mirp1  (Alomone Labs)


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    Alomone Labs mirp1
    Mirp1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mirp1/product/Alomone Labs
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mirp1 - by Bioz Stars, 2022-05
    91/100 stars

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    Alomone Labs rabbit anti mirp1
    <t>MIRP1</t> and DPPX expression in rabbit CB chemoreceptor cells. (A) The presence of MiRP1 protein in cultured CB chemoreceptor cells was explored by double labeling with anti-TH and anti-MiRP1 antibody. MiRP1-positive cells were scant and of those very few were chemoreceptor cells (as the one marked with the arrow). The corresponding transmitted light image is also shown for each field. (B) Immunofluorescence labeling of DPPX shows the expression of DPPX in every TH-positive cell (and also in some TH-negative cells). Anti-DPPX antibody provided by E. Wettwer. (C) Same results as in B were obtained with anti-DPPX antibody from Santa Cruz Biotechnologies. (D) Double labeling of CB chemoreceptor cells with anti-Kv4.3 and anti-DPPX antibodies shows an almost perfect coexpression of these two proteins, as expected if they associate in heteromultimeric channels. (E) Specificity of the DPPX antibodies was explored in HEK cells transfected with GFP+DPPX. (F) Deconvolved images showing a preferential localization of DPPX (arrows) in the surface of a Kv4.3+DPPX-transfected HEK cell (left) and a chemoreceptor cell (right). Red fluorescence corresponds to DPPX labeling, and green fluorescence corresponds to GFP (left) or TH (right) labeling. Anti-DPPX antibody from E. Wettwer was used in E and F, but the same results were obtained with the other antibody tested. (G) Real-time PCR showing the relative abundance of DPPX mRNA in CB chemoreceptor cells in primary culture. Normalized amount of DPPX mRNA in rabbit hippocampus (Hipp) was used as calibrator, and DPPX mRNA abundance in whole cerebellum (Tissue) and in cerebellar granule cells (G cells) were determined for comparisons. For details of the 2 −ΔΔCt relative quantification method see Materials and methods section. Each bar is the mean ± SEM of four to seven individual determinations.
    Rabbit Anti Mirp1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti mirp1/product/Alomone Labs
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti mirp1 - by Bioz Stars, 2022-05
    91/100 stars
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    MIRP1 and DPPX expression in rabbit CB chemoreceptor cells. (A) The presence of MiRP1 protein in cultured CB chemoreceptor cells was explored by double labeling with anti-TH and anti-MiRP1 antibody. MiRP1-positive cells were scant and of those very few were chemoreceptor cells (as the one marked with the arrow). The corresponding transmitted light image is also shown for each field. (B) Immunofluorescence labeling of DPPX shows the expression of DPPX in every TH-positive cell (and also in some TH-negative cells). Anti-DPPX antibody provided by E. Wettwer. (C) Same results as in B were obtained with anti-DPPX antibody from Santa Cruz Biotechnologies. (D) Double labeling of CB chemoreceptor cells with anti-Kv4.3 and anti-DPPX antibodies shows an almost perfect coexpression of these two proteins, as expected if they associate in heteromultimeric channels. (E) Specificity of the DPPX antibodies was explored in HEK cells transfected with GFP+DPPX. (F) Deconvolved images showing a preferential localization of DPPX (arrows) in the surface of a Kv4.3+DPPX-transfected HEK cell (left) and a chemoreceptor cell (right). Red fluorescence corresponds to DPPX labeling, and green fluorescence corresponds to GFP (left) or TH (right) labeling. Anti-DPPX antibody from E. Wettwer was used in E and F, but the same results were obtained with the other antibody tested. (G) Real-time PCR showing the relative abundance of DPPX mRNA in CB chemoreceptor cells in primary culture. Normalized amount of DPPX mRNA in rabbit hippocampus (Hipp) was used as calibrator, and DPPX mRNA abundance in whole cerebellum (Tissue) and in cerebellar granule cells (G cells) were determined for comparisons. For details of the 2 −ΔΔCt relative quantification method see Materials and methods section. Each bar is the mean ± SEM of four to seven individual determinations.

    Journal: The Journal of General Physiology

    Article Title: A Role for DPPX Modulating External TEA Sensitivity of Kv4 Channels

    doi: 10.1085/jgp.200709912

    Figure Lengend Snippet: MIRP1 and DPPX expression in rabbit CB chemoreceptor cells. (A) The presence of MiRP1 protein in cultured CB chemoreceptor cells was explored by double labeling with anti-TH and anti-MiRP1 antibody. MiRP1-positive cells were scant and of those very few were chemoreceptor cells (as the one marked with the arrow). The corresponding transmitted light image is also shown for each field. (B) Immunofluorescence labeling of DPPX shows the expression of DPPX in every TH-positive cell (and also in some TH-negative cells). Anti-DPPX antibody provided by E. Wettwer. (C) Same results as in B were obtained with anti-DPPX antibody from Santa Cruz Biotechnologies. (D) Double labeling of CB chemoreceptor cells with anti-Kv4.3 and anti-DPPX antibodies shows an almost perfect coexpression of these two proteins, as expected if they associate in heteromultimeric channels. (E) Specificity of the DPPX antibodies was explored in HEK cells transfected with GFP+DPPX. (F) Deconvolved images showing a preferential localization of DPPX (arrows) in the surface of a Kv4.3+DPPX-transfected HEK cell (left) and a chemoreceptor cell (right). Red fluorescence corresponds to DPPX labeling, and green fluorescence corresponds to GFP (left) or TH (right) labeling. Anti-DPPX antibody from E. Wettwer was used in E and F, but the same results were obtained with the other antibody tested. (G) Real-time PCR showing the relative abundance of DPPX mRNA in CB chemoreceptor cells in primary culture. Normalized amount of DPPX mRNA in rabbit hippocampus (Hipp) was used as calibrator, and DPPX mRNA abundance in whole cerebellum (Tissue) and in cerebellar granule cells (G cells) were determined for comparisons. For details of the 2 −ΔΔCt relative quantification method see Materials and methods section. Each bar is the mean ± SEM of four to seven individual determinations.

    Article Snippet: The primary antibodies, mouse anti-TH (Abcam), goat anti-Kv4.3 (Santa Cruz Biotechnology), rabbit anti-MiRP1 (Alomone laboratories), rabbit anti-DPPX (provided by E. Wettwer, Dresden University of Technology, Dresden, Germany) or goat anti-DPPX (Santa Cruz Biotechnologies), were diluted in blocking solution and incubated with the cells for 60 min at room temperature.

    Techniques: Expressing, Cell Culture, Labeling, Immunofluorescence, Transfection, Fluorescence, Real-time Polymerase Chain Reaction

    Putative BACE1 and PS/γ-secretase cleavage sites of human KCNE1 and KCNE2.

    Journal: The FASEB Journal

    Article Title: BACE1 and presenilin/?-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels

    doi: 10.1096/fj.12-214056

    Figure Lengend Snippet: Putative BACE1 and PS/γ-secretase cleavage sites of human KCNE1 and KCNE2.

    Article Snippet: Primary antibodies were used at the following dilutions: GAPDH, 1:1000 (Chemicon, Temecula, CA, USA), BACE1 poly antibody, 1:1000 (Abcam), anti-KCNQ1 antibody, 1:200 (UC Davis/NIH NeuroMab Facility), anti-KCNE1, 1:250 with 5% BSA (Alomone Labs), anti-KCNE2, 1:250 with 1% BSA (Alomone Labs), and anti-V5, 1:5000 with 5% BSA (Invitrogen).

    Techniques:

    Elevated BACE1 activity increases KCNE1- and KCNE2-CTF levels in B104 rat neuroblastoma cells. A ) Overexpression of human BACE1 increased KCNE1-CTF levels in B104 cells. DAPT treatment further enhanced KCNE1-CTF levels in control and BACE1-overexpressing cells. B ) KCNE2-CTF levels were also elevated by BACE1 overexpression in B104 cells.

    Journal: The FASEB Journal

    Article Title: BACE1 and presenilin/?-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels

    doi: 10.1096/fj.12-214056

    Figure Lengend Snippet: Elevated BACE1 activity increases KCNE1- and KCNE2-CTF levels in B104 rat neuroblastoma cells. A ) Overexpression of human BACE1 increased KCNE1-CTF levels in B104 cells. DAPT treatment further enhanced KCNE1-CTF levels in control and BACE1-overexpressing cells. B ) KCNE2-CTF levels were also elevated by BACE1 overexpression in B104 cells.

