anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface <t>mGluR1</t> before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Anti Mglur1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mglur1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mglur1 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways"

    Article Title: Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0006011

    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Figure Legend Snippet: Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.

    Techniques Used:

    anti girk2  (Alomone Labs)


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    Structured Review

    Alomone Labs anti girk2
    (a) Currents of the paddle chimera (PC) and designs are plotted against varying test voltages. Each curve represents recordings from n ⩾8 oocytes. Error bars represent standard deviations. (b) Average currents (paddle chimera: 0.91±0.19 μA, D1: 4.65±1.52 μA, D2: 12.50±1.63 μA). (c) Western blot results reporting total membrane expression. The blots were labeled with anti-FLAG (top) or with <t>anti-GIRK2</t> (as control; bottom) antibodies. (d) Normalized blot intensities. The experiment was performed in triplicate. Error bars represent the standard deviation. (e) Normalized tail currents were recorded at -50mV as a function of the test pulse voltage (see inset). Measured tail current amplitudes were fitted with a single-component Boltzmann equation (solid lines), from which V 1/2 of activation was inferred. (f) Inferred V 1/2 values (paddle chimera: 16.10±5.39 mV, D1: -8.33±3.49 mV, and, D2: -16.61±2.75 mV).
    Anti Girk2, supplied by Alomone Labs, 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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    Images

    1) Product Images from "One-shot design elevates functional expression levels of a voltage-gated potassium channel"

    Article Title: One-shot design elevates functional expression levels of a voltage-gated potassium channel

    Journal: bioRxiv

    doi: 10.1101/2022.12.28.522065

    (a) Currents of the paddle chimera (PC) and designs are plotted against varying test voltages. Each curve represents recordings from n ⩾8 oocytes. Error bars represent standard deviations. (b) Average currents (paddle chimera: 0.91±0.19 μA, D1: 4.65±1.52 μA, D2: 12.50±1.63 μA). (c) Western blot results reporting total membrane expression. The blots were labeled with anti-FLAG (top) or with anti-GIRK2 (as control; bottom) antibodies. (d) Normalized blot intensities. The experiment was performed in triplicate. Error bars represent the standard deviation. (e) Normalized tail currents were recorded at -50mV as a function of the test pulse voltage (see inset). Measured tail current amplitudes were fitted with a single-component Boltzmann equation (solid lines), from which V 1/2 of activation was inferred. (f) Inferred V 1/2 values (paddle chimera: 16.10±5.39 mV, D1: -8.33±3.49 mV, and, D2: -16.61±2.75 mV).
    Figure Legend Snippet: (a) Currents of the paddle chimera (PC) and designs are plotted against varying test voltages. Each curve represents recordings from n ⩾8 oocytes. Error bars represent standard deviations. (b) Average currents (paddle chimera: 0.91±0.19 μA, D1: 4.65±1.52 μA, D2: 12.50±1.63 μA). (c) Western blot results reporting total membrane expression. The blots were labeled with anti-FLAG (top) or with anti-GIRK2 (as control; bottom) antibodies. (d) Normalized blot intensities. The experiment was performed in triplicate. Error bars represent the standard deviation. (e) Normalized tail currents were recorded at -50mV as a function of the test pulse voltage (see inset). Measured tail current amplitudes were fitted with a single-component Boltzmann equation (solid lines), from which V 1/2 of activation was inferred. (f) Inferred V 1/2 values (paddle chimera: 16.10±5.39 mV, D1: -8.33±3.49 mV, and, D2: -16.61±2.75 mV).

    Techniques Used: Western Blot, Expressing, Labeling, Standard Deviation, Activation Assay

    anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface <t>mGluR1</t> before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Anti Mglur1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mglur1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mglur1 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways"

    Article Title: Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0006011

    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Figure Legend Snippet: Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.

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    rabbit polyclonal  (Alomone Labs)


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    Alomone Labs rabbit polyclonal
    Rabbit Polyclonal, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 1 article reviews
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    rabbit polyclonal - by Bioz Stars, 2023-01
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    anti cftr  (Alomone Labs)


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    Alomone Labs anti cftr
    <t>CFTR,</t> NF KappaB and <t>MUC1</t> <t>immunohistochemical</t> staining in the endometrium. Representative images of positive control CFTR, NF KappaB and MUC1 immunostaining ( A - C ) and negative control CFTR, NF KappaB and MUC1 immunostaining ( D - F ), respectively. CFTR, NF KappaB and MUC1 immunostaining in the endometrium of control infertile patients without a hydrosalpinx ( G – L ) and infertile patients with a hydrosalpinx ( M – R ). Endometrial tissues in the proliferative ( D – I , M – O ) and secretory ( J – L , P – R ) phases are shown for both groups; ×400 magnification.
    Anti Cftr, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti cftr/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti cftr - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "NF kappaB expression increases and CFTR and MUC1 expression decreases in the endometrium of infertile patients with hydrosalpinx: a comparative study"

    Article Title: NF kappaB expression increases and CFTR and MUC1 expression decreases in the endometrium of infertile patients with hydrosalpinx: a comparative study

    Journal: Reproductive Biology and Endocrinology : RB&E

    doi: 10.1186/1477-7827-10-86

    CFTR, NF KappaB and MUC1 immunohistochemical staining in the endometrium. Representative images of positive control CFTR, NF KappaB and MUC1 immunostaining ( A - C ) and negative control CFTR, NF KappaB and MUC1 immunostaining ( D - F ), respectively. CFTR, NF KappaB and MUC1 immunostaining in the endometrium of control infertile patients without a hydrosalpinx ( G – L ) and infertile patients with a hydrosalpinx ( M – R ). Endometrial tissues in the proliferative ( D – I , M – O ) and secretory ( J – L , P – R ) phases are shown for both groups; ×400 magnification.
    Figure Legend Snippet: CFTR, NF KappaB and MUC1 immunohistochemical staining in the endometrium. Representative images of positive control CFTR, NF KappaB and MUC1 immunostaining ( A - C ) and negative control CFTR, NF KappaB and MUC1 immunostaining ( D - F ), respectively. CFTR, NF KappaB and MUC1 immunostaining in the endometrium of control infertile patients without a hydrosalpinx ( G – L ) and infertile patients with a hydrosalpinx ( M – R ). Endometrial tissues in the proliferative ( D – I , M – O ) and secretory ( J – L , P – R ) phases are shown for both groups; ×400 magnification.

