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Santa Cruz Biotechnology mouse anti spectrin βii
Mouse Anti Spectrin βii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+spectrin+%CE%B2ii/bio_rxiv__64898__2026__02__25__708020-306-9-14?v=Santa+Cruz+Biotechnology
Average 94 stars, based on 28 article reviews

mouse anti spectrin βii - by Bioz Stars, 2026-07

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$( A to D ) Left: Stitched SIM images showing the distributions of endogenous endocytic pits, clathrin (A), Cav1 (B), Flot1 (C), or EndoA2 (D) in WT neurons. Endocytic pits are shown in green, with compartment markers MAP2 (magenta) and neurofacsin (yellow). Scale bar, 10 μm. Right: Enlarged SIM images of the three boxed regions on the left, corresponding to soma, dendrite, and AIS compartments, respectively. Scale bar, 2 μm. ( E ) Boxplots showing the area fraction of endogenous endocytic pits in different compartments of WT neurons. ( F ) Left: SIM images of tau (magenta) and endogenous endocytic pits (green) in distal axons of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( G ) Boxplots showing the area fraction of endogenous endocytic pits (green) in distal axons of WT and βII-spectrin KD neurons. ( H ) Left: SIM images of MAP2 (magenta) and endogenous endocytic pits (green) in dendrites of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( I ) Boxplots showing the area fraction of endogenous endocytic pits in dendrites of WT and βII-spectrin KD neurons.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A to D ) Left: Stitched SIM images showing the distributions of endogenous endocytic pits, clathrin (A), Cav1 (B), Flot1 (C), or EndoA2 (D) in WT neurons. Endocytic pits are shown in green, with compartment markers MAP2 (magenta) and neurofacsin (yellow). Scale bar, 10 μm. Right: Enlarged SIM images of the three boxed regions on the left, corresponding to soma, dendrite, and AIS compartments, respectively. Scale bar, 2 μm. ( E ) Boxplots showing the area fraction of endogenous endocytic pits in different compartments of WT neurons. ( F ) Left: SIM images of tau (magenta) and endogenous endocytic pits (green) in distal axons of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( G ) Boxplots showing the area fraction of endogenous endocytic pits (green) in distal axons of WT and βII-spectrin KD neurons. ( H ) Left: SIM images of MAP2 (magenta) and endogenous endocytic pits (green) in dendrites of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( I ) Boxplots showing the area fraction of endogenous endocytic pits in dendrites of WT and βII-spectrin KD neurons.

Article Snippet: The following primary antibodies were used in this study: guinea pig anti-tau antibody 1:500 dilution for IF (Synaptic Systems, 314004), mouse anti-tau antibody 1:500 dilution for IF (BD Biosciences, 556319), guinea pig anti-MAP2 antibody 1:500 dilution for IF (Synaptic Systems, 188004), rabbit anti-MAP2 antibody 1:500 dilution for IF (Synaptic Systems, 188002), chicken anti-neurofascin antibody (R&D system, AF3235), rabbit anti-CHC antibody 1:500 dilution for IF (Abcam, ab21679), rabbit anti-Cav1 antibody 1:400 dilution for IF (Cell Signaling Technology, 3238S), mouse anti-Flot1 antibody 1:100 dilution for IF (BD Biosciences, 610820), mouse anti-endophilinA2 antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-365704), mouse anti–αII-spectrin (EnCor Biotechnology, MCA-3D7), mouse anti-βII spectrin antibody 1:200 dilution for IF (Santa Cruz Biotechnology, sc-515592), mouse anti-βII spectrin antibody 1:200 dilution for IF (BD Biosciences, 612563), rabbit anti-adducin antibody 1:500 dilution for IF (Abcam, ab51130), chicken anti-GFP antibody 1:500 dilution for IF (Thermo Fisher Scientific, A10262), rabbit anti-GFP antibody 1:500 dilution for IF (Thermo Fisher Scientific, A11122), goat anti-βIII spectrin antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-9660), mouse anti-βIII spectrin antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-515737), mouse anti-HA antibody 1:200 dilution for HA-mGluR5a internalization and IF (Thermo Fisher Scientific, 26183), rat anti-NCAM1 (CD56) antibody 1:40 dilution for NCAM1 internalization and IF (Cedarlane, CL10008AP), rat anti-TfR (CD71) antibody 1:500 dilution for IF (Bio-Rad, MCA1033GA), goat anti–LDL receptor (LDLR) antibody 1:100 dilution for IF (Thermo Fisher Scientific, PA5-46987), rabbit anti–phospho-ERK antibody 1:300 dilution (Cell Signaling Technology, 4370S), mouse anti-Aβ42 antibody 1:200 dilution for IF (BioLegend, 805501), and rabbit anti–cleaved caspase-3 (Asp175) antibody 1:400 dilution for IF (Cell Signaling Technology, 9661).

Techniques:

( A ) Schematic illustrating the spatial distributions of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in axons. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βII-spectrin lattice in axons. Class I pits do not overlap with MPS lattice, whereas class II do. The MPS was visualized by immunostaining with antibodies targeting the C terminus of βII-spectrin, which mark the centers of spectrin tetramers. ( C ) The same as in (B) but showing spatial relationships with the periodic adducin lattice in axons. The MPS was visualized by immunostaining with antibodies targeting the adducin, which mark the terminal ends of spectrin tetramers. ( D ) Left: Dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green) in axons. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), and 200 nm (right). ( E ) PCCs between βII-spectrin and endogenous clathrin under experimental and randomized conditions. ( F ) Left: Averaged dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profiles of the averaged images shown on the left. Scale bar, 100 nm. ( G to I ) The same as in (D) to (F) but for βII-spectrin (magenta) and exogenously expressed Cav1 (green). ( J to L ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed Flot1 (green). ( M to O ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( P ) Percentages of class I and class II pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1 and exogenously expressed EndoA2 in axons.

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the spatial distributions of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in axons. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βII-spectrin lattice in axons. Class I pits do not overlap with MPS lattice, whereas class II do. The MPS was visualized by immunostaining with antibodies targeting the C terminus of βII-spectrin, which mark the centers of spectrin tetramers. ( C ) The same as in (B) but showing spatial relationships with the periodic adducin lattice in axons. The MPS was visualized by immunostaining with antibodies targeting the adducin, which mark the terminal ends of spectrin tetramers. ( D ) Left: Dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green) in axons. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), and 200 nm (right). ( E ) PCCs between βII-spectrin and endogenous clathrin under experimental and randomized conditions. ( F ) Left: Averaged dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profiles of the averaged images shown on the left. Scale bar, 100 nm. ( G to I ) The same as in (D) to (F) but for βII-spectrin (magenta) and exogenously expressed Cav1 (green). ( J to L ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed Flot1 (green). ( M to O ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( P ) Percentages of class I and class II pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1 and exogenously expressed EndoA2 in axons.

Techniques: Immunostaining, Generated

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the spatial distribution of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in dendrites. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βIII-spectrin or adducin lattice in dendrites. Class I pits do not overlap with MPS lattice, whereas class II pits do. The MPS was visualized by immunostaining with antibodies targeting the N terminus of βIII-spectrin or adducin, which both mark terminal ends of spectrin tetramers. ( C ) Left: Dual-color STORM images of βIII-spectrin (magenta) and endogenous clathrin (green) in dendrites. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), 200 nm (right). ( D ) PCCs between βIII-spectrin and endogenous clathrin under experimental and randomized conditions. ( E ) Left: Averaged dual-color STROM images of βIII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profile of averaged images shown on the left. Scale bar, 100 nm. ( F to H ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed Cav1 (green). ( I to K ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed Flot1 (green). ( L to N ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( O ) Percentages of class I and class II endocytic pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1, and exogenously expressed EndoA2 in dendrites.

Techniques: Immunostaining, Generated

$( A ) Confocal fluorescence images of MAP2 (magenta) and internalized CF568-transferrin (green) in somatodendritic region of WT or βII-spectrin KD neurons treated with CF568-transferrin for 2, 10, and 20 min. Scale bars, 10 μm. ( B ) Time course of CF568-transferrin endocytosis in somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of transferrin-positive endosomes. Solid lines represent single-exponential fits to the data. ( C ) Confocal fluorescence images of MAP2 (gray), internalized HA-mGluR5a (green), and endogenous Cav1 (magenta) in somatodendritic region of WT or βII-spectrin KD neurons overexpressing HA-mGluR5a and treated with anti-HA antibody for 5, 10, and 20 min. Scale bars, 10 μm. ( D ) Time course of Cav1-mediated HA-mGluR5a endocytosis in the somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of Cav1-positive HA-mGluR5a endosomes. Solid lines represent single-exponential fits to the data. ( E ) SIM images of internalized NCAM1 (green) and endogenous EndoA2 (magenta) in axonal (top) and somatodendritic (bottom) regions of WT or βII-spectrin KD neurons treated with anti-NCAM1 antibody for 30 min. Scale bars, 2 μm. ( F ) Boxplots of EndoA2-mediated NCAM1 endocytosis in axonal and somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area proportion of EndoA2-positive NCAM1 endosomes.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Confocal fluorescence images of MAP2 (magenta) and internalized CF568-transferrin (green) in somatodendritic region of WT or βII-spectrin KD neurons treated with CF568-transferrin for 2, 10, and 20 min. Scale bars, 10 μm. ( B ) Time course of CF568-transferrin endocytosis in somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of transferrin-positive endosomes. Solid lines represent single-exponential fits to the data. ( C ) Confocal fluorescence images of MAP2 (gray), internalized HA-mGluR5a (green), and endogenous Cav1 (magenta) in somatodendritic region of WT or βII-spectrin KD neurons overexpressing HA-mGluR5a and treated with anti-HA antibody for 5, 10, and 20 min. Scale bars, 10 μm. ( D ) Time course of Cav1-mediated HA-mGluR5a endocytosis in the somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of Cav1-positive HA-mGluR5a endosomes. Solid lines represent single-exponential fits to the data. ( E ) SIM images of internalized NCAM1 (green) and endogenous EndoA2 (magenta) in axonal (top) and somatodendritic (bottom) regions of WT or βII-spectrin KD neurons treated with anti-NCAM1 antibody for 30 min. Scale bars, 2 μm. ( F ) Boxplots of EndoA2-mediated NCAM1 endocytosis in axonal and somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area proportion of EndoA2-positive NCAM1 endosomes.

Techniques: Fluorescence

$( A ) Schematic illustrating ligand-induced ERK activation via three major endocytic pathways: CME of TfR, LRME of HA-mGluR5a, and FEME of NCAM1. ( B ) Top: Epi-fluorescence images showing pERK immunostaining in neurons without ligand treatment, neurons treated with CF568-transferrin, and neurons overexpressing HA-mGluR5a treated with anti-HA antibody. Bottom: The same as the top but with neurons pretreated with dyngo-4a before ligand treatment. Scale bars, 25 μm. ( C ) Time course of ERK activation in neurons under the same conditions as in (B). ( D ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons under various treatments. First column: neurons pretreated with dimethyl sulfoxide (DMSO), dyngo-4a, U0126, MDL, or VAD. Second column: neurons pretreated with the same inhibitors followed by CF568-transferrin treatment. Third column: neurons overexpressing HA-mGluR5a pretreated with the same inhibitors followed by the anti-HA antibody treatment. Fourth column: neurons pretreated with the same inhibitors followed by anti-NCAM1 antibody treatment. Scale bars, 1 μm. Color scale bar represents the z -coordinate information. ( E ) Averaged 1D autocorrelation amplitudes of βIII-spectrin, calculated for the same conditions as in (D). ( F ) SIM images of MAP2 (magenta) and internalized CF568-transferrin (green) in neurons pretreated with DMSO, MDL, or VAD followed by CF568-transferrin treatment. Scale bars, 2 μm. ( G ) Boxplots of transferrin-positive endosome area fractions. ( H ) Confocal fluorescence images of MAP2 (magenta) and internalized HA-mGluR5a (green) in neurons overexpressing HA-mGluR5a pretreated with DMSO, MDL, or VAD followed by anti-HA antibody treatment. Scale bars, 10 μm. ( I ) Boxplots of HA-mGluR5a endosome area fractions. ( J ) Schematic summarizing the proposed positive feedback mechanism: Receptor endocytosis via CME, LRME, or FEME activates ERK signaling, which triggers calpain- and caspase-mediated MPS degradation; MPS disruption in turn facilitates further endocytosis, establishing a positive feedback loop.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating ligand-induced ERK activation via three major endocytic pathways: CME of TfR, LRME of HA-mGluR5a, and FEME of NCAM1. ( B ) Top: Epi-fluorescence images showing pERK immunostaining in neurons without ligand treatment, neurons treated with CF568-transferrin, and neurons overexpressing HA-mGluR5a treated with anti-HA antibody. Bottom: The same as the top but with neurons pretreated with dyngo-4a before ligand treatment. Scale bars, 25 μm. ( C ) Time course of ERK activation in neurons under the same conditions as in (B). ( D ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons under various treatments. First column: neurons pretreated with dimethyl sulfoxide (DMSO), dyngo-4a, U0126, MDL, or VAD. Second column: neurons pretreated with the same inhibitors followed by CF568-transferrin treatment. Third column: neurons overexpressing HA-mGluR5a pretreated with the same inhibitors followed by the anti-HA antibody treatment. Fourth column: neurons pretreated with the same inhibitors followed by anti-NCAM1 antibody treatment. Scale bars, 1 μm. Color scale bar represents the z -coordinate information. ( E ) Averaged 1D autocorrelation amplitudes of βIII-spectrin, calculated for the same conditions as in (D). ( F ) SIM images of MAP2 (magenta) and internalized CF568-transferrin (green) in neurons pretreated with DMSO, MDL, or VAD followed by CF568-transferrin treatment. Scale bars, 2 μm. ( G ) Boxplots of transferrin-positive endosome area fractions. ( H ) Confocal fluorescence images of MAP2 (magenta) and internalized HA-mGluR5a (green) in neurons overexpressing HA-mGluR5a pretreated with DMSO, MDL, or VAD followed by anti-HA antibody treatment. Scale bars, 10 μm. ( I ) Boxplots of HA-mGluR5a endosome area fractions. ( J ) Schematic summarizing the proposed positive feedback mechanism: Receptor endocytosis via CME, LRME, or FEME activates ERK signaling, which triggers calpain- and caspase-mediated MPS degradation; MPS disruption in turn facilitates further endocytosis, establishing a positive feedback loop.

