rabbit polyclonal anti atp7a  (Hycult Biotech)


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    Structured Review

    Hycult Biotech rabbit polyclonal anti atp7a
    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for <t>ATP7A</t> and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
    Rabbit Polyclonal Anti Atp7a, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti atp7a/product/Hycult Biotech
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti atp7a - by Bioz Stars, 2024-07
    90/100 stars

    Images

    1) Product Images from "Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway"

    Article Title: Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway

    Journal: Nature Communications

    doi: 10.1038/ncomms10640

    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
    Figure Legend Snippet: ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).

    Techniques Used: Immunostaining, Marker, Expressing, Staining


    Structured Review

    Affinity Biosciences polyclonal anti rabbit anti atp7a antibody
    Polyclonal Anti Rabbit Anti Atp7a Antibody, supplied by Affinity Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti rabbit anti atp7a antibody/product/Affinity Biosciences
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti rabbit anti atp7a antibody - by Bioz Stars, 2024-07
    86/100 stars

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    Structured Review

    Affinity Biosciences polyclonal anti rabbit anti atp7a antibody
    Schematic representation of the role of <t>ATP7A</t> and ATP7B proteins in response to Cu exposure in enterocytes ( A ) and in hepatocytes ( B ). In both cell types, Cu is initially taken up via the Cu transporter 1 (CTR1). It is then guided by the Cu chaperone ATOX1 protein to reach ATP7A or ATP7B located within the trans-Golgi network (TGN). Upon an increase in Cu levels, ATP7A and ATP7B relocate from the TGN to the outer edges of the cell. In enterocytes, ATP7A promotes Cu excretion into the bloodstream from the basolateral side, while in hepatocytes, Cu is expelled from the apical side into the bile [ , ].
    Polyclonal Anti Rabbit Anti Atp7a Antibody, supplied by Affinity Biosciences, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti rabbit anti atp7a antibody/product/Affinity Biosciences
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti rabbit anti atp7a antibody - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "Response of Fibroblasts from Menkes’ and Wilson’s Copper Metabolism-Related Disorders to Ionizing Radiation: Influence of the Nucleo-Shuttling of the ATM Protein Kinase"

    Article Title: Response of Fibroblasts from Menkes’ and Wilson’s Copper Metabolism-Related Disorders to Ionizing Radiation: Influence of the Nucleo-Shuttling of the ATM Protein Kinase

    Journal: Biomolecules

    doi: 10.3390/biom13121746

    Schematic representation of the role of ATP7A and ATP7B proteins in response to Cu exposure in enterocytes ( A ) and in hepatocytes ( B ). In both cell types, Cu is initially taken up via the Cu transporter 1 (CTR1). It is then guided by the Cu chaperone ATOX1 protein to reach ATP7A or ATP7B located within the trans-Golgi network (TGN). Upon an increase in Cu levels, ATP7A and ATP7B relocate from the TGN to the outer edges of the cell. In enterocytes, ATP7A promotes Cu excretion into the bloodstream from the basolateral side, while in hepatocytes, Cu is expelled from the apical side into the bile [ , ].
    Figure Legend Snippet: Schematic representation of the role of ATP7A and ATP7B proteins in response to Cu exposure in enterocytes ( A ) and in hepatocytes ( B ). In both cell types, Cu is initially taken up via the Cu transporter 1 (CTR1). It is then guided by the Cu chaperone ATOX1 protein to reach ATP7A or ATP7B located within the trans-Golgi network (TGN). Upon an increase in Cu levels, ATP7A and ATP7B relocate from the TGN to the outer edges of the cell. In enterocytes, ATP7A promotes Cu excretion into the bloodstream from the basolateral side, while in hepatocytes, Cu is expelled from the apical side into the bile [ , ].