    Techniques Used: Immunohistochemical staining, Staining, Positive Control, Immunostaining, Negative Control

    Real-time PCR analysis of CFTR, MUC1 and NF kappa B mRNA in the endometrium with or without hydrosalpinx. MUC1 mRNA and CFTR mRNA were expressed at significantly lower levels in the hydrosalpinx group than the control group, while NF KappaB mRNA was expressed at significantly higher levels in the hydrosalpinx group than the control group.
    Figure Legend Snippet: Real-time PCR analysis of CFTR, MUC1 and NF kappa B mRNA in the endometrium with or without hydrosalpinx. MUC1 mRNA and CFTR mRNA were expressed at significantly lower levels in the hydrosalpinx group than the control group, while NF KappaB mRNA was expressed at significantly higher levels in the hydrosalpinx group than the control group.

    Techniques Used: Real-time Polymerase Chain Reaction

    rabbit polyclonal anti cftr  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti cftr
    Rabbit Polyclonal Anti Cftr, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit anti girk2  (Alomone Labs)


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    Alomone Labs rabbit anti girk2
    Cells labeled with Shh-GIFM at different time points have a changing potential to contribute to subpopulations of DA neurons . (A-H) Immunofluorescent staining for β-gal-positive fate-mapped cells (Shh-GIFM at E8.5 or E11.5) and DA neurons (TH) on coronal sections of the ventral midbrain (P21 to P30). The areas shown in (A-D) are indicated in (E-H). Arrows indicate double-labeled cells; arrowheads indicate β-gal-positive cells with astrocytic morphology. (E'-H') Representative schematics of the immunostained sections showing the distribution of TH-positive fate-mapped cells (red dots) and of fate-mapped cells with astrocytic morphology (yellow crosses). Rostral, Bregma -2.92; caudal, Bregma -3.40 . If, interfascicular nucleus; Pn, paranigral nucleus; Snc, substantia nigra pars compacta; Snl, substantia nigra lateralis; Vta, VTA. Fate-mapped cells outside these areas are not represented. Cells with astrocytic morphology are not present with TM8.5. Scale bars: (A-D) 40 μm; (E-H) 200 μm. (I) Relative contribution of cells marked with Shh-GIFM between E8.5 and E11.5 to the SN (Snl + Snc), dorsal-lateral VTA (Vta) and ventral-medial VTA (Pn + If); see schematic in (L). For each animal (n ≥ 3), TH-positive fate-mapped cells were counted in the three indicated areas and normalized for the combined number of overlapping cells counted in these areas (in percent). Error bars indicate standard deviation. Significance (* P < 0.05; ** P < 0.01; *** P < 0.001) was determined by ANOVA and LSD post-hoc analysis. (J) Distribution of Calbindin- and <t>Girk2-positive</t> cells. (K) Relative contribution of fate-mapped cells to Calbindin (VTA) versus Girk2 (SN) positive cells. Calbindin- or Girk2-positive fate-mapped cells were counted in three different rostral-caudal midbrain areas (n ≥ 3). The ratio of Calbindin-positive fate-mapped cells to Girk2-positive fate-mapped cells was determined. Significance (*** P < 0.001) was determined by Student's t -test. (L) Schematic showing the SN, dlVTA and vmVTA. (M) Fate mapping strategy.
    Rabbit Anti Girk2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti girk2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti girk2 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Temporal-spatial changes in Sonic Hedgehog expression and signaling reveal different potentials of ventral mesencephalic progenitors to populate distinct ventral midbrain nuclei"

    Article Title: Temporal-spatial changes in Sonic Hedgehog expression and signaling reveal different potentials of ventral mesencephalic progenitors to populate distinct ventral midbrain nuclei