Techniques: Activation Assay, Fluorescence, Immunostaining, Disruption

$( A ) Schematic illustrating the sequential cleavage of APP695 by β-secretase and γ-secretase to produce Aβ42. ( B ) Schematic illustrating the structure of SEP-APP. ( C ) Left: Epi-fluorescence images of pERK in neurons overexpressing SEP-APP without ligand treatment. Middle: The same as the left but treated with GFP nanobody. Right: The same as the middle but with dyngo-4a preincubation before GFP nanobody treatment. Scale bars, 25 μm. ( D ) Time course of ERK activation in neurons under the same conditions as in (C). ( E ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons pretreated with DMSO, dyngo-4a, U0126, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 1 μm. ( F ) Averaged 1D autocorrelation amplitude of βIII-spectrin, calculated for the same conditions as in (E). ( G ) Confocal fluorescence images of CTB (magenta) and internalized SEP-APP (green) in neurons pretreated with DMSO, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 10 μm. ( H ) Boxplots of SEP-APP endosome area fractions. ( I ) Left: Confocal fluorescence images of MAP2 (magenta) and intracellular Aβ42 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 10 μm. ( J ) Boxplots of intracellular Aβ42 area fractions in somatodendritic regions of neurons. ( K ) Left, SIM images of MAP2 (magenta) and cleaved caspase-3 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 2 μm. ( L ) Boxplots of cleaved caspase-3 area fractions in dendrites of neurons. ( M ) Schematic illustrating APP endocytosis triggers downstream ERK signaling, leading to MPS degradation through caspase- and calpain-mediated spectrin cleavage. This degradation further accelerates APP endocytosis, promoting intracellular Aβ42 accumulation and caspase-3 activation.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the sequential cleavage of APP695 by β-secretase and γ-secretase to produce Aβ42. ( B ) Schematic illustrating the structure of SEP-APP. ( C ) Left: Epi-fluorescence images of pERK in neurons overexpressing SEP-APP without ligand treatment. Middle: The same as the left but treated with GFP nanobody. Right: The same as the middle but with dyngo-4a preincubation before GFP nanobody treatment. Scale bars, 25 μm. ( D ) Time course of ERK activation in neurons under the same conditions as in (C). ( E ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons pretreated with DMSO, dyngo-4a, U0126, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 1 μm. ( F ) Averaged 1D autocorrelation amplitude of βIII-spectrin, calculated for the same conditions as in (E). ( G ) Confocal fluorescence images of CTB (magenta) and internalized SEP-APP (green) in neurons pretreated with DMSO, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 10 μm. ( H ) Boxplots of SEP-APP endosome area fractions. ( I ) Left: Confocal fluorescence images of MAP2 (magenta) and intracellular Aβ42 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 10 μm. ( J ) Boxplots of intracellular Aβ42 area fractions in somatodendritic regions of neurons. ( K ) Left, SIM images of MAP2 (magenta) and cleaved caspase-3 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 2 μm. ( L ) Boxplots of cleaved caspase-3 area fractions in dendrites of neurons. ( M ) Schematic illustrating APP endocytosis triggers downstream ERK signaling, leading to MPS degradation through caspase- and calpain-mediated spectrin cleavage. This degradation further accelerates APP endocytosis, promoting intracellular Aβ42 accumulation and caspase-3 activation.

Techniques: Fluorescence, Activation Assay

A MEFs immunolabelled for βII-spectrin (green) and F-actin (phalloidin magenta), imaged by total internal reflection microscopy (TIRFM, scale bar 20 μm). Overlay and single-channel images are shown, as well as zooms related to the square box (1). Images are representative of at least 3 independent experiments. B Frequency distribution of signal intensities per μm 2 . Inset highlights the different signal distributions of F-actin (magenta) and βII-spectrin (green) at high-intensity zones ( n = 40 cells). C Area of high-intensity clusters (P 0.95 of signal intensity distribution) and related aspect ratio ( D ) highlights the smaller and elliptic shape of βII-spectrin and αII-spectrin clusters compared to elongated F-actin (data are presented as mean ± SD, statistical analysis Brown-Forsythe and Welch ANOVA test with multiple comparisons, **** p < 0.0001). E Orientation analysis of endogenous βII-spectrin (green), F-actin (phalloidin, magenta), and αII-spectrin (blue). The vectors highlight the orientation of the signal in the local window for the three independent channels. Coherency heatmaps are shown (LUT 16-colors, scale bar 20 μm). F Distribution of orientations of βII-spectrin (green), F-actin (magenta), and αII-spectrin (blue), normalized to F-actin dominant direction ( n = 40 cells). G Projected cell area of clonal populations KO for βII-spectrin ( sptbn1 ), based on the phalloidin staining presented in H (scale bar 500 μm, n = 3307( + / + ), 1202(Cl.8), 1712(Cl.9), 886(Cl.10) and 527(Cl.15) cells in 3 independent experiments, data are presented as mean ± SD, statistical analysis Brown-Forsythe and Welch ANOVA test with multiple comparisons, **** p -value < 0.0001).

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A MEFs immunolabelled for βII-spectrin (green) and F-actin (phalloidin magenta), imaged by total internal reflection microscopy (TIRFM, scale bar 20 μm). Overlay and single-channel images are shown, as well as zooms related to the square box (1). Images are representative of at least 3 independent experiments. B Frequency distribution of signal intensities per μm 2 . Inset highlights the different signal distributions of F-actin (magenta) and βII-spectrin (green) at high-intensity zones ( n = 40 cells). C Area of high-intensity clusters (P 0.95 of signal intensity distribution) and related aspect ratio ( D ) highlights the smaller and elliptic shape of βII-spectrin and αII-spectrin clusters compared to elongated F-actin (data are presented as mean ± SD, statistical analysis Brown-Forsythe and Welch ANOVA test with multiple comparisons, **** p < 0.0001). E Orientation analysis of endogenous βII-spectrin (green), F-actin (phalloidin, magenta), and αII-spectrin (blue). The vectors highlight the orientation of the signal in the local window for the three independent channels. Coherency heatmaps are shown (LUT 16-colors, scale bar 20 μm). F Distribution of orientations of βII-spectrin (green), F-actin (magenta), and αII-spectrin (blue), normalized to F-actin dominant direction ( n = 40 cells). G Projected cell area of clonal populations KO for βII-spectrin ( sptbn1 ), based on the phalloidin staining presented in H (scale bar 500 μm, n = 3307( + / + ), 1202(Cl.8), 1712(Cl.9), 886(Cl.10) and 527(Cl.15) cells in 3 independent experiments, data are presented as mean ± SD, statistical analysis Brown-Forsythe and Welch ANOVA test with multiple comparisons, **** p -value < 0.0001).