    Techniques Used:

    Expression of the ATP7A and ATP7B proteins in MD and WD fibroblasts. Anti-ATP7A and anti-ATP7B immunoblots with total or cytoplasmic protein extracts were applied to the indicated non-irradiated control Hs27, MD ( A , B ), and WD ( C , D ) fibroblasts. The grey levels corresponding to each condition are shown in . Original western blot images can be found in raw data.
    Figure Legend Snippet: Expression of the ATP7A and ATP7B proteins in MD and WD fibroblasts. Anti-ATP7A and anti-ATP7B immunoblots with total or cytoplasmic protein extracts were applied to the indicated non-irradiated control Hs27, MD ( A , B ), and WD ( C , D ) fibroblasts. The grey levels corresponding to each condition are shown in . Original western blot images can be found in raw data.

    Techniques Used: Expressing, Western Blot, Irradiation

    Interaction between ATM and ATP7A or ATP7B proteins observed by applying the proximity ligation assay (PLA). The PLA was applied to the indicated MD ( A , B ) and WD ( C , D ) cell lines that were exposed ( B , D ) or not to two Gy X-rays followed by 10 min ( A , C ). Representative PLA images of ATM–ATP7A or ATM–ATP7B complexes observed in the indicated MD, WD, and control cells. The nuclei were counterstained with DAPI (blue). The red foci indicate an ATM-ATP7 protein complex. The average numbers of red foci were scored per 100 cells. Each data point represents the mean ± SEM of two independent replicates. * and *** asterisks represent a p < 0.05 and p < 0.001 difference by comparison to controls data, respectively. White bars represent 30 µm.
    Figure Legend Snippet: Interaction between ATM and ATP7A or ATP7B proteins observed by applying the proximity ligation assay (PLA). The PLA was applied to the indicated MD ( A , B ) and WD ( C , D ) cell lines that were exposed ( B , D ) or not to two Gy X-rays followed by 10 min ( A , C ). Representative PLA images of ATM–ATP7A or ATM–ATP7B complexes observed in the indicated MD, WD, and control cells. The nuclei were counterstained with DAPI (blue). The red foci indicate an ATM-ATP7 protein complex. The average numbers of red foci were scored per 100 cells. Each data point represents the mean ± SEM of two independent replicates. * and *** asterisks represent a p < 0.05 and p < 0.001 difference by comparison to controls data, respectively. White bars represent 30 µm.

    Techniques Used: Proximity Ligation Assay, Comparison

    Summary of the major biological and radiobiological features of MD and WD fibroblasts.
    Figure Legend Snippet: Summary of the major biological and radiobiological features of MD and WD fibroblasts.

    Techniques Used: Expressing, Transformation Assay

    Radiobiological characterization of MD and WD cells. Schematic illustration of the RIANS model. In the case of radioresistant cells, MD, and WD cells, the model shows that radiation-induced ATM monomers diffuse in the nucleus. Once in the nucleus, ATM monomers initiate DSB recognition and repair via the phosphorylation of H2AX histones. In MD cells, ATP7A mutations result in the disappearance or the non-availability of ATP7A Conversely the ATP7B protein is overexpressed in cytoplasm and may sequestrate ATM in the cytoplasm, which may delay the RIANS. In WD cells, ATP7B mutations cause an impaired cytoplasmic localization of the ATP7B protein and its overexpression. However, the ATP7A protein is also expressed. After irradiation, a number of ATM–ATP7B complexes, and less frequently of ATM–ATP7A protein result in a delayed RIANS. IR: ionizing radiation.
    Figure Legend Snippet: Radiobiological characterization of MD and WD cells. Schematic illustration of the RIANS model. In the case of radioresistant cells, MD, and WD cells, the model shows that radiation-induced ATM monomers diffuse in the nucleus. Once in the nucleus, ATM monomers initiate DSB recognition and repair via the phosphorylation of H2AX histones. In MD cells, ATP7A mutations result in the disappearance or the non-availability of ATP7A Conversely the ATP7B protein is overexpressed in cytoplasm and may sequestrate ATM in the cytoplasm, which may delay the RIANS. In WD cells, ATP7B mutations cause an impaired cytoplasmic localization of the ATP7B protein and its overexpression. However, the ATP7A protein is also expressed. After irradiation, a number of ATM–ATP7B complexes, and less frequently of ATM–ATP7A protein result in a delayed RIANS. IR: ionizing radiation.