    Article Snippet: Primary antibodies were used at the following dilutions: GAPDH, 1:1000 (Chemicon, Temecula, CA, USA), BACE1 poly antibody, 1:1000 (Abcam), anti-KCNQ1 antibody, 1:200 (UC Davis/NIH NeuroMab Facility), anti-KCNE1, 1:250 with 5% BSA (Alomone Labs), anti-KCNE2, 1:250 with 1% BSA (Alomone Labs), and anti-V5, 1:5000 with 5% BSA (Invitrogen).

    Techniques: Activity Assay, Over Expression

    PS/γ-secretase activity regulates generation of KCNE1- and KCNE2-ICDs. A ) Western blot analysis showed that KCNE1-ICD is specifically regulated by PS/γ-secretase activity in B104 cells stably expressing full-length KCNE1. Epoxomicin, a proteasome inhibitor, prevented KCNE1-ICD degradation. B ) KCNE2-ICD is detected in the similar conditions.

    Journal: The FASEB Journal

    Article Title: BACE1 and presenilin/?-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels

    doi: 10.1096/fj.12-214056

    Figure Lengend Snippet: PS/γ-secretase activity regulates generation of KCNE1- and KCNE2-ICDs. A ) Western blot analysis showed that KCNE1-ICD is specifically regulated by PS/γ-secretase activity in B104 cells stably expressing full-length KCNE1. Epoxomicin, a proteasome inhibitor, prevented KCNE1-ICD degradation. B ) KCNE2-ICD is detected in the similar conditions.

    Article Snippet: Primary antibodies were used at the following dilutions: GAPDH, 1:1000 (Chemicon, Temecula, CA, USA), BACE1 poly antibody, 1:1000 (Abcam), anti-KCNQ1 antibody, 1:200 (UC Davis/NIH NeuroMab Facility), anti-KCNE1, 1:250 with 5% BSA (Alomone Labs), anti-KCNE2, 1:250 with 1% BSA (Alomone Labs), and anti-V5, 1:5000 with 5% BSA (Invitrogen).

    Techniques: Activity Assay, Western Blot, Stable Transfection, Expressing

    KCNE1 and KCNE2 undergo sequential cleavage mediated by α- and PS/γ-secretases. A ) Schematic diagram showing sequential cleavage of KCNE1 and KCNE2 by BACE1, α-, and PS/γ-secretases. α-Secretase inhibitor (TAPI-1) or BACE1 inhibitor ( D R9) decreases generation of KCNE C-terminal fragments (KCNE-CTFs), while PMA, an α-secretase activator, increases KCNE-CTF levels. KCNE-CTFs are then cleaved by PS/γ-secretases to generate KCNE intracellular domains (KCNE-ICDs). B ) Western blot analysis of human KCNE1 full-length (F.L.) and its CTF expressed in B104 cells. KCNE1-CTF levels were increased by treatment with DAPT and further elevated by cotreatment with PMA, while partially decreased by TAPI-1. C ) Western blot analysis of human KCNE2 F.L. and its CTF expressed in B104 cells. Similar to KCNE1, KCNE2-CTF levels are also increased by DAPT treatment and further elevated by cotreatment with PMA.

    Journal: The FASEB Journal

    Article Title: BACE1 and presenilin/?-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels

    doi: 10.1096/fj.12-214056

    Figure Lengend Snippet: KCNE1 and KCNE2 undergo sequential cleavage mediated by α- and PS/γ-secretases. A ) Schematic diagram showing sequential cleavage of KCNE1 and KCNE2 by BACE1, α-, and PS/γ-secretases. α-Secretase inhibitor (TAPI-1) or BACE1 inhibitor ( D R9) decreases generation of KCNE C-terminal fragments (KCNE-CTFs), while PMA, an α-secretase activator, increases KCNE-CTF levels. KCNE-CTFs are then cleaved by PS/γ-secretases to generate KCNE intracellular domains (KCNE-ICDs). B ) Western blot analysis of human KCNE1 full-length (F.L.) and its CTF expressed in B104 cells. KCNE1-CTF levels were increased by treatment with DAPT and further elevated by cotreatment with PMA, while partially decreased by TAPI-1. C ) Western blot analysis of human KCNE2 F.L. and its CTF expressed in B104 cells. Similar to KCNE1, KCNE2-CTF levels are also increased by DAPT treatment and further elevated by cotreatment with PMA.