Article Snippet: After the transfer, membranes were blocked in PBS supplemented with 0.1–0.3% Tween20 and 5% milk for 1 h at room temperature, then incubated overnight at 4° with primary antibodies at the following dilutions: mouse anti-βII-spectrin 1:2000 (BD-bioscience), rabbit anti-βII-spectrin 1:2000 (Abcam), and mouse anti-β-tubulin 1:5000 (Sigma-Aldrich).

Techniques: Microscopy, Staining

A Cartoon representation of actin-spectrin tetramers (estimated length ≈ 180/190 nm) and the relative positions of the immuno-reactive epitopes (Y symbols). B The experimental pipeline to enhance the spatial resolution by Expansion Microscopy (ExM). C Representative ExM images of MEFs immunolabelled for βII-spectrin (green) and β-actin (magenta) are shown; in white is reported the “real” scale bar of the image (10 μm) and in red the extrapolated scale according to the expansion factor of 4x. The zooms related to βII-spectrin white boxes (1–6) are shown to highlight periodic clusters ( D ), and the corresponding intensity line scans and peak-to-peak distances are reported (real in white and extrapolated in red). E Representative ExM image showing βII-spectrin (green) in the diffused (zoom 1, white dashed box) and constrained mesh configurations between stress fibers are shown (zoom 2). Images are representative of at least 3 independent experiments. F Nearest Neighbor Distance distributions in the two configurations are calculated for the βII-spectrin epitopes. Adjacent zones within the same cells can display large discrepancies in terms of spectrin organizations (drawn in G ). Panel ( B ) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Cartoon representation of actin-spectrin tetramers (estimated length ≈ 180/190 nm) and the relative positions of the immuno-reactive epitopes (Y symbols). B The experimental pipeline to enhance the spatial resolution by Expansion Microscopy (ExM). C Representative ExM images of MEFs immunolabelled for βII-spectrin (green) and β-actin (magenta) are shown; in white is reported the “real” scale bar of the image (10 μm) and in red the extrapolated scale according to the expansion factor of 4x. The zooms related to βII-spectrin white boxes (1–6) are shown to highlight periodic clusters ( D ), and the corresponding intensity line scans and peak-to-peak distances are reported (real in white and extrapolated in red). E Representative ExM image showing βII-spectrin (green) in the diffused (zoom 1, white dashed box) and constrained mesh configurations between stress fibers are shown (zoom 2). Images are representative of at least 3 independent experiments. F Nearest Neighbor Distance distributions in the two configurations are calculated for the βII-spectrin epitopes. Adjacent zones within the same cells can display large discrepancies in terms of spectrin organizations (drawn in G ). Panel ( B ) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.

Techniques: Microscopy

A Live imaging in dual mode (EPI and TIRF microscopy) of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta). Relevant frames are shown (scale bar 20 μm), as well as dynamic zooms of high-intensity βII-spectrin clusters only observed in the TIRF plane (white dashed boxes). Live images are representative of at least 3 independent experiments. B Temporal analysis of GFP-βII-spectrin clusters evolution (P 0.95 of fluorescent signal intensity distribution). The resulting mask is shown with the clusters outlined, while the color-coded temporal projection is shown for the same cell presented in A, to highlight the dynamic nature of these clusters over time. C Auto-correlation coefficients between subsequent frames related to GFP-βII-spectrin (green) and RFP-actin (magenta) are shown ( n = 8 independent cells and 486 frame pairs analyzed, data are presented as mean ± SD, statistical analysis paired t-test, **** p -value < 0.0001). D Representative frames during time lapse analysis of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta). The vectors highlight the orientation of the signal in the local window for the two channels. Coherency heatmaps are shown. E The graph reports the distribution of orientations of GFP-βII-spectrin (green) and RFP-actin (magenta), normalized to the Actin dominant direction ( n = 8 cells in independent time lapses).

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Live imaging in dual mode (EPI and TIRF microscopy) of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta). Relevant frames are shown (scale bar 20 μm), as well as dynamic zooms of high-intensity βII-spectrin clusters only observed in the TIRF plane (white dashed boxes). Live images are representative of at least 3 independent experiments. B Temporal analysis of GFP-βII-spectrin clusters evolution (P 0.95 of fluorescent signal intensity distribution). The resulting mask is shown with the clusters outlined, while the color-coded temporal projection is shown for the same cell presented in A, to highlight the dynamic nature of these clusters over time. C Auto-correlation coefficients between subsequent frames related to GFP-βII-spectrin (green) and RFP-actin (magenta) are shown ( n = 8 independent cells and 486 frame pairs analyzed, data are presented as mean ± SD, statistical analysis paired t-test, **** p -value < 0.0001). D Representative frames during time lapse analysis of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta). The vectors highlight the orientation of the signal in the local window for the two channels. Coherency heatmaps are shown. E The graph reports the distribution of orientations of GFP-βII-spectrin (green) and RFP-actin (magenta), normalized to the Actin dominant direction ( n = 8 cells in independent time lapses).