    Techniques Used: Over Expression, Irradiation


    Structured Review

    Absolute Biotech Inc rabbit polyclonal igg antibody against atp7a
    (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased <t>ATP7A</t> and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.
    Rabbit Polyclonal Igg Antibody Against Atp7a, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal igg antibody against atp7a/product/Absolute Biotech Inc
    Average 86 stars, based on 1 article reviews
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    Images

    1) Product Images from "Effect of flavonoids hydroxygenkwanin on vascular smooth muscle cell proliferation, migration, and neointimal formation"

    Article Title: Effect of flavonoids hydroxygenkwanin on vascular smooth muscle cell proliferation, migration, and neointimal formation

    Journal: bioRxiv

    doi: 10.1101/2022.12.20.521220

    (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased ATP7A and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.
    Figure Legend Snippet: (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased ATP7A and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.

    Techniques Used: Expressing, Immunoprecipitation, Western Blot, Translocation Assay, Immunofluorescence, Staining

    rabbit polyclonal anti atp7a antibody  (Danaher Inc)


    Bioz Verified Symbol Danaher Inc is a verified supplier
    Bioz Manufacturer Symbol Danaher Inc manufactures this product  
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  • 86

    Structured Review

    Danaher Inc rabbit polyclonal anti atp7a antibody
    Rabbit Polyclonal Anti Atp7a Antibody, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti atp7a antibody/product/Danaher Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti atp7a antibody - by Bioz Stars, 2024-07
    86/100 stars

    Images


    Structured Review

    Abcam rabbit polyclonal anti atp7a antibody
    A – Colocalization of <t>ATP7A</t> with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
    Rabbit Polyclonal Anti Atp7a Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti atp7a antibody/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti atp7a antibody - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia"

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    Journal: bioRxiv

    doi: 10.1101/2021.03.18.435926

    A – Colocalization of ATP7A with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
    Figure Legend Snippet: A – Colocalization of ATP7A with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.

    Techniques Used:

    ATP7A has been represented in green and the TGN markers and RAB7 in red. Image acquired by S timulated E mission D epletion (STED) microscopy.
    Figure Legend Snippet: ATP7A has been represented in green and the TGN markers and RAB7 in red. Image acquired by S timulated E mission D epletion (STED) microscopy.

    Techniques Used: Microscopy

    ATP7A containing vesicles do not colocalize with LAMP1 in the differentiated C-6 (glia) cells.
    Figure Legend Snippet: ATP7A containing vesicles do not colocalize with LAMP1 in the differentiated C-6 (glia) cells.

    Techniques Used:

    ATP7A containing vesicles do not colocalize with gamma-tubulin in the differentiated C-6 (glia) cells.
    Figure Legend Snippet: ATP7A containing vesicles do not colocalize with gamma-tubulin in the differentiated C-6 (glia) cells.

    Techniques Used:

    Localization of ATP7A in the RAB11 positive compartment in the perinuclear region (soma) and along the neurites in the differentiated C-6 (glia) cells.
    Figure Legend Snippet: Localization of ATP7A in the RAB11 positive compartment in the perinuclear region (soma) and along the neurites in the differentiated C-6 (glia) cells.

    Techniques Used:

    A: Orthogonal (X/Y) images of ATP7A and RAB11 in the undifferentiated and differentiated C-6 cells has been represented. Region highlighted by boxes in the differentiated cell has been enlarged and represented in panel B. B – Orthogonal (X/Y) images of the enlarged perinuclear (soma) and neurite of a single cell, demonstrated in the panel A (right) and , have been represented.
    Figure Legend Snippet: A: Orthogonal (X/Y) images of ATP7A and RAB11 in the undifferentiated and differentiated C-6 cells has been represented. Region highlighted by boxes in the differentiated cell has been enlarged and represented in panel B. B – Orthogonal (X/Y) images of the enlarged perinuclear (soma) and neurite of a single cell, demonstrated in the panel A (right) and , have been represented.

    Techniques Used:

    A (upper): ATP7A colocalizes with RAB11 in the perinuclear soma. A (lower): A Magnified area from the upper panel shows both ATP7A overlapping and juxtaposing with RAB11 demonstrating its presence in the RAB11 positive compartment. B (upper): ATP7A colocalizing with RAB11 positive compartments in the neurites. B (Lower): Magnified area from the upper panel shows colocalization and juxtaposition with RAB11.
    Figure Legend Snippet: A (upper): ATP7A colocalizes with RAB11 in the perinuclear soma. A (lower): A Magnified area from the upper panel shows both ATP7A overlapping and juxtaposing with RAB11 demonstrating its presence in the RAB11 positive compartment. B (upper): ATP7A colocalizing with RAB11 positive compartments in the neurites. B (Lower): Magnified area from the upper panel shows colocalization and juxtaposition with RAB11.

    Techniques Used:

    A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the perinuclear region of the differentiated C-6 (glia). B – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region of the glia. C – An enlarged region showing exclusive and overlapping TGN38+Golgin97 and RAB11 positive compartments (left) and merged image (right) showing localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region. D – Graph showing ATP7A distribution in the overlapping and exclusive RAB11 and TGN38+Golgin97 compartments in the perinuclear region.
    Figure Legend Snippet: A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the perinuclear region of the differentiated C-6 (glia). B – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region of the glia. C – An enlarged region showing exclusive and overlapping TGN38+Golgin97 and RAB11 positive compartments (left) and merged image (right) showing localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region. D – Graph showing ATP7A distribution in the overlapping and exclusive RAB11 and TGN38+Golgin97 compartments in the perinuclear region.

    Techniques Used:

    A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the neurites of the differentiated C-6 (glia). B (left) – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating colocalization of ATP7A (green) with RAB11 (red) and not TGN38+Golgin97 (cyan) in the neurite. The nuclei have been indicated in blue. B (right) – An enlarged region, in the neurite showing colocalization of ATP7A with RAB11 and lack of any colocalization of ATP7A with TGN38+Golgin97.
    Figure Legend Snippet: A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the neurites of the differentiated C-6 (glia). B (left) – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating colocalization of ATP7A (green) with RAB11 (red) and not TGN38+Golgin97 (cyan) in the neurite. The nuclei have been indicated in blue. B (right) – An enlarged region, in the neurite showing colocalization of ATP7A with RAB11 and lack of any colocalization of ATP7A with TGN38+Golgin97.

    Techniques Used:

    C-6 cells were differentiated as described, and then treated with 30uM TTM for 2 hours. Disappearance of the ATP7A containing vesicles along the neurites and retention of ATP7A in the TGN38 and Golgin97 positive Trans Golgi Network (TGN) is observed in response to the copper chelation.
    Figure Legend Snippet: C-6 cells were differentiated as described, and then treated with 30uM TTM for 2 hours. Disappearance of the ATP7A containing vesicles along the neurites and retention of ATP7A in the TGN38 and Golgin97 positive Trans Golgi Network (TGN) is observed in response to the copper chelation.

    Techniques Used:

    C-6 cells are plated and differentiated in the presence of 30uM Ammonium Tetrathiomolybdate (TTM). A – Bright field image of the C-6 cells differentiated in presence and absence of TTM. B – Relative mRNA level of GFAP in the glial cells differentiated in presence and absence of TTM (no of replicate – 3). C - ATP7A localization in the glial cells differentiated in presence and absence of TTM.
    Figure Legend Snippet: C-6 cells are plated and differentiated in the presence of 30uM Ammonium Tetrathiomolybdate (TTM). A – Bright field image of the C-6 cells differentiated in presence and absence of TTM. B – Relative mRNA level of GFAP in the glial cells differentiated in presence and absence of TTM (no of replicate – 3). C - ATP7A localization in the glial cells differentiated in presence and absence of TTM.