    Journal: Neural Development

    doi: 10.1186/1749-8104-6-29

    Cells labeled with Shh-GIFM at different time points have a changing potential to contribute to subpopulations of DA neurons . (A-H) Immunofluorescent staining for β-gal-positive fate-mapped cells (Shh-GIFM at E8.5 or E11.5) and DA neurons (TH) on coronal sections of the ventral midbrain (P21 to P30). The areas shown in (A-D) are indicated in (E-H). Arrows indicate double-labeled cells; arrowheads indicate β-gal-positive cells with astrocytic morphology. (E'-H') Representative schematics of the immunostained sections showing the distribution of TH-positive fate-mapped cells (red dots) and of fate-mapped cells with astrocytic morphology (yellow crosses). Rostral, Bregma -2.92; caudal, Bregma -3.40 . If, interfascicular nucleus; Pn, paranigral nucleus; Snc, substantia nigra pars compacta; Snl, substantia nigra lateralis; Vta, VTA. Fate-mapped cells outside these areas are not represented. Cells with astrocytic morphology are not present with TM8.5. Scale bars: (A-D) 40 μm; (E-H) 200 μm. (I) Relative contribution of cells marked with Shh-GIFM between E8.5 and E11.5 to the SN (Snl + Snc), dorsal-lateral VTA (Vta) and ventral-medial VTA (Pn + If); see schematic in (L). For each animal (n ≥ 3), TH-positive fate-mapped cells were counted in the three indicated areas and normalized for the combined number of overlapping cells counted in these areas (in percent). Error bars indicate standard deviation. Significance (* P < 0.05; ** P < 0.01; *** P < 0.001) was determined by ANOVA and LSD post-hoc analysis. (J) Distribution of Calbindin- and Girk2-positive cells. (K) Relative contribution of fate-mapped cells to Calbindin (VTA) versus Girk2 (SN) positive cells. Calbindin- or Girk2-positive fate-mapped cells were counted in three different rostral-caudal midbrain areas (n ≥ 3). The ratio of Calbindin-positive fate-mapped cells to Girk2-positive fate-mapped cells was determined. Significance (*** P < 0.001) was determined by Student's t -test. (L) Schematic showing the SN, dlVTA and vmVTA. (M) Fate mapping strategy.
    Figure Legend Snippet: Cells labeled with Shh-GIFM at different time points have a changing potential to contribute to subpopulations of DA neurons . (A-H) Immunofluorescent staining for β-gal-positive fate-mapped cells (Shh-GIFM at E8.5 or E11.5) and DA neurons (TH) on coronal sections of the ventral midbrain (P21 to P30). The areas shown in (A-D) are indicated in (E-H). Arrows indicate double-labeled cells; arrowheads indicate β-gal-positive cells with astrocytic morphology. (E'-H') Representative schematics of the immunostained sections showing the distribution of TH-positive fate-mapped cells (red dots) and of fate-mapped cells with astrocytic morphology (yellow crosses). Rostral, Bregma -2.92; caudal, Bregma -3.40 . If, interfascicular nucleus; Pn, paranigral nucleus; Snc, substantia nigra pars compacta; Snl, substantia nigra lateralis; Vta, VTA. Fate-mapped cells outside these areas are not represented. Cells with astrocytic morphology are not present with TM8.5. Scale bars: (A-D) 40 μm; (E-H) 200 μm. (I) Relative contribution of cells marked with Shh-GIFM between E8.5 and E11.5 to the SN (Snl + Snc), dorsal-lateral VTA (Vta) and ventral-medial VTA (Pn + If); see schematic in (L). For each animal (n ≥ 3), TH-positive fate-mapped cells were counted in the three indicated areas and normalized for the combined number of overlapping cells counted in these areas (in percent). Error bars indicate standard deviation. Significance (* P < 0.05; ** P < 0.01; *** P < 0.001) was determined by ANOVA and LSD post-hoc analysis. (J) Distribution of Calbindin- and Girk2-positive cells. (K) Relative contribution of fate-mapped cells to Calbindin (VTA) versus Girk2 (SN) positive cells. Calbindin- or Girk2-positive fate-mapped cells were counted in three different rostral-caudal midbrain areas (n ≥ 3). The ratio of Calbindin-positive fate-mapped cells to Girk2-positive fate-mapped cells was determined. Significance (*** P < 0.001) was determined by Student's t -test. (L) Schematic showing the SN, dlVTA and vmVTA. (M) Fate mapping strategy.

    Techniques Used: Labeling, Staining, Standard Deviation

    rabbit anti pro bdnf ab  (Alomone Labs)


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    Structured Review

    Alomone Labs rabbit anti pro bdnf ab
    (A): RT-PCR of <t>BDNF,</t> its <t>high</t> <t>(TrkB)</t> and low (p75 NTR ) affinity receptors, TrkA, and TrkC from cells cultured in basal (10% FCS medium), WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). GAPDH mRNA levels was used as an internal control. Positive control (lane 5) was the neuroblastoma cell line (IMR32) for BDNF, TrkB and p75 NTR ; and the erythromyeloblastoid leukemia cells (K562) for TrkA and C. A representative result of at least three to five independent experiments. (B) Comparison of TrkB95 and p75 NTR on total RNA extracted from WiDr cells cultured in 10% FCS or after 24 to 72 h serum deprivation (0% FCS). TrkB95 and p75 NTR mRNA/GAPDH mRNA quantification of band intensities evaluated by densitometry are shown above lanes and expressed in arbitrary units (mean of three independent experiments). (C) Same experiment: RT-PCR of TrkA and TrkC on total RNA extracted from WiDr cells cultured under basal culture conditions (10% FCS) and after 24–72 h of serum starvation in comparison to positive control (K562) (D) Expression of pro-BDNF and BDNF, full length TrkB 145 and truncated TrkB 95 and p75 NTR proteins in CRC cell lines cultured in 10% FCS. TrkA and TrkC were not detected. Actin was used as loading protein control. WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). Positive control (lane: 5) were IMR32 cells for BDNF, pro-BDNF, TrkB and p75 NTR and K562 cells or TrkA and TrkC. A representative result of at least three independent experiments.
    Rabbit Anti Pro Bdnf Ab, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti pro bdnf ab/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti pro bdnf ab - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Fine-Tuning Roles of Endogenous Brain-Derived Neurotrophic Factor, TrkB and Sortilin in Colorectal Cancer Cell Survival"

    Article Title: Fine-Tuning Roles of Endogenous Brain-Derived Neurotrophic Factor, TrkB and Sortilin in Colorectal Cancer Cell Survival

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0025097

    (A): RT-PCR of BDNF, its high (TrkB) and low (p75 NTR ) affinity receptors, TrkA, and TrkC from cells cultured in basal (10% FCS medium), WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). GAPDH mRNA levels was used as an internal control. Positive control (lane 5) was the neuroblastoma cell line (IMR32) for BDNF, TrkB and p75 NTR ; and the erythromyeloblastoid leukemia cells (K562) for TrkA and C. A representative result of at least three to five independent experiments. (B) Comparison of TrkB95 and p75 NTR on total RNA extracted from WiDr cells cultured in 10% FCS or after 24 to 72 h serum deprivation (0% FCS). TrkB95 and p75 NTR mRNA/GAPDH mRNA quantification of band intensities evaluated by densitometry are shown above lanes and expressed in arbitrary units (mean of three independent experiments). (C) Same experiment: RT-PCR of TrkA and TrkC on total RNA extracted from WiDr cells cultured under basal culture conditions (10% FCS) and after 24–72 h of serum starvation in comparison to positive control (K562) (D) Expression of pro-BDNF and BDNF, full length TrkB 145 and truncated TrkB 95 and p75 NTR proteins in CRC cell lines cultured in 10% FCS. TrkA and TrkC were not detected. Actin was used as loading protein control. WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). Positive control (lane: 5) were IMR32 cells for BDNF, pro-BDNF, TrkB and p75 NTR and K562 cells or TrkA and TrkC. A representative result of at least three independent experiments.
    Figure Legend Snippet: (A): RT-PCR of BDNF, its high (TrkB) and low (p75 NTR ) affinity receptors, TrkA, and TrkC from cells cultured in basal (10% FCS medium), WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). GAPDH mRNA levels was used as an internal control. Positive control (lane 5) was the neuroblastoma cell line (IMR32) for BDNF, TrkB and p75 NTR ; and the erythromyeloblastoid leukemia cells (K562) for TrkA and C. A representative result of at least three to five independent experiments. (B) Comparison of TrkB95 and p75 NTR on total RNA extracted from WiDr cells cultured in 10% FCS or after 24 to 72 h serum deprivation (0% FCS). TrkB95 and p75 NTR mRNA/GAPDH mRNA quantification of band intensities evaluated by densitometry are shown above lanes and expressed in arbitrary units (mean of three independent experiments). (C) Same experiment: RT-PCR of TrkA and TrkC on total RNA extracted from WiDr cells cultured under basal culture conditions (10% FCS) and after 24–72 h of serum starvation in comparison to positive control (K562) (D) Expression of pro-BDNF and BDNF, full length TrkB 145 and truncated TrkB 95 and p75 NTR proteins in CRC cell lines cultured in 10% FCS. TrkA and TrkC were not detected. Actin was used as loading protein control. WiDr (lane: 1), SW480 (lane: 2), SW620 (lane: 3), COLO 205 (lane: 4). Positive control (lane: 5) were IMR32 cells for BDNF, pro-BDNF, TrkB and p75 NTR and K562 cells or TrkA and TrkC. A representative result of at least three independent experiments.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Cell Culture, Positive Control, Expressing

    BDNF release and effect of exogenous BDNF,  pro-BDNF,   TrkB  inhibitor (K252a) and neutralizing anti-BDNF on apoptosis and proliferation in primary CRC cell lines.
    Figure Legend Snippet: BDNF release and effect of exogenous BDNF, pro-BDNF, TrkB inhibitor (K252a) and neutralizing anti-BDNF on apoptosis and proliferation in primary CRC cell lines.

    Techniques Used:

    BDNF release and effect of exogenous BDNF,  pro-BDNF,   TrkB  inhibitor (K252a) and neutralizing anti-BDNF on apoptosis and proliferation in metastatic CRC cell lines.
    Figure Legend Snippet: BDNF release and effect of exogenous BDNF, pro-BDNF, TrkB inhibitor (K252a) and neutralizing anti-BDNF on apoptosis and proliferation in metastatic CRC cell lines.

    Techniques Used:

    Confocal microscopy of WiDr (A, B) and COLO 205 (C, D) cells, stained with an anti-BDNF Ab (red), anti-TrkB mAb (green) or both (overlay) cultured with 10% FCS (A, C) or after 24-h serum deprivation (B, D). Under basal culture conditions (10% FCS), TrkB and BDNF were sequestered in the cytoplasm (arrows) in WiDr (A) and COLO 205 (C) cells. The same staining patterns were obtained with the two other cell lines (data not shown). After serum starvation relocation to the cell membrane and colocalization of TrkB and BDNF (yellow in merged, arrows) were detected in WiDr (B) and COLO 205 (D). Images were representative for at least three to five independent experiments.
    Figure Legend Snippet: Confocal microscopy of WiDr (A, B) and COLO 205 (C, D) cells, stained with an anti-BDNF Ab (red), anti-TrkB mAb (green) or both (overlay) cultured with 10% FCS (A, C) or after 24-h serum deprivation (B, D). Under basal culture conditions (10% FCS), TrkB and BDNF were sequestered in the cytoplasm (arrows) in WiDr (A) and COLO 205 (C) cells. The same staining patterns were obtained with the two other cell lines (data not shown). After serum starvation relocation to the cell membrane and colocalization of TrkB and BDNF (yellow in merged, arrows) were detected in WiDr (B) and COLO 205 (D). Images were representative for at least three to five independent experiments.

    Techniques Used: Confocal Microscopy, Staining, Cell Culture

    (A) Role of endogenous BDNF and its receptor TrkB on CRC cell proliferation: effects of exogenous BDNF and suppressing endogenous TrkB receptor on cell proliferation. The four cell lines were cultured for 24 h in FCS-free medium (FCS 10%, −) in the presence of exogenous BDNF (+), K252a (+) alone or in combination. Cell proliferation was determined by flow cytometry analysis using EdU Alexa Fluor 488. The data are presented as histograms of proliferating cells in relative units ± SEM of five independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free medium. (B, C) Effects of exogenous BDNF and suppressing endogenous TrkB receptor on cell survival. Apoptotic ratios of soluble nucleosomes were detected by ELISA Cell for WiDr, SW480, SW620, and COLO 205 induced by serum deprivation alone (FCS 10%, −) or in association either with exogenous BDNF (+), or with K252a (+), during 24–72 h of serum deprivation. Histograms, mean ratio of apoptotic cells ± SEM of at least three independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free condition alone. (D, E) apoptotic ratio after 24 h serum deprivation alone (0% FCS) or with combination with a neutralizing anti-BDNF mAb (0% anti-BDNF). Histograms, mean ratio of apoptotic cells ± SEM of three independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free condition alone.
    Figure Legend Snippet: (A) Role of endogenous BDNF and its receptor TrkB on CRC cell proliferation: effects of exogenous BDNF and suppressing endogenous TrkB receptor on cell proliferation. The four cell lines were cultured for 24 h in FCS-free medium (FCS 10%, −) in the presence of exogenous BDNF (+), K252a (+) alone or in combination. Cell proliferation was determined by flow cytometry analysis using EdU Alexa Fluor 488. The data are presented as histograms of proliferating cells in relative units ± SEM of five independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free medium. (B, C) Effects of exogenous BDNF and suppressing endogenous TrkB receptor on cell survival. Apoptotic ratios of soluble nucleosomes were detected by ELISA Cell for WiDr, SW480, SW620, and COLO 205 induced by serum deprivation alone (FCS 10%, −) or in association either with exogenous BDNF (+), or with K252a (+), during 24–72 h of serum deprivation. Histograms, mean ratio of apoptotic cells ± SEM of at least three independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free condition alone. (D, E) apoptotic ratio after 24 h serum deprivation alone (0% FCS) or with combination with a neutralizing anti-BDNF mAb (0% anti-BDNF). Histograms, mean ratio of apoptotic cells ± SEM of three independent experiments. *, p <0.05; **, p <0.01; ***, p <0.001, when compared with serum-free condition alone.