Techniques: Imaging, Microscopy, Transfection

$A Schematic pipeline and representative ExM image of MEFs seeded on microfabricated adhesive lines (4 μm adhesive cross-section, 12 μm non-adhesive surface) and immunolabelled for endogenous βII-spectrin (green) and β-actin (magenta). A large volumetric imaging was performed by tile scan approach, and a projection of multiple planes is shown (scale bar: 200 μm). B Two protrusions from independent cells are shown to highlight the differential positioning of βII-spectrin and β-actin, black arrowheads indicate clusters with incomplete periodic organization (scale bar: 20 μm). Images are representative of at least 3 independent experiments. C Live imaging by TIRF microscopy of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta), treated with Jasplakinolide 100 nM and Blebbistatin 10 μM for 3-4 h. Relevant frames are shown to highlight the differential effects on cell shape and protein clustering the two drugs induce (scale bare 20 μm). Cluster area normalized to the initial frames is calculated in response to each treatment and plotted over time ( n = 10 independent cells, data are presented as mean ± SD, statistical analysis: one-way ANOVA of values at t = 100 min). D ExM images of MEFs treated for 3-4 h with 10 μM Blebbistatin and 100 nM Jasplakinolide, immunolabelled for βII-spectrin (scale bars: 20 μm). 30 μm 2 zooms are shown, corresponding to the yellow boxes, to highlight the differential effects of the drugs on spectrin organization. NND values are reported, as well as line scans related to the yellow lines in the zooms (1 and 2). Images are representative of at least 3 independent experiments. E , F Recovery curves resulting from the FRAP assay are shown for GFP-βII-spectrin and GFP-Actin, transiently transfected in MEFs and treated 3-4 h with the different cytoskeletal impairing drugs (Jasplakinolide 100 nM, Blebbistatin 10 μM). Mobile fractions are reported in the graphs (data are presented as mean ± SD, statistical analysis one-way ANOVA with multiple comparisons, *** p- value < 0.005, **** p- value < 0.0001, n = 25-28(GFP-βII-spectrin) and 19-25(RFP-actin) cells in 3 independent experiments). Half-time recovery rates resulting from the fitting of the raw data with a one-exponential equation are reported in the graphs (data are presented as mean ± SD, statistical analysis one-way ANOVA with multiple comparisons, * p -value < 0.05, **** p-value < 0.0001, n = 25-28(GFP-βII-spectrin) and 19-25(RFP-actin) cells in 3 independent experiments). Panel ( A ) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.$

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Schematic pipeline and representative ExM image of MEFs seeded on microfabricated adhesive lines (4 μm adhesive cross-section, 12 μm non-adhesive surface) and immunolabelled for endogenous βII-spectrin (green) and β-actin (magenta). A large volumetric imaging was performed by tile scan approach, and a projection of multiple planes is shown (scale bar: 200 μm). B Two protrusions from independent cells are shown to highlight the differential positioning of βII-spectrin and β-actin, black arrowheads indicate clusters with incomplete periodic organization (scale bar: 20 μm). Images are representative of at least 3 independent experiments. C Live imaging by TIRF microscopy of MEFs transiently transfected with GFP-βII-spectrin (green) and RFP-actin (magenta), treated with Jasplakinolide 100 nM and Blebbistatin 10 μM for 3-4 h. Relevant frames are shown to highlight the differential effects on cell shape and protein clustering the two drugs induce (scale bare 20 μm). Cluster area normalized to the initial frames is calculated in response to each treatment and plotted over time ( n = 10 independent cells, data are presented as mean ± SD, statistical analysis: one-way ANOVA of values at t = 100 min). D ExM images of MEFs treated for 3-4 h with 10 μM Blebbistatin and 100 nM Jasplakinolide, immunolabelled for βII-spectrin (scale bars: 20 μm). 30 μm 2 zooms are shown, corresponding to the yellow boxes, to highlight the differential effects of the drugs on spectrin organization. NND values are reported, as well as line scans related to the yellow lines in the zooms (1 and 2). Images are representative of at least 3 independent experiments. E , F Recovery curves resulting from the FRAP assay are shown for GFP-βII-spectrin and GFP-Actin, transiently transfected in MEFs and treated 3-4 h with the different cytoskeletal impairing drugs (Jasplakinolide 100 nM, Blebbistatin 10 μM). Mobile fractions are reported in the graphs (data are presented as mean ± SD, statistical analysis one-way ANOVA with multiple comparisons, *** p- value < 0.005, **** p- value < 0.0001, n = 25-28(GFP-βII-spectrin) and 19-25(RFP-actin) cells in 3 independent experiments). Half-time recovery rates resulting from the fitting of the raw data with a one-exponential equation are reported in the graphs (data are presented as mean ± SD, statistical analysis one-way ANOVA with multiple comparisons, * p -value < 0.05, **** p-value < 0.0001, n = 25-28(GFP-βII-spectrin) and 19-25(RFP-actin) cells in 3 independent experiments). Panel ( A ) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.

Techniques: Adhesive, Imaging, Microscopy, Transfection, FRAP Assay

A Schematic representation of the βII-spectrin FRET-based tension sensor. ∆ABD (red) lacks the actin-binding domain, while the FRET pair (cpst-Cerulean and cpst-Venus) is inserted between the Actin Binding Domain and the central rod in the full-length counterpart (FL, blue). B InvFRET is calculated according to Meng and Sachs (2012): higher ratio reflects a higher tensional state (lower FRET) and vice versa, the expected relationship between tension and fluorescence intensity of the acceptor is also reported. C Representative FRET images are shown (scale bar 20 μm). Pixel-by-pixel analysis was performed in at least n = 90 cells per condition, and scatter plots show the local relationship between the invFRET and Venus intensity. Contours of 2D Kernel densities are reported with the corresponding calibration bar, Pearson’s correlation coefficients as well as coefficient of Variation (CV, defined as the ratio of the standard deviation to the mean) are also reported. The frequency distribution of the invFRET highlights the peculiar behavior of the FL βII-spectrin FRET-based tension sensor upon Jasplakinolide treatment, which displayed a unique bimodal distribution with the appearance of low invFRET values in correspondence of high-intensity Venus (highlighted by the red box). The same was not observed in any other experimental conditions. Mean ± SD values are reported. D Cartoon representation of the differential configurations of the spectrin mesh upon drug perturbations, and the relationship with tension.

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Schematic representation of the βII-spectrin FRET-based tension sensor. ∆ABD (red) lacks the actin-binding domain, while the FRET pair (cpst-Cerulean and cpst-Venus) is inserted between the Actin Binding Domain and the central rod in the full-length counterpart (FL, blue). B InvFRET is calculated according to Meng and Sachs (2012): higher ratio reflects a higher tensional state (lower FRET) and vice versa, the expected relationship between tension and fluorescence intensity of the acceptor is also reported. C Representative FRET images are shown (scale bar 20 μm). Pixel-by-pixel analysis was performed in at least n = 90 cells per condition, and scatter plots show the local relationship between the invFRET and Venus intensity. Contours of 2D Kernel densities are reported with the corresponding calibration bar, Pearson’s correlation coefficients as well as coefficient of Variation (CV, defined as the ratio of the standard deviation to the mean) are also reported. The frequency distribution of the invFRET highlights the peculiar behavior of the FL βII-spectrin FRET-based tension sensor upon Jasplakinolide treatment, which displayed a unique bimodal distribution with the appearance of low invFRET values in correspondence of high-intensity Venus (highlighted by the red box). The same was not observed in any other experimental conditions. Mean ± SD values are reported. D Cartoon representation of the differential configurations of the spectrin mesh upon drug perturbations, and the relationship with tension.

Techniques: Binding Assay, Fluorescence, Standard Deviation

A Idealized cell showing periodic spectrin (green bundles) between stress fibers (magenta). The square box shows a magnification of the spectrin cluster. A schematic picture of the stress fibers (pink) attached to the extracellular space through focal adhesions (purple) creating contractile stress is shown at the bottom. B Initial configuration of the modeled spectrin cluster showing spectrin bundles (green edges), myosin (magenta), and stress fibers (black lines). The short actin filaments are depicted by purple circles. Black full circles correspond to focal adhesions that can move vertically, as shown by the purple arrows. C Histogram showing the initial and final length of spectrin filaments that are initially smaller (larger) than the resting length thereby acting as a compressed (stretched) spring and exerting a restorative positive (negative) force on the mesh. The time to reach such a state is 60 s. The corresponding meshes are in Supplementary Fig. . D Spectrin mesh with spring elements attached to fixed focal adhesions (black dots) through cable elements (black edges). E Final configuration after equilibration (120 s) of the network without allowing for any spectrin removal for the mesh shown in ( D ). F Configuration of the network in ( D ) after equilibration allowing spectrin bundles to detach when the force generated by the spring element is above F th . The histogram shows the number of spectrin bundles per short-actin filament. Zooms of the final configurations are highlighted in squared boxes. G Spectrin mesh with the spring elements attached to stress fibers represented by black edges. The stress fibers have spring and cable elements connected by black empty circles. Solid circles represent fixed focal adhesions. H , I Final configuration of the network in ( G ), allowing spectrin bundle removal. In ( I ), focal adhesions are vertically pulled together during the first half of the simulation. In the second half, focal adhesions are fixed. The total duration is 600 s. Histograms represent the number of connected spectrin bundles per short-actin filament.

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Idealized cell showing periodic spectrin (green bundles) between stress fibers (magenta). The square box shows a magnification of the spectrin cluster. A schematic picture of the stress fibers (pink) attached to the extracellular space through focal adhesions (purple) creating contractile stress is shown at the bottom. B Initial configuration of the modeled spectrin cluster showing spectrin bundles (green edges), myosin (magenta), and stress fibers (black lines). The short actin filaments are depicted by purple circles. Black full circles correspond to focal adhesions that can move vertically, as shown by the purple arrows. C Histogram showing the initial and final length of spectrin filaments that are initially smaller (larger) than the resting length thereby acting as a compressed (stretched) spring and exerting a restorative positive (negative) force on the mesh. The time to reach such a state is 60 s. The corresponding meshes are in Supplementary Fig. . D Spectrin mesh with spring elements attached to fixed focal adhesions (black dots) through cable elements (black edges). E Final configuration after equilibration (120 s) of the network without allowing for any spectrin removal for the mesh shown in ( D ). F Configuration of the network in ( D ) after equilibration allowing spectrin bundles to detach when the force generated by the spring element is above F th . The histogram shows the number of spectrin bundles per short-actin filament. Zooms of the final configurations are highlighted in squared boxes. G Spectrin mesh with the spring elements attached to stress fibers represented by black edges. The stress fibers have spring and cable elements connected by black empty circles. Solid circles represent fixed focal adhesions. H , I Final configuration of the network in ( G ), allowing spectrin bundle removal. In ( I ), focal adhesions are vertically pulled together during the first half of the simulation. In the second half, focal adhesions are fixed. The total duration is 600 s. Histograms represent the number of connected spectrin bundles per short-actin filament.

Techniques: Generated

A Live imaging by TIRF microscopy of MEFs transiently transfected with GFP-βII-spectrin (green) and mCherry-MLC (magenta) seeded on microfabricated adhesive lines (not stained, gray dashes) to force discrete cortical organizations (scale bar = 20 μm). Live images are representative of at least 3 independent experiments. Three different regions are highlighted and display representative cortical dynamics (1–3). Automated tracking of mCherry-MLC puncta with two different filtering parameters: in ( B ), all tracks are shown in a single representative frame, while in ( C ) only long-lived tracks (> 150 s) preferentially localized on stress fibers. D Pulsative myosin dynamics is shown at spectrin-rich cortical domains (5 × 5 μm zoom). GFP-βII-spectrin and mCherry-MLC clustering are highlighted by white and yellow arrowheads respectively. Kymograph qualitative analysis showed fenestration in the GFP-βII-spectrin signal (white arrowheads) in correspondence with the mCherry-MLC pulse (yellow arrowhead). The yellow bar highlighted an MLC pulse of ≈ 60 s. E Differential lifetime of MLC puncta presented in ( B ) (All MLC Tracking) and ( C ) (Long-lived MLC Tracking), data are presented as the center (median), box (25th to 75th IQR), whiskers (min and max) ( n = 2200-6965 tracks in 5 independent cells, statistical analysis Mann-Whitney test **** p- value < 0.0001). F Top: initial configuration of the theoretical model where the spectrin mesh is attached to the stress fibers (black edges) through myosin linkers with cable elements (magenta lines, with empty circles at their ends). Myosin rods with less rigid cable elements are randomly distributed in the mesh. Focal adhesions are pulled together at a constant velocity during the first 300 s of the simulation, after which, they are held fixed. The total duration of the simulation is 600 s. Bottom: position of the short-actin filaments at the end of the simulation (equilibration), color-coded to represent the number of attached spectrin bundles per node. G Histograms denote the initial and final number of spectrin bundles per short-actin filament. H Boxplot of the lifetime of the myosin rods in the spectrin network for the two different simulation conditions ( n = 5 single myosin, n = 11 dynamic myosin), data are presented as center (median), box (25th to 75th IQR), whiskers (min and max). I The phase diagram integrates the different experimental and theoretical parameters identified in this study to explain the contribution of the different players in the topological transition of the spectrin meshwork. Panel (I) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.

Journal: Nature Communications

Article Title: Mechanically induced topological transition of spectrin regulates its distribution in the mammalian cell cortex

doi: 10.1038/s41467-024-49906-6

Figure Lengend Snippet: A Live imaging by TIRF microscopy of MEFs transiently transfected with GFP-βII-spectrin (green) and mCherry-MLC (magenta) seeded on microfabricated adhesive lines (not stained, gray dashes) to force discrete cortical organizations (scale bar = 20 μm). Live images are representative of at least 3 independent experiments. Three different regions are highlighted and display representative cortical dynamics (1–3). Automated tracking of mCherry-MLC puncta with two different filtering parameters: in ( B ), all tracks are shown in a single representative frame, while in ( C ) only long-lived tracks (> 150 s) preferentially localized on stress fibers. D Pulsative myosin dynamics is shown at spectrin-rich cortical domains (5 × 5 μm zoom). GFP-βII-spectrin and mCherry-MLC clustering are highlighted by white and yellow arrowheads respectively. Kymograph qualitative analysis showed fenestration in the GFP-βII-spectrin signal (white arrowheads) in correspondence with the mCherry-MLC pulse (yellow arrowhead). The yellow bar highlighted an MLC pulse of ≈ 60 s. E Differential lifetime of MLC puncta presented in ( B ) (All MLC Tracking) and ( C ) (Long-lived MLC Tracking), data are presented as the center (median), box (25th to 75th IQR), whiskers (min and max) ( n = 2200-6965 tracks in 5 independent cells, statistical analysis Mann-Whitney test **** p- value < 0.0001). F Top: initial configuration of the theoretical model where the spectrin mesh is attached to the stress fibers (black edges) through myosin linkers with cable elements (magenta lines, with empty circles at their ends). Myosin rods with less rigid cable elements are randomly distributed in the mesh. Focal adhesions are pulled together at a constant velocity during the first 300 s of the simulation, after which, they are held fixed. The total duration of the simulation is 600 s. Bottom: position of the short-actin filaments at the end of the simulation (equilibration), color-coded to represent the number of attached spectrin bundles per node. G Histograms denote the initial and final number of spectrin bundles per short-actin filament. H Boxplot of the lifetime of the myosin rods in the spectrin network for the two different simulation conditions ( n = 5 single myosin, n = 11 dynamic myosin), data are presented as center (median), box (25th to 75th IQR), whiskers (min and max). I The phase diagram integrates the different experimental and theoretical parameters identified in this study to explain the contribution of the different players in the topological transition of the spectrin meshwork. Panel (I) was created with BioRender.com and released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license.

Techniques: Imaging, Microscopy, Transfection, Adhesive, Staining, MANN-WHITNEY

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