    Article Snippet: Primary antibodies were used at the following dilutions: GAPDH, 1:1000 (Chemicon, Temecula, CA, USA), BACE1 poly antibody, 1:1000 (Abcam), anti-KCNQ1 antibody, 1:200 (UC Davis/NIH NeuroMab Facility), anti-KCNE1, 1:250 with 5% BSA (Alomone Labs), anti-KCNE2, 1:250 with 1% BSA (Alomone Labs), and anti-V5, 1:5000 with 5% BSA (Invitrogen).

    Techniques: Western Blot

    α-Secretase, BACE1, and PS/γ-secretase activities regulate KCNE2-CTF levels in cultured mouse primary neurons. A ) Detection of endogenous KCNE2 full-length (F.L.) and KCNE2-CTF bands in cultured mouse primary cortical/hippocampal neurons (DIV14). DAPT treatment specifically increased 10-kDa KCNE2-CTF levels. B ) Relative levels of KCNE2-CTF in panel A were quantitated ( n =3/condition). * P

    Journal: The FASEB Journal

    Article Title: BACE1 and presenilin/?-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels

    doi: 10.1096/fj.12-214056

    Figure Lengend Snippet: α-Secretase, BACE1, and PS/γ-secretase activities regulate KCNE2-CTF levels in cultured mouse primary neurons. A ) Detection of endogenous KCNE2 full-length (F.L.) and KCNE2-CTF bands in cultured mouse primary cortical/hippocampal neurons (DIV14). DAPT treatment specifically increased 10-kDa KCNE2-CTF levels. B ) Relative levels of KCNE2-CTF in panel A were quantitated ( n =3/condition). * P

    Article Snippet: Primary antibodies were used at the following dilutions: GAPDH, 1:1000 (Chemicon, Temecula, CA, USA), BACE1 poly antibody, 1:1000 (Abcam), anti-KCNQ1 antibody, 1:200 (UC Davis/NIH NeuroMab Facility), anti-KCNE1, 1:250 with 5% BSA (Alomone Labs), anti-KCNE2, 1:250 with 1% BSA (Alomone Labs), and anti-V5, 1:5000 with 5% BSA (Invitrogen).

    Techniques: Cell Culture

    Dysbindin null developing hippocampus changes the expression of potassium channel subunits. (A) Volcano plot of Cuffdiff analysis shows ( Trapnell et al., 2012 ) differentially expressed genes in Bloc1s8 sdy/sdy hippocampus as in Figure 3B . Arrows mark potassium channel subunit genes for reference. (B) Illumina sequence reads maps for the listed genes from assembly mm9. (C) Postnatal day 7 hippocampi mRNA were quantified by real time quantitative PCR for Kcne2 and Kcnj13 . All determinations were performed from at least three animals per genotype and three independent cDNA preparations for qRT-PCR. Comparisons between wild type and Bloc1s8 sdy/sdy were performed with Wilcoxon–Mann–Whitney Rank Sum Test. All comparisons were significantly different with a p

    Journal: Frontiers in Genetics

    Article Title: Dysbindin Deficiency Modifies the Expression of GABA Neuron and Ion Permeation Transcripts in the Developing Hippocampus

    doi: 10.3389/fgene.2017.00028

    Figure Lengend Snippet: Dysbindin null developing hippocampus changes the expression of potassium channel subunits. (A) Volcano plot of Cuffdiff analysis shows ( Trapnell et al., 2012 ) differentially expressed genes in Bloc1s8 sdy/sdy hippocampus as in Figure 3B . Arrows mark potassium channel subunit genes for reference. (B) Illumina sequence reads maps for the listed genes from assembly mm9. (C) Postnatal day 7 hippocampi mRNA were quantified by real time quantitative PCR for Kcne2 and Kcnj13 . All determinations were performed from at least three animals per genotype and three independent cDNA preparations for qRT-PCR. Comparisons between wild type and Bloc1s8 sdy/sdy were performed with Wilcoxon–Mann–Whitney Rank Sum Test. All comparisons were significantly different with a p

    Article Snippet: AntibodiesAntibodies utilized in this study: rabbit anti-parvalbumin (ThermoFisher Scientific PA1-933), mouse anti-synaptophysin (EMD Millipore MAB5258), mouse anti-actin-beta (Sigma A5451), mouse anti-Hspa9/mortalin (NeuroMab N52A/42), rabbit anti-Bloc1s8 (gift from Dr. Talbot), mouse anti-Vgat (Synaptic Systems 131011), and rabbit anti-Kcne2 (Alomone APC-054).

    Techniques: Expressing, Sequencing, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, MANN-WHITNEY