    Techniques Used:

    Left: Differentiation of the PC-12 cells involve increased level of the CTR1 (blue cylinder) resulting into an increased intracellular copper (golden sphere). A bulk of the cytosolic copper is reportedly utilized by the Golgi based secretory pathway. Cytosolic copper binds to MEK1/2 (green circle with spikes) and triggers ERK1/2 phosphorylation (green ellipse) which is crucial for the viability of the neurons. ATP7A (orange cylinder) is retained in the TGN, despite high intracellular copper. Right: Differentiated C-6 (glia) have low intracellular copper and thereby downregulation of the copper dependent ERK1/2 phosphorylation. ATP7A localizes in the TGN38 and RAB11 positive compartments in the perinuclear region. In addition, ATP7A localizes into the RAB11 positive vesicles in the neurites (inset) despite low intracellular copper.
    Figure Legend Snippet: Left: Differentiation of the PC-12 cells involve increased level of the CTR1 (blue cylinder) resulting into an increased intracellular copper (golden sphere). A bulk of the cytosolic copper is reportedly utilized by the Golgi based secretory pathway. Cytosolic copper binds to MEK1/2 (green circle with spikes) and triggers ERK1/2 phosphorylation (green ellipse) which is crucial for the viability of the neurons. ATP7A (orange cylinder) is retained in the TGN, despite high intracellular copper. Right: Differentiated C-6 (glia) have low intracellular copper and thereby downregulation of the copper dependent ERK1/2 phosphorylation. ATP7A localizes in the TGN38 and RAB11 positive compartments in the perinuclear region. In addition, ATP7A localizes into the RAB11 positive vesicles in the neurites (inset) despite low intracellular copper.

    Techniques Used:


    Structured Review

    Abcam rabbit polyclonal antibodies anti atp7a
    Rabbit Polyclonal Antibodies Anti Atp7a, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antibodies anti atp7a/product/Abcam
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antibodies anti atp7a - by Bioz Stars, 2024-07
    86/100 stars

    Images


    Structured Review

    Santa Cruz Biotechnology rabbit polyclonal anti atp7a antibody
    Rabbit Polyclonal Anti Atp7a Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal anti atp7a antibody  (Novus Biologicals)


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    Novus Biologicals rabbit polyclonal anti atp7a antibody
    Rabbit Polyclonal Anti Atp7a Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Structured Review

    Santa Cruz Biotechnology rabbit polyclonal anti atp7a antibody
    Rabbit Polyclonal Anti Atp7a Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal anti atp7a  (Hycult Biotech)


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    Hycult Biotech rabbit polyclonal anti atp7a
    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for <t>ATP7A</t> and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
    Rabbit Polyclonal Anti Atp7a, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway"

    Article Title: Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway

    Journal: Nature Communications

    doi: 10.1038/ncomms10640

    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
    Figure Legend Snippet: ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).

    Techniques Used: Immunostaining, Marker, Expressing, Staining

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    Hycult Biotech rabbit polyclonal anti atp7a
    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for <t>ATP7A</t> and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
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    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for <t>ATP7A</t> and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).
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    (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased <t>ATP7A</t> and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.
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    (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased <t>ATP7A</t> and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.
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    A – Colocalization of <t>ATP7A</t> with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
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    A – Colocalization of <t>ATP7A</t> with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
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    A – Colocalization of <t>ATP7A</t> with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
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    A – Colocalization of <t>ATP7A</t> with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.
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    Image Search Results


    ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).

