anti gga3 rabbit monoclonal  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gga3 rabbit monoclonal
    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , <t>GGA3</t> −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.
    Anti Gga3 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gga3 rabbit monoclonal/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gga3 rabbit monoclonal - by Bioz Stars, 2023-01
    93/100 stars

    Images

    1) Product Images from "Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting"

    Article Title: Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting

    Journal: FEBS Open Bio

    doi: 10.1002/2211-5463.13040

    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.
    Figure Legend Snippet: Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.

    Techniques Used: Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page, Autoradiography, Radioactivity

    anti gga3 rabbit monoclonal  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gga3 rabbit monoclonal
    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , <t>GGA3</t> −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.
    Anti Gga3 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gga3 rabbit monoclonal/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gga3 rabbit monoclonal - by Bioz Stars, 2023-01
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    Images

    1) Product Images from "Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting"

    Article Title: Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting

    Journal: FEBS Open Bio

    doi: 10.1002/2211-5463.13040

    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.
    Figure Legend Snippet: Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.

    Techniques Used: Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page, Autoradiography, Radioactivity

    anti gga3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gga3
    Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or <t>GGA3-siRNA</t> and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.
    Anti Gga3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gga3/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    anti gga3 - by Bioz Stars, 2023-01
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    Images

    1) Product Images from "An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease"

    Article Title: An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease

    Journal: EMBO Molecular Medicine

    doi: 10.15252/emmm.201404438

    Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.
    Figure Legend Snippet: Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.

    Techniques Used: Immunostaining, Transfection, MANN-WHITNEY

    dvl3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc dvl3
    TABLE 1
    Dvl3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dvl3/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    1) Product Images from "Sequential Activation and Inactivation of Dishevelled in the Wnt/?-Catenin Pathway by Casein Kinases "

    Article Title: Sequential Activation and Inactivation of Dishevelled in the Wnt/?-Catenin Pathway by Casein Kinases

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.169870

    TABLE 1
    Figure Legend Snippet: TABLE 1

    Techniques Used:

    dvl3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc dvl3
    TABLE 1
    Dvl3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dvl3/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    dvl3 - by Bioz Stars, 2023-01
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    1) Product Images from "Sequential Activation and Inactivation of Dishevelled in the Wnt/?-Catenin Pathway by Casein Kinases "

    Article Title: Sequential Activation and Inactivation of Dishevelled in the Wnt/?-Catenin Pathway by Casein Kinases

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.169870

    TABLE 1
    Figure Legend Snippet: TABLE 1

    Techniques Used:

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    Cell Signaling Technology Inc anti gga3 rabbit monoclonal
    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , <t>GGA3</t> −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.
    Anti Gga3 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gga3 rabbit monoclonal/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    Cell Signaling Technology Inc anti gga3
    Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or <t>GGA3-siRNA</t> and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.
    Anti Gga3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gga3/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc dvl3
    TABLE 1
    Dvl3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dvl3/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    Image Search Results


    Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.

    Journal: FEBS Open Bio

    Article Title: Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting

    doi: 10.1002/2211-5463.13040

    Figure Lengend Snippet: Sorting of cathepsin D in the absence of GGA proteins. (A) Parental WT, GGA1 −/− , GGA2 −/− , GGA3 −/− , and GGA123 −/− HeLa cell lines were metabolically labeled with [ 35 S]methionine/cysteine and processed as described under ‘ ’. Secreted and intracellular cathepsin D molecules were immunoprecipitated with a polyclonal anti‐cathepsin D antibody, resolved by 10% SDS/PAGE and visualized by autoradiography of the dried gel. A representative autoradiograph is shown. (B) The percentage of cathepsin D in the media (m) was calculated as the ratio of radioactivity in the secreted form divided by the sum of the processed (c) and secreted forms (m). The data shown are the mean ± SD for four independent experiments. (C) Parental WT, GGA123 −/− , and GNPTAB −/− HeLa cell lines were processed for cathepsin D sorting as described in (A). A representative autoradiograph is shown, and data presented are the mean of two independent experiments.

    Article Snippet: The following published/validated commercial antibodies against human GGA proteins were used to screen for the GGA knockout cell lines: anti‐GGA1 rabbit monoclonal (Abcam, Cat # ab170956, Cambridge, MA, USA), anti‐GGA2 mouse monoclonal (BD Biosciences, Cat # 612612), and anti‐GGA3 rabbit monoclonal (Cell Signaling, Cat # D66F1, Beverly, MA, USA).

    Techniques: Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page, Autoradiography, Radioactivity

    Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.

    Journal: EMBO Molecular Medicine

    Article Title: An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease

    doi: 10.15252/emmm.201404438

    Figure Lengend Snippet: Down-regulation of BACE1 protein in aged Mgat3 −/− mouse brain Immunostaining of 12-month-old brain sections (cerebral cortex) with anti-BACE1. Scale bar, 100 μm. Proteins from the membrane fractions of 12-month-old mouse brains ( n = 4–5) were immunoblotted for BACE1, and BACE1 intensity was quantified. * P = 0.044. Lysates from MEFs were immunoblotted for APP, BACE1, or GAPDH (loading control), and BACE1 intensity was quantified ( n = 4). Amount of Aβ40 in the culture medium of immortalized MEFs ( n = 3). * P = 0.045. MEFs were transfected with control siRNA or GGA3-siRNA and then immunoblotted for BACE1, GGA3, or GAPDH (loading control) ( n = 6). Data Information: All graphs show means ± SEM (* P < 0.05; Student's t -test for (B) and the Mann–Whitney U -test for (D)). Source data are available online for this figure.

    Article Snippet: The commercially available antibodies used were as follows: rabbit anti-BACE1 (5606), anti-nicastrin (9447S), anti-GGA3 (8027), anti-rab5 (3547), anti-rab7 (9367), and anti-rab9 (5118) from Cell Signaling Technology; anti-APP C-term (recognizes C-terminal part of APP, 18961), anti-APP N-term (10D1), and anti-sAPPβ-sw (10321, clone 6A1) from Immuno-Biological Laboratories; anti-Aβ (SIG-39220, clone 4G8) and anti-sAPPα (SIG-39320, clone 6E10) from SIGNET; anti-Lamp1 (ab25630) and anti-PSD95 (ab2723) from Abcam; anti-actin (A4700) from Sigma; anti-syntaxin 6 (610635) from BD Biosciences; anti-GAPDH (MAB374), anti-APP (22C11), and anti-MBP (MAB386) from Millipore; anti-MAP2 (sc-20172) from Santa Cruz Biotechnology; anti-GFAP (13-0300) from Life Technologies; anti-CHL1 (AF2147) and anti-contactin-2 (AF4439) from R&D systems; and anti-Iba1 (019-197419) from Wako.

    Techniques: Immunostaining, Transfection, MANN-WHITNEY

    TABLE 1

    Journal: The Journal of Biological Chemistry

    Article Title: Sequential Activation and Inactivation of Dishevelled in the Wnt/?-Catenin Pathway by Casein Kinases

    doi: 10.1074/jbc.M110.169870

    Figure Lengend Snippet: TABLE 1

    Article Snippet: The antibodies used include phospho-LRP6 (Ser-1490, #2568), Dvl3 (#3218), Dvl2 (#3224), Axin1 (#2087) from Cell Signaling Technologies, actin (C-11, sc-1615), Dvl3 (sc-8027), Dvl2 (sc-8026), CK1ϵ (sc-6471), and Myc (sc-40) from Santa Cruz Biotechnology, CK2α (#611610) from BD Transduction Laboratories, and FLAG M2 (F1804) from Sigma.

    Techniques: