DHA (1.5 μM), RSL-3 (100 nM), and DFO (50 μM) for 12 h, and the average fluorescence intensity are shown. Scale bars, 200 μm, as indicated. Data are means ± SEM, n = 3 wells from one representative of two independent experiments unless specified. One-way ANOVA was performed.

    Article Snippet: Alpha Tubulin Monoclonal antibody (1:10000) , Proteintech , 66031-1-Ig; RRID: AB_11042766.

    Techniques: Western Blot, Expressing, Flow Cytometry, Fluorescence, Staining

    (A), colony anterior showing pneumatophore (pn), nectophores and gastrozooids (gz) attached to the central stem, visible through the transparent nectosome. (B), entire isolated nectophore stained with anti-tubulin antibody (green) and phalliodin (red); both the upper nerve (un) and the lower nerve (ln) join the nerve ring (rn); endodermal muscles (em); the terminal ganglion (tg) is located at the back of the nectophore where it normally contacts the stem. (C), the lower nerve (ln) terminates in the terminal ganglion (tg). (D), the point at which the lower nerve (ln) joins the nerve ring (rn) shown by an arrow. (E), terminal ganglion (tg) at high magnification; nuclei (blue) shown by DAPI labeling. Scale bars: A, 5 mm; B, 500 µm; C, D, 200 µm; E, 30 µm;

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: (A), colony anterior showing pneumatophore (pn), nectophores and gastrozooids (gz) attached to the central stem, visible through the transparent nectosome. (B), entire isolated nectophore stained with anti-tubulin antibody (green) and phalliodin (red); both the upper nerve (un) and the lower nerve (ln) join the nerve ring (rn); endodermal muscles (em); the terminal ganglion (tg) is located at the back of the nectophore where it normally contacts the stem. (C), the lower nerve (ln) terminates in the terminal ganglion (tg). (D), the point at which the lower nerve (ln) joins the nerve ring (rn) shown by an arrow. (E), terminal ganglion (tg) at high magnification; nuclei (blue) shown by DAPI labeling. Scale bars: A, 5 mm; B, 500 µm; C, D, 200 µm; E, 30 µm;

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Isolation, Staining, Muscles, Labeling

    Stem nervous system labeled with anti-tubulin antibody (green); nuclear DAPI staining (blue) . (A), stem anterior where it connects to the pneumatophore (pn) showing the origin of the giant axon (ga); the nerve network that covers the outer layer of the pneumatophore merges into the stem. (B), giant axon (ga) running along the entire stem. (C, D), the polygonal nerve network covers the subepithelial layer in the stem and merges with the giant axons (ga) at numerous points (arrows). (E), the cone-shaped structure, which serves as a nectophore docking site, contains the same polygonal nerve network as the stem. (F), higher magnification of the cone and its polygonal nerve network; arrows point to the nectophore attachment surface; cell nuclei (blue). Scale bars: A, B, 200 µm; C–F, 100 µm.

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: Stem nervous system labeled with anti-tubulin antibody (green); nuclear DAPI staining (blue) . (A), stem anterior where it connects to the pneumatophore (pn) showing the origin of the giant axon (ga); the nerve network that covers the outer layer of the pneumatophore merges into the stem. (B), giant axon (ga) running along the entire stem. (C, D), the polygonal nerve network covers the subepithelial layer in the stem and merges with the giant axons (ga) at numerous points (arrows). (E), the cone-shaped structure, which serves as a nectophore docking site, contains the same polygonal nerve network as the stem. (F), higher magnification of the cone and its polygonal nerve network; arrows point to the nectophore attachment surface; cell nuclei (blue). Scale bars: A, B, 200 µm; C–F, 100 µm.

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Labeling, Staining

    (Ai), two lateral giant axons (ga) and their associated nerve network (green), together with FMRFa-ir neural tracts connecting contralateral cones. (Aii), red channel of (Ai) showing FMRFa IR only; each neural tract connects contralateral cones (arrows) but not immediate neighbours. (Aiii), green channel of (Ai) showing tubulin IR only. (B), higher power of the stem showing the giant axons (ga), the polygonal nerve network (green), the neural tract (red; arrows), all running along the stem; there is a neural loop at the tip of each cone. (Ci), cone with its polygonal nerve network (green) and FMRFa-ir neural loop (red) at the cone tip. (Cii), red channel of (Ci) showing FMRFa-ir labeling only; arrows show some of the numerous neural cell bodies. (Di), high magnification of the polygonal nerve network (green) and the FMRFa-ir neural tract (red). (Dii), red channel of (Di) showing FMRFa IR only; arrows show some of the immunoreactive cell bodies. (Diii), green channel of (Di) showing that the FMRFa-ir neural tract does not label with tubulin IR. Scale bars: Ai-Aiii, 500 µm; B, 200 µm; Ci, Cii, 100 µm; Di-Diii, 50 µm.