    Journal: Nature Communications

    Article Title: Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway

    doi: 10.1038/ncomms10640

    Figure Lengend Snippet: ( a ) Immunostaining of PAM (green) in a chicken spinal cord (HH stage 20 embryo). Traverse sections of chick embryos were analysed. Differentiated cells in marginal zones were identified by postmitotic marker isl1/2 (red). Scale bar, 50 μm. ( b ) Intensity profile along the line indicated by the arrow in a shows overlap between PAM and Isl1/2 expression. Medial and lateral borders are represented as M and L, respevtively. ( c ) Schematic of differentiation of SH-SY5Y cells by sequential treatments with retinoic acid (DIF RA) and BDNF (DIF BDNF). ( d ) Differentiation is associated with upregulation of genes involved in copper fluxes to mitochondria and, especially, the secretory pathway. The mRNA levels were determined by ΔΔCt analysis using GAPDH as a reference gene and normalized to non-differentiated cells (red line). Each value is presented as mean±s.d. ( n =3). ( e ) Protein levels for ATP7A and Atox1 increase upon differentiation. Equal amount of protein was loaded to each lane. Neuronal differentiation was verified by upregulation of MAP2. ( f ) Cellular copper content in differentiated SH-SY5Y cells (BDNF) is higher than in non-differentiated (ND) cells. Copper amounts were determined by atomic absorption and normalized to protein amounts. Data from three independent measurements. ( g , h ) ATP7A is localized within TGN and vesicular structures which are distinct from endosomal or lysosomal compartments. Coimmunostaining with TGN was shown as a representative image (see for other images). Nucleus was stained with DAPI (blue). Scale bar, 10 μm. Colocalization of ATP7A and various markers were evaluated using Pearson's product-moment coefficients. Three replicate samples were prepared and analysed. Each value is presented as mean±s.d. ( n =3).

    Article Snippet: Primary antibodies used in cell staining were mouse monoclonal anti-FLAG M2 clone (Sigma, F1804), rabbit polyclonal anti-ATP7A (Hycult Biotech, HP8040), mouse monoclonal anti-ATP7A (Santa Cruz, 376467), mouse monoclonal anti-EEA1 (BD Biosciences, 610456), mouse monoclonal anti-Rab11 (BD Biosciences, 610656), mouse monoclonal anti-Lamp1 (developmental studies hybridoma bank, H4A3-s), and sheep monoclonal anti-TGN46 (Gene Tex, GTX74290).

    Techniques: Immunostaining, Marker, Expressing, Staining

    (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased ATP7A and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.

    Journal: bioRxiv

    Article Title: Effect of flavonoids hydroxygenkwanin on vascular smooth muscle cell proliferation, migration, and neointimal formation

    doi: 10.1101/2022.12.20.521220

    Figure Lengend Snippet: (A) An RNA transcriptome analysis was performed to analyze the gene expression profile of PDGF-BB (PDGF)-treated VSMCs treated with or without HGK(PDGF/HGK). (B) A volcano plot of the 13 differentially regulated mRNA transcripts (shown in blue and red). ATP7 was one of the most upregulated annotated genes and is indicated with a circle. (C) Immunoprecipitation showed that treatment with 10 μM HGK or 1 μM MK2206 decreased ATP7A and Rac1 colocalization. (D) Western blot analysis showed that treatment with 10 μM HGK or 1 μM MK2206 decreased PDGF-induced Rac1 translocation from the cytosolic compartment to the membrane compartment. GAPDH or Na+/K+-ATPase was processed in parallel as an internal control for protein loading. (E) Immunofluorescence staining showed that pretreatment with 10 μM HGK or 1 μM MK2206 decreased PDGF (20 ng/ml)-induced ATP7A and Rac1 colocalization and translocation. The scale bar represents 12.5 μm in (E). Nuclei were stained with DAPI. The values are presented as the means ± SDs. *p < 0.05 compared with the CTRL group. †p < 0.05 compared with the PDGF group. N=5-10. CTRL, control group. Statistical comparisons were performed using one-way ANOVA.

    Article Snippet: A rabbit polyclonal IgG antibody against ATP7A was purchased from LSBio (Seattle, WA, USA).

    Techniques: Expressing, Immunoprecipitation, Western Blot, Translocation Assay, Immunofluorescence, Staining

    A – Colocalization of ATP7A with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: A – Colocalization of ATP7A with TGN38 in the PC-12 cells. ATP7A colocalizes primarily with TGN38 in the perinuclear (soma) area. B – Colocalization of ATP7A with TGN38 and Golgin 97 in the C-6 cells. ATP7A localizes into the vesicular structures in the neurites in addition to the perinuclear localization. ATP7A colocalizes with TGN38 and Golgin97 in the perinuclear area. However, there is no colocalization of ATP7A containing vesicles in the neurites with the TGN markers.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    ATP7A has been represented in green and the TGN markers and RAB7 in red. Image acquired by S timulated E mission D epletion (STED) microscopy.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: ATP7A has been represented in green and the TGN markers and RAB7 in red. Image acquired by S timulated E mission D epletion (STED) microscopy.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques: Microscopy