    Techniques Used: Cell Culture, Flow Cytometry, Enzyme-linked Immunosorbent Assay

    rabbit anti reag2  (Alomone Labs)


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    Structured Review

    Alomone Labs rabbit anti reag2
    Subcellular localization of native rEag1 and <t>rEag2</t> channels in young and mature hippocampal neurons in culture. Dissociated hippocampal neurons at DIV3, DIV7, and DIV12 were immunostained with the anti-rEag1 (A, B) or the anti-rEag2 (C, D) antibodies ( shown in green; left panels ), followed by counterstaining with the antibody for the dendritic marker MAP2 or the axonal marker tau ( shown in red; middle panels ). Merged images are shown in the right panels. (A) rEag1 immunoreactivities were localized in cell bodies, as well as in MAP2-positive and MAP2-negative ( arrows ) processes. (B) rEag1 immunoreactivities were present in the axonal compartment that was clearly defined by the immunofluorescence signal of tau ( arrows ). For DIV12 neurons in both (A) and (B), note the presence of punctate rEag1 staining patterns throughout proximal and distal neurites. (C, D) rEag2 immunoreactivities were present in both MAP2-positive and tau-positive processes. No significant rEag2 puncta were observed. Scale bar, 25 μm.
    Rabbit Anti Reag2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti reag2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti reag2 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "The punctate localization of rat Eag1 K + channels is conferred by the proximal post-CNBHD region"

    Article Title: The punctate localization of rat Eag1 K + channels is conferred by the proximal post-CNBHD region

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-15-23

    Subcellular localization of native rEag1 and rEag2 channels in young and mature hippocampal neurons in culture. Dissociated hippocampal neurons at DIV3, DIV7, and DIV12 were immunostained with the anti-rEag1 (A, B) or the anti-rEag2 (C, D) antibodies ( shown in green; left panels ), followed by counterstaining with the antibody for the dendritic marker MAP2 or the axonal marker tau ( shown in red; middle panels ). Merged images are shown in the right panels. (A) rEag1 immunoreactivities were localized in cell bodies, as well as in MAP2-positive and MAP2-negative ( arrows ) processes. (B) rEag1 immunoreactivities were present in the axonal compartment that was clearly defined by the immunofluorescence signal of tau ( arrows ). For DIV12 neurons in both (A) and (B), note the presence of punctate rEag1 staining patterns throughout proximal and distal neurites. (C, D) rEag2 immunoreactivities were present in both MAP2-positive and tau-positive processes. No significant rEag2 puncta were observed. Scale bar, 25 μm.
    Figure Legend Snippet: Subcellular localization of native rEag1 and rEag2 channels in young and mature hippocampal neurons in culture. Dissociated hippocampal neurons at DIV3, DIV7, and DIV12 were immunostained with the anti-rEag1 (A, B) or the anti-rEag2 (C, D) antibodies ( shown in green; left panels ), followed by counterstaining with the antibody for the dendritic marker MAP2 or the axonal marker tau ( shown in red; middle panels ). Merged images are shown in the right panels. (A) rEag1 immunoreactivities were localized in cell bodies, as well as in MAP2-positive and MAP2-negative ( arrows ) processes. (B) rEag1 immunoreactivities were present in the axonal compartment that was clearly defined by the immunofluorescence signal of tau ( arrows ). For DIV12 neurons in both (A) and (B), note the presence of punctate rEag1 staining patterns throughout proximal and distal neurites. (C, D) rEag2 immunoreactivities were present in both MAP2-positive and tau-positive processes. No significant rEag2 puncta were observed. Scale bar, 25 μm.

    Techniques Used: Marker, Immunofluorescence, Staining

    Synaptic localization of rEag1 channels. (A) Hippocampal neurons were double-stained for rEag1/rEag2 ( left panels ) and the postsynaptic density marker PSD-95 ( middle panels ). Scale bar, 25 μm. (B) Quantification of the number of puncta per 100-μm neurite (puncta/100 μm) for PSD-95, rEag1, and rEag2. The number in parenthesis denotes the amount of neurites analyzed, and the asterisk indicates a significant difference ( t -test, p < 0.05) from PSD-95. Data were collected from 7-11 different neurons. (C) Quantification of the co-localization of PSD-95 with rEag1 or rEag2. The data illustrate the fraction of PSD-95 puncta that were co-localized with rEag1/2 puncta, as well as the fraction of rEag1/2 puncta that were co-localized with PSD-95 puncta. The number in parenthesis denotes the amount of neurites analyzed, and the asterisk indicates a significant difference ( t -test, p < 0.05) from rEag1. Data were collected from 7-8 different neurons. (D) Subcellular fractionation of rat brains: the homogenate (H), the soluble fraction (S1), the crude membrane fraction (P2), the synaptosomal fraction (SPM), and the two postsynaptic density (PSD) preparations (PSD I: one Triton X-100 wash; PSD II: two Triton X-100 washes). The left panel ( 25 μg ) illustrates the primary fractionation profile, whereas the right panel ( 5 μg ) exemplifies the further enrichment pattern in the three sub-fractions of synaptosomes. All fractions were subject to immunoblotting analyses with the indicated antibodies. 25 μg and 5 μg refer to the amount of total protein loaded in each lane.
    Figure Legend Snippet: Synaptic localization of rEag1 channels. (A) Hippocampal neurons were double-stained for rEag1/rEag2 ( left panels ) and the postsynaptic density marker PSD-95 ( middle panels ). Scale bar, 25 μm. (B) Quantification of the number of puncta per 100-μm neurite (puncta/100 μm) for PSD-95, rEag1, and rEag2. The number in parenthesis denotes the amount of neurites analyzed, and the asterisk indicates a significant difference ( t -test, p < 0.05) from PSD-95. Data were collected from 7-11 different neurons. (C) Quantification of the co-localization of PSD-95 with rEag1 or rEag2. The data illustrate the fraction of PSD-95 puncta that were co-localized with rEag1/2 puncta, as well as the fraction of rEag1/2 puncta that were co-localized with PSD-95 puncta. The number in parenthesis denotes the amount of neurites analyzed, and the asterisk indicates a significant difference ( t -test, p < 0.05) from rEag1. Data were collected from 7-8 different neurons. (D) Subcellular fractionation of rat brains: the homogenate (H), the soluble fraction (S1), the crude membrane fraction (P2), the synaptosomal fraction (SPM), and the two postsynaptic density (PSD) preparations (PSD I: one Triton X-100 wash; PSD II: two Triton X-100 washes). The left panel ( 25 μg ) illustrates the primary fractionation profile, whereas the right panel ( 5 μg ) exemplifies the further enrichment pattern in the three sub-fractions of synaptosomes. All fractions were subject to immunoblotting analyses with the indicated antibodies. 25 μg and 5 μg refer to the amount of total protein loaded in each lane.

    Techniques Used: Staining, Marker, Fractionation, Western Blot

    Expression of GFP-rEag1 and GFP-rEag2 channels in HEK293T cells and hippocampal neurons. (A) Immunofluorescence staining and functional expression of GFP-rEag1 and GFP-rEag2 K + channels in HEK293T cells. GFP fluorescence ( shown in green ) and rEag1/rEag2 immunofluorescence ( shown in red ) signals demonstrated lucid co-localization at the membrane region. Scale bar, 10 μm. Whole-cell patch clamp parameters: the holding potential for rEag1 and rEag2 was -90 and -110 mV, respectively; the pulse protocol comprised 300-ms depolarizing test pulses ranging from -70 to +50 mV (rEag1) or from -90 to +30 mV (rEag2), with 10-mV increments. (B) Over-expression of GFP-rEag1/rEag2 in DIV12 hippocampal neurons. GFP signal is shown in green, and MAP2 immunofluorescence signal in red. Note the presence of prominent GFP puncta for rEag1, but not rEag2. Scale bar, 25 μm. (C) ( Top ) Schematic representation of the structural topology of Eag K + channel. ( Bottom ) Protein sequence alignment between rEag1 and rEag2 over the post-CNBHD region. Yellow shade: identical residues. Green shade: homologous residues. Sequence alignment analysis was implemented with the Vector NTI software (InforMax).
    Figure Legend Snippet: Expression of GFP-rEag1 and GFP-rEag2 channels in HEK293T cells and hippocampal neurons. (A) Immunofluorescence staining and functional expression of GFP-rEag1 and GFP-rEag2 K + channels in HEK293T cells. GFP fluorescence ( shown in green ) and rEag1/rEag2 immunofluorescence ( shown in red ) signals demonstrated lucid co-localization at the membrane region. Scale bar, 10 μm. Whole-cell patch clamp parameters: the holding potential for rEag1 and rEag2 was -90 and -110 mV, respectively; the pulse protocol comprised 300-ms depolarizing test pulses ranging from -70 to +50 mV (rEag1) or from -90 to +30 mV (rEag2), with 10-mV increments. (B) Over-expression of GFP-rEag1/rEag2 in DIV12 hippocampal neurons. GFP signal is shown in green, and MAP2 immunofluorescence signal in red. Note the presence of prominent GFP puncta for rEag1, but not rEag2. Scale bar, 25 μm. (C) ( Top ) Schematic representation of the structural topology of Eag K + channel. ( Bottom ) Protein sequence alignment between rEag1 and rEag2 over the post-CNBHD region. Yellow shade: identical residues. Green shade: homologous residues. Sequence alignment analysis was implemented with the Vector NTI software (InforMax).

    Techniques Used: Expressing, Immunofluorescence, Staining, Functional Assay, Fluorescence, Patch Clamp, Over Expression, Sequencing, Plasmid Preparation, Software

    Characterization of rEag1-I and rEag2-I chimeric channels. (A) Schematic representation of the construction of rEag1-I and rEag2-I chimeras. For all schematic cartoons hereafter, rEag1 and rEag2 sequences are shown in red and black, respectively. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated Eag constructs. Two-electrode voltage clamp parameters: the holding potential for rEag1 and rEag2 was -90 and -110 mV, respectively; the pulse protocol comprised 300-ms depolarizing test pulses ranging from -70 to +60 mV (rEag1) or from -100 to +40 mV (rEag2), with 10-mV increments. (C) Membrane localization of GFP-rEag1-I/rEag2-I channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of GFP-rEag1-I/rEag2-I channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for GFP-rEag1, GFP-rEag1-I, GFP-rEag2-I, and GFP-rEag2. The number in parenthesis denotes the amount of neurons analyzed. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)
    Figure Legend Snippet: Characterization of rEag1-I and rEag2-I chimeric channels. (A) Schematic representation of the construction of rEag1-I and rEag2-I chimeras. For all schematic cartoons hereafter, rEag1 and rEag2 sequences are shown in red and black, respectively. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated Eag constructs. Two-electrode voltage clamp parameters: the holding potential for rEag1 and rEag2 was -90 and -110 mV, respectively; the pulse protocol comprised 300-ms depolarizing test pulses ranging from -70 to +60 mV (rEag1) or from -100 to +40 mV (rEag2), with 10-mV increments. (C) Membrane localization of GFP-rEag1-I/rEag2-I channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of GFP-rEag1-I/rEag2-I channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for GFP-rEag1, GFP-rEag1-I, GFP-rEag2-I, and GFP-rEag2. The number in parenthesis denotes the amount of neurons analyzed. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)

    Techniques Used: Expressing, Construct

    Characterization of rEag1-II, III, and IV chimeric channels. (A) Schematic representation of the construction of rEag1-II, rEag1-III, and rEag1-IV chimeras. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated rEag1 constructs. (C) Membrane localization of the GFP-rEag1 chimeric channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of the GFP-rEag1 chimeric channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for the GFP-rEag1 chimeric channels. Note the presence of rEag2-like GFP puncta density in rEag1-II only. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)
    Figure Legend Snippet: Characterization of rEag1-II, III, and IV chimeric channels. (A) Schematic representation of the construction of rEag1-II, rEag1-III, and rEag1-IV chimeras. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated rEag1 constructs. (C) Membrane localization of the GFP-rEag1 chimeric channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of the GFP-rEag1 chimeric channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for the GFP-rEag1 chimeric channels. Note the presence of rEag2-like GFP puncta density in rEag1-II only. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)

    Techniques Used: Expressing, Construct

    Characterization of rEag2-II, III, and IV chimeric channels. (A) Schematic representation of the construction of rEag2-II, rEag2-III, and rEag2-IV chimeras. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated rEag2 constructs. (C) Membrane localization of the GFP-rEag2 chimeric channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of the GFP-rEag2 chimeric channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for the GFP-rEag2 chimeric channels. Note the presence of rEag1-like GFP puncta density in rEag2-II only. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)
    Figure Legend Snippet: Characterization of rEag2-II, III, and IV chimeric channels. (A) Schematic representation of the construction of rEag2-II, rEag2-III, and rEag2-IV chimeras. (B) Representative K + currents recorded from Xenopus oocytes over-expressing the indicated rEag2 constructs. (C) Membrane localization of the GFP-rEag2 chimeric channels in HEK293T cells. Scale bar, 10 μm. (D) Expression of the GFP-rEag2 chimeric channels in DIV12 hippocampal neurons. Scale bar, 25 μm. (E) Quantification of the number of GFP puncta per neuron for the GFP-rEag2 chimeric channels. Note the presence of rEag1-like GFP puncta density in rEag2-II only. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)

    Techniques Used: Expressing, Construct

    Expression of GFP-rEag1-K848X channels in hippocampal neurons. ( Left panel ) GFP-rEag1-K848X was over-expressed in DIV12 hippocampal neurons. Similar to GFP-rEag1 channels, the GFP signal arising from the truncation mutant also displayed the characteristic punctate pattern. Scale bar, 25 μm. ( Right panel ) Quantification of the number of GFP puncta per neuron for rEag1-K848X. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)
    Figure Legend Snippet: Expression of GFP-rEag1-K848X channels in hippocampal neurons. ( Left panel ) GFP-rEag1-K848X was over-expressed in DIV12 hippocampal neurons. Similar to GFP-rEag1 channels, the GFP signal arising from the truncation mutant also displayed the characteristic punctate pattern. Scale bar, 25 μm. ( Right panel ) Quantification of the number of GFP puncta per neuron for rEag1-K848X. (*: significantly different from GFP-rEag1; t -test, p < 0.05)(#: significantly different from GFP-rEag2; t -test, p < 0.05)

    Techniques Used: Expressing, Mutagenesis

    The biophysical properties of the chimeric Eag channels. Comparison of the voltage-dependent gating properties of the rEag1 (A) or rEag2 (B) chimeras with their wild-type (WT) counterparts. Steady-state voltage dependence (activation curve) is illustrated as the fraction of open channels ( P o) against the corresponding membrane potential. Activation time constants at indicated potentials were obtained from single exponential fits to the late rising phase of Eag K + currents. Deactivation time constants were derived from single exponential fits to the decay phase of Eag K + currents at the indicated tail potential in response to a +40 mV test pulse. All values are presented as mean ± SEM. Data were collected and analyzed as described previously .
    Figure Legend Snippet: The biophysical properties of the chimeric Eag channels. Comparison of the voltage-dependent gating properties of the rEag1 (A) or rEag2 (B) chimeras with their wild-type (WT) counterparts. Steady-state voltage dependence (activation curve) is illustrated as the fraction of open channels ( P o) against the corresponding membrane potential. Activation time constants at indicated potentials were obtained from single exponential fits to the late rising phase of Eag K + currents. Deactivation time constants were derived from single exponential fits to the decay phase of Eag K + currents at the indicated tail potential in response to a +40 mV test pulse. All values are presented as mean ± SEM. Data were collected and analyzed as described previously .

    Techniques Used: Activation Assay, Derivative Assay

    Steady-state voltage-dependent activation parameters of the rEag1 and  rEag2  chimeric channels
    Figure Legend Snippet: Steady-state voltage-dependent activation parameters of the rEag1 and rEag2 chimeric channels

    Techniques Used: Activation Assay

    cftr antibody  (Alomone Labs)


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    Structured Review

    Alomone Labs cftr antibody
    (A) Immunohistochemical staining of <t>CFTR</t> in SD rat prostate with negative control in the absence of primary antibody. CFTR was expressed at the apical surface of rat ventral prostate epithelium. Scale bar: 100 µm. (B) CFTR transcript was detected by RT-PCR in cultured rat prostate epithelial cells with predicted amplification products at 481 bp. (C) CFTR protein was detected in rat prostate epithelial cells by Western blotting which recognizes a band at MW 160 kDa. (D) Phase contrast image (left) and immunofluorescence staining <t>of</t> <t>cytokeratin</t> 5&8 (middle, green) or CFTR (right, green) in rat prostate epithelial cells. Cell nuclei were counterstained with DAPI (blue). Scale bar: 100 µm.
    Cftr Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cftr antibody/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cftr antibody - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "A Host Defense Mechanism Involving CFTR-Mediated Bicarbonate Secretion in Bacterial Prostatitis"

    Article Title: A Host Defense Mechanism Involving CFTR-Mediated Bicarbonate Secretion in Bacterial Prostatitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0015255

    (A) Immunohistochemical staining of CFTR in SD rat prostate with negative control in the absence of primary antibody. CFTR was expressed at the apical surface of rat ventral prostate epithelium. Scale bar: 100 µm. (B) CFTR transcript was detected by RT-PCR in cultured rat prostate epithelial cells with predicted amplification products at 481 bp. (C) CFTR protein was detected in rat prostate epithelial cells by Western blotting which recognizes a band at MW 160 kDa. (D) Phase contrast image (left) and immunofluorescence staining of cytokeratin 5&8 (middle, green) or CFTR (right, green) in rat prostate epithelial cells. Cell nuclei were counterstained with DAPI (blue). Scale bar: 100 µm.
    Figure Legend Snippet: (A) Immunohistochemical staining of CFTR in SD rat prostate with negative control in the absence of primary antibody. CFTR was expressed at the apical surface of rat ventral prostate epithelium. Scale bar: 100 µm. (B) CFTR transcript was detected by RT-PCR in cultured rat prostate epithelial cells with predicted amplification products at 481 bp. (C) CFTR protein was detected in rat prostate epithelial cells by Western blotting which recognizes a band at MW 160 kDa. (D) Phase contrast image (left) and immunofluorescence staining of cytokeratin 5&8 (middle, green) or CFTR (right, green) in rat prostate epithelial cells. Cell nuclei were counterstained with DAPI (blue). Scale bar: 100 µm.

    Techniques Used: Immunohistochemical staining, Staining, Negative Control, Reverse Transcription Polymerase Chain Reaction, Cell Culture, Amplification, Western Blot, Immunofluorescence

    (A)When 1×10 4 CFU of E.coli was inoculated to the apical compartment of the rat prostate epithelial cells for 18 h, there was no bacterial activity detected in the culture medium. 10 µM CFTR inh -172 (A), 1∶500 CFTR antibody (B) or 50 µM acetazolamide (C) were added with 1×10 5 E.coli to block CFTR or CAII activity and their effect on bacterial activity 18 hours after incubation was shown. (**P<0.01, ***P<0.001).
    Figure Legend Snippet: (A)When 1×10 4 CFU of E.coli was inoculated to the apical compartment of the rat prostate epithelial cells for 18 h, there was no bacterial activity detected in the culture medium. 10 µM CFTR inh -172 (A), 1∶500 CFTR antibody (B) or 50 µM acetazolamide (C) were added with 1×10 5 E.coli to block CFTR or CAII activity and their effect on bacterial activity 18 hours after incubation was shown. (**P<0.01, ***P<0.001).

    Techniques Used: Activity Assay, Blocking Assay, Incubation

    anti cftr antibody  (Alomone Labs)


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  • 95

    Structured Review

    Alomone Labs anti cftr antibody
    (A)When 1×10 4 CFU of E.coli was inoculated to the apical compartment of the rat prostate epithelial cells for 18 h, there was no bacterial activity detected in the culture medium. 10 µM <t>CFTR</t> <t>inh</t> -172 (A), 1∶500 CFTR antibody (B) or 50 µM acetazolamide (C) were added with 1×10 5 E.coli to block CFTR or CAII activity and their effect on bacterial activity 18 hours after incubation was shown. (**P<0.01, ***P<0.001).
    Anti Cftr Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti cftr antibody/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti cftr antibody - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "A Host Defense Mechanism Involving CFTR-Mediated Bicarbonate Secretion in Bacterial Prostatitis"

    Article Title: A Host Defense Mechanism Involving CFTR-Mediated Bicarbonate Secretion in Bacterial Prostatitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0015255

    (A)When 1×10 4 CFU of E.coli was inoculated to the apical compartment of the rat prostate epithelial cells for 18 h, there was no bacterial activity detected in the culture medium. 10 µM CFTR inh -172 (A), 1∶500 CFTR antibody (B) or 50 µM acetazolamide (C) were added with 1×10 5 E.coli to block CFTR or CAII activity and their effect on bacterial activity 18 hours after incubation was shown. (**P<0.01, ***P<0.001).
    Figure Legend Snippet: (A)When 1×10 4 CFU of E.coli was inoculated to the apical compartment of the rat prostate epithelial cells for 18 h, there was no bacterial activity detected in the culture medium. 10 µM CFTR inh -172 (A), 1∶500 CFTR antibody (B) or 50 µM acetazolamide (C) were added with 1×10 5 E.coli to block CFTR or CAII activity and their effect on bacterial activity 18 hours after incubation was shown. (**P<0.01, ***P<0.001).

    Techniques Used: Activity Assay, Blocking Assay, Incubation

    (A) Comparison of E coli bacterial activities recovered from rat prostatitis models without or with CFTR inh -172 (10 µM). Each point indicates the bacterial CFU per gram of prostate tissue weight (***P<0.001). (B) E.coli up-regulated the expression of cytokine genes, CFTR and CAII in rat prostate as determined by RT-PCR. Data were from three experiments. (C) Expression of CFTR (160 kD) and CAII (29 kD) protein was significantly up-regulated in E.coli -infected rat prostate as determined by western blot. Data were from three experiments. (*P<0.05, **P<0.01, ***P<0.001).
    Figure Legend Snippet: (A) Comparison of E coli bacterial activities recovered from rat prostatitis models without or with CFTR inh -172 (10 µM). Each point indicates the bacterial CFU per gram of prostate tissue weight (***P<0.001). (B) E.coli up-regulated the expression of cytokine genes, CFTR and CAII in rat prostate as determined by RT-PCR. Data were from three experiments. (C) Expression of CFTR (160 kD) and CAII (29 kD) protein was significantly up-regulated in E.coli -infected rat prostate as determined by western blot. Data were from three experiments. (*P<0.05, **P<0.01, ***P<0.001).

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Infection, Western Blot