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: (Ai), two lateral giant axons (ga) and their associated nerve network (green), together with FMRFa-ir neural tracts connecting contralateral cones. (Aii), red channel of (Ai) showing FMRFa IR only; each neural tract connects contralateral cones (arrows) but not immediate neighbours. (Aiii), green channel of (Ai) showing tubulin IR only. (B), higher power of the stem showing the giant axons (ga), the polygonal nerve network (green), the neural tract (red; arrows), all running along the stem; there is a neural loop at the tip of each cone. (Ci), cone with its polygonal nerve network (green) and FMRFa-ir neural loop (red) at the cone tip. (Cii), red channel of (Ci) showing FMRFa-ir labeling only; arrows show some of the numerous neural cell bodies. (Di), high magnification of the polygonal nerve network (green) and the FMRFa-ir neural tract (red). (Dii), red channel of (Di) showing FMRFa IR only; arrows show some of the immunoreactive cell bodies. (Diii), green channel of (Di) showing that the FMRFa-ir neural tract does not label with tubulin IR. Scale bars: Ai-Aiii, 500 µm; B, 200 µm; Ci, Cii, 100 µm; Di-Diii, 50 µm.

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Labeling

    (Ai), double labeled image. (Aii), red channel with FMRFa IR only. (Aiii), green channel with tubulin IR only; yellow arrow indicates a thick process with only tubulin IR; white arrows indicate processes with cross-reactivity for both tubulin IR and FMRFa IR. (Bi), double labeled image of the stem with giant axon (ga) and adjacent nerve network; asterisk shows pentagonal shaped neural unit. (Bii), red channel, with FMRFa-ir processes (arrows) that cross the giant axon rather than merging with it. (Biii), green channel showing that the giant axon (ga) is labeled only with tubulin IR; yellow arrow shows tubulin-ir threads merging with the giant axon. (Ci) pentagonal shaped neural unit from Bi; (Cii) red channel with FMRFa IR only; (Ciii) green channel with tubulin IR only. Yellow arrows indicate thick neural threads with tubulin IR only; white arrows indicate processes with both tubulin IR and FMRFa IR. Scale bars: A, B, 50 µm; C, 12 µm.

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: (Ai), double labeled image. (Aii), red channel with FMRFa IR only. (Aiii), green channel with tubulin IR only; yellow arrow indicates a thick process with only tubulin IR; white arrows indicate processes with cross-reactivity for both tubulin IR and FMRFa IR. (Bi), double labeled image of the stem with giant axon (ga) and adjacent nerve network; asterisk shows pentagonal shaped neural unit. (Bii), red channel, with FMRFa-ir processes (arrows) that cross the giant axon rather than merging with it. (Biii), green channel showing that the giant axon (ga) is labeled only with tubulin IR; yellow arrow shows tubulin-ir threads merging with the giant axon. (Ci) pentagonal shaped neural unit from Bi; (Cii) red channel with FMRFa IR only; (Ciii) green channel with tubulin IR only. Yellow arrows indicate thick neural threads with tubulin IR only; white arrows indicate processes with both tubulin IR and FMRFa IR. Scale bars: A, B, 50 µm; C, 12 µm.

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Labeling

    (A), the stem neural system includes two giant axons, two tubulin-ir nerve networks and a system of FMRFa-ir, double-threaded, neural tracts between contralateral cones; the stem itself consists of two columns of cone-shaped protrusions that serve as docking stations for the nectophores; the terminal ganglion is located at the attachment point; it is connected to the nerve ring, in the margin of the nectophore, by the lower nerve; also shown are the Claus muscles of the velum (cm) and the muscles of the endoderm (em) that abut onto them . (B), detailed view of the cone attachment area between the nectophore and the stem; the terminal ganglion of the nectophore is separated from the cone surface by a simple narrow cleft. Outside of the terminal ganglion contact, the epithelial layer of the nectophore is firmly attached to the cone. In this area (black dotted line), electrical junctions may couple the nerve network of the cone with the epithelial conductance pathway in the nectophore.

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: (A), the stem neural system includes two giant axons, two tubulin-ir nerve networks and a system of FMRFa-ir, double-threaded, neural tracts between contralateral cones; the stem itself consists of two columns of cone-shaped protrusions that serve as docking stations for the nectophores; the terminal ganglion is located at the attachment point; it is connected to the nerve ring, in the margin of the nectophore, by the lower nerve; also shown are the Claus muscles of the velum (cm) and the muscles of the endoderm (em) that abut onto them . (B), detailed view of the cone attachment area between the nectophore and the stem; the terminal ganglion of the nectophore is separated from the cone surface by a simple narrow cleft. Outside of the terminal ganglion contact, the epithelial layer of the nectophore is firmly attached to the cone. In this area (black dotted line), electrical junctions may couple the nerve network of the cone with the epithelial conductance pathway in the nectophore.

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Muscles

    (A), early stage nectophore attached to the stem by an extended side-branch (sb). (B), later stage nectophore showing lower nerve (ln) and terminal ganglion (tg) at the point of contact with the shortened stem branch (sb); arrow indicates the FMRFa-ir neural loop (red). (C), mature nectophore connected to the stem via a short cone. (Di), higher magnification of the terminal ganglion (tg) area from (C); the terminal ganglion and cone are separated by a narrow cleft (arrow); many thin nerve fibres, both tubulin-ir and FMRFa-ir, come to the cone surface here. (Dii), green channel of (Di) showing the nerve fibres opposite the nectophore terminal ganglion (tg). (Diii), red channel of (Di) showing FMRFa-ir cell bodies; labeling absent from terminal ganglion or lower nerve. (E), side view of the contact between the terminal ganglion and the cone, showing the thin nerve fibres at the cone surface, opposite the narrow cleft (arrows) that separates the cone from the terminal ganglion; nerve contains both tubulin-ir and FMRFa-ir elements. (F), different view of the terminal ganglion (tg), from the side and slightly above, showing that the polygonal nerve network gives rise to numerous fine processes (arrows) that project toward the terminal ganglion. (G), high magnification of (C) showing the area of contact between the nectophore epithelium and the cone surface (arrow); the outline of the epithelial cells is revealed by background tubulin-ir. D, E and F, different preparations. Scale bars: A, B, 200 µm; C, 100 µm; Di-Diii, G, 50 µm; E, 40 µm; F, 30 µm.

    Journal: bioRxiv

    Article Title: Structure and function of the nervous system in the stem of the siphonophore Nanomia septata : its role in swimming coordination

    doi: 10.1101/2025.11.27.690755

    Figure Lengend Snippet: (A), early stage nectophore attached to the stem by an extended side-branch (sb). (B), later stage nectophore showing lower nerve (ln) and terminal ganglion (tg) at the point of contact with the shortened stem branch (sb); arrow indicates the FMRFa-ir neural loop (red). (C), mature nectophore connected to the stem via a short cone. (Di), higher magnification of the terminal ganglion (tg) area from (C); the terminal ganglion and cone are separated by a narrow cleft (arrow); many thin nerve fibres, both tubulin-ir and FMRFa-ir, come to the cone surface here. (Dii), green channel of (Di) showing the nerve fibres opposite the nectophore terminal ganglion (tg). (Diii), red channel of (Di) showing FMRFa-ir cell bodies; labeling absent from terminal ganglion or lower nerve. (E), side view of the contact between the terminal ganglion and the cone, showing the thin nerve fibres at the cone surface, opposite the narrow cleft (arrows) that separates the cone from the terminal ganglion; nerve contains both tubulin-ir and FMRFa-ir elements. (F), different view of the terminal ganglion (tg), from the side and slightly above, showing that the polygonal nerve network gives rise to numerous fine processes (arrows) that project toward the terminal ganglion. (G), high magnification of (C) showing the area of contact between the nectophore epithelium and the cone surface (arrow); the outline of the epithelial cells is revealed by background tubulin-ir. D, E and F, different preparations. Scale bars: A, B, 200 µm; C, 100 µm; Di-Diii, G, 50 µm; E, 40 µm; F, 30 µm.

    Article Snippet: Therefore, as a first marker, rat monoclonal anti-tubulin antibody was used (AbD Serotec, Bio-Rad, Cat# MCA77G, RRID: AB_325003), which recognizes the alpha subunit of α-tubulin, specifically binding tyrosylated α-tubulin ( ; ).

    Techniques: Labeling