    ATP7A containing vesicles do not colocalize with LAMP1 in the differentiated C-6 (glia) cells.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: ATP7A containing vesicles do not colocalize with LAMP1 in the differentiated C-6 (glia) cells.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    ATP7A containing vesicles do not colocalize with gamma-tubulin in the differentiated C-6 (glia) cells.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: ATP7A containing vesicles do not colocalize with gamma-tubulin in the differentiated C-6 (glia) cells.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    Localization of ATP7A in the RAB11 positive compartment in the perinuclear region (soma) and along the neurites in the differentiated C-6 (glia) cells.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: Localization of ATP7A in the RAB11 positive compartment in the perinuclear region (soma) and along the neurites in the differentiated C-6 (glia) cells.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    A: Orthogonal (X/Y) images of ATP7A and RAB11 in the undifferentiated and differentiated C-6 cells has been represented. Region highlighted by boxes in the differentiated cell has been enlarged and represented in panel B. B – Orthogonal (X/Y) images of the enlarged perinuclear (soma) and neurite of a single cell, demonstrated in the panel A (right) and , have been represented.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: A: Orthogonal (X/Y) images of ATP7A and RAB11 in the undifferentiated and differentiated C-6 cells has been represented. Region highlighted by boxes in the differentiated cell has been enlarged and represented in panel B. B – Orthogonal (X/Y) images of the enlarged perinuclear (soma) and neurite of a single cell, demonstrated in the panel A (right) and , have been represented.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    A (upper): ATP7A colocalizes with RAB11 in the perinuclear soma. A (lower): A Magnified area from the upper panel shows both ATP7A overlapping and juxtaposing with RAB11 demonstrating its presence in the RAB11 positive compartment. B (upper): ATP7A colocalizing with RAB11 positive compartments in the neurites. B (Lower): Magnified area from the upper panel shows colocalization and juxtaposition with RAB11.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: A (upper): ATP7A colocalizes with RAB11 in the perinuclear soma. A (lower): A Magnified area from the upper panel shows both ATP7A overlapping and juxtaposing with RAB11 demonstrating its presence in the RAB11 positive compartment. B (upper): ATP7A colocalizing with RAB11 positive compartments in the neurites. B (Lower): Magnified area from the upper panel shows colocalization and juxtaposition with RAB11.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the perinuclear region of the differentiated C-6 (glia). B – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region of the glia. C – An enlarged region showing exclusive and overlapping TGN38+Golgin97 and RAB11 positive compartments (left) and merged image (right) showing localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region. D – Graph showing ATP7A distribution in the overlapping and exclusive RAB11 and TGN38+Golgin97 compartments in the perinuclear region.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the perinuclear region of the differentiated C-6 (glia). B – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region of the glia. C – An enlarged region showing exclusive and overlapping TGN38+Golgin97 and RAB11 positive compartments (left) and merged image (right) showing localization of ATP7A in the TGN38+Golgin97 and RAB11 positive compartments in the perinuclear region. D – Graph showing ATP7A distribution in the overlapping and exclusive RAB11 and TGN38+Golgin97 compartments in the perinuclear region.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the neurites of the differentiated C-6 (glia). B (left) – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating colocalization of ATP7A (green) with RAB11 (red) and not TGN38+Golgin97 (cyan) in the neurite. The nuclei have been indicated in blue. B (right) – An enlarged region, in the neurite showing colocalization of ATP7A with RAB11 and lack of any colocalization of ATP7A with TGN38+Golgin97.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: A – Localization of ATP7A, TGN38+Golgin97 and RAB11 in the neurites of the differentiated C-6 (glia). B (left) – Merged (ATP7A, TGN38+Golgin97, RAB11) image demonstrating colocalization of ATP7A (green) with RAB11 (red) and not TGN38+Golgin97 (cyan) in the neurite. The nuclei have been indicated in blue. B (right) – An enlarged region, in the neurite showing colocalization of ATP7A with RAB11 and lack of any colocalization of ATP7A with TGN38+Golgin97.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    C-6 cells were differentiated as described, and then treated with 30uM TTM for 2 hours. Disappearance of the ATP7A containing vesicles along the neurites and retention of ATP7A in the TGN38 and Golgin97 positive Trans Golgi Network (TGN) is observed in response to the copper chelation.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: C-6 cells were differentiated as described, and then treated with 30uM TTM for 2 hours. Disappearance of the ATP7A containing vesicles along the neurites and retention of ATP7A in the TGN38 and Golgin97 positive Trans Golgi Network (TGN) is observed in response to the copper chelation.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    C-6 cells are plated and differentiated in the presence of 30uM Ammonium Tetrathiomolybdate (TTM). A – Bright field image of the C-6 cells differentiated in presence and absence of TTM. B – Relative mRNA level of GFAP in the glial cells differentiated in presence and absence of TTM (no of replicate – 3). C - ATP7A localization in the glial cells differentiated in presence and absence of TTM.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: C-6 cells are plated and differentiated in the presence of 30uM Ammonium Tetrathiomolybdate (TTM). A – Bright field image of the C-6 cells differentiated in presence and absence of TTM. B – Relative mRNA level of GFAP in the glial cells differentiated in presence and absence of TTM (no of replicate – 3). C - ATP7A localization in the glial cells differentiated in presence and absence of TTM.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques:

    Left: Differentiation of the PC-12 cells involve increased level of the CTR1 (blue cylinder) resulting into an increased intracellular copper (golden sphere). A bulk of the cytosolic copper is reportedly utilized by the Golgi based secretory pathway. Cytosolic copper binds to MEK1/2 (green circle with spikes) and triggers ERK1/2 phosphorylation (green ellipse) which is crucial for the viability of the neurons. ATP7A (orange cylinder) is retained in the TGN, despite high intracellular copper. Right: Differentiated C-6 (glia) have low intracellular copper and thereby downregulation of the copper dependent ERK1/2 phosphorylation. ATP7A localizes in the TGN38 and RAB11 positive compartments in the perinuclear region. In addition, ATP7A localizes into the RAB11 positive vesicles in the neurites (inset) despite low intracellular copper.

    Journal: bioRxiv

    Article Title: Copper dependent ERK1/2 phosphorylation is essential for the viability of neurons and not glia

    doi: 10.1101/2021.03.18.435926

    Figure Lengend Snippet: Left: Differentiation of the PC-12 cells involve increased level of the CTR1 (blue cylinder) resulting into an increased intracellular copper (golden sphere). A bulk of the cytosolic copper is reportedly utilized by the Golgi based secretory pathway. Cytosolic copper binds to MEK1/2 (green circle with spikes) and triggers ERK1/2 phosphorylation (green ellipse) which is crucial for the viability of the neurons. ATP7A (orange cylinder) is retained in the TGN, despite high intracellular copper. Right: Differentiated C-6 (glia) have low intracellular copper and thereby downregulation of the copper dependent ERK1/2 phosphorylation. ATP7A localizes in the TGN38 and RAB11 positive compartments in the perinuclear region. In addition, ATP7A localizes into the RAB11 positive vesicles in the neurites (inset) despite low intracellular copper.

    Article Snippet: Rabbit polyclonal Anti-ATP7A antibody (abcam, 1:300 dilution), mouse monoclonal TGN38 antibody (Novus Biologicals, 1:400 dilution), mouse monoclonal Golgin 97antibody (Thermo Fisher Scientific, 1:400 dilution), mouse monoclonal LAMP1 (Developmental Studies Hybridoma Bank, University of Iowa1:400 dilution,), mouse monoclonal Gama Tubulin (Invitrogen, 1:400 dilution), mouse monoclonal RAB 7 (Novus Biologicals, 1:50 dilution), goat polyclonal RAB11 (Santa Cruz Biotechnology Inc., 1:50 dilution), rabbit monoclonal anti-FLAG antibody (Cell signalling technology, 1:600), mouse monoclonal anti-GFAP (Sigma Aldrich) is used to detect the respective proteins.

    Techniques: