anti nkcc1 slc12a2 extracellular antibody  (Alomone Labs)


Bioz Verified Symbol Alomone Labs is a verified supplier
Bioz Manufacturer Symbol Alomone Labs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Alomone Labs anti nkcc1 slc12a2 extracellular antibody
    Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary <t>anti-NKCC1</t> antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.
    Anti Nkcc1 Slc12a2 Extracellular Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti nkcc1 slc12a2 extracellular antibody/product/Alomone Labs
    Average 94 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    anti nkcc1 slc12a2 extracellular antibody - by Bioz Stars, 2022-08
    94/100 stars

    Images

    1) Product Images from "Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus"

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    Journal: bioRxiv

    doi: 10.1101/2022.02.21.481301

    Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.
    Figure Legend Snippet: Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.

    Techniques Used: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    2) Product Images from "Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus"

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    Journal: Fluids and Barriers of the CNS

    doi: 10.1186/s12987-022-00335-x

    Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side
    Figure Legend Snippet: Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side

    Techniques Used: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    3) Product Images from "Novel γ-sarcoglycan interactors in murine muscle membranes"

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    Journal: Skeletal Muscle

    doi: 10.1186/s13395-021-00285-2

    Pathway analysis suggests cross-talk between interconnected survival signaling pathways and sarcolemmal sarcoglycans, dystrophin, and archvillin. The gene names of proteins co-immunoprecipitating with or binding to Sgcg as shown here were arranged in the default Organic View using IPA software. Eleven of 13 Top Candidate Sgcg interactors, as well as 3 of 5 Other Candidate interactors (Fig. 3 ), were assigned to either the TP53/ESR2/TRIM25-associated signaling network or to the sarcoglycan, dystrophin, dystroglycan-associated sarcolemmal network. Colors highlight SGCG (magenta), SVIL (yellow), NKCC1/SLC12A2 (green), additional Top Candidate Interactors (blue) and Other Candidate Interactors (gray). Additional genes (white) and direct (solid lines) and indirect (dashed lines) interactions were added by the IPA software. Interactions involving the B-Raf, MEK1/2, and ERK1/2 signaling cascade (orange) with β-dystroglycan/DAG [ 88 ] and SVIL [ 30 ] were added manually
    Figure Legend Snippet: Pathway analysis suggests cross-talk between interconnected survival signaling pathways and sarcolemmal sarcoglycans, dystrophin, and archvillin. The gene names of proteins co-immunoprecipitating with or binding to Sgcg as shown here were arranged in the default Organic View using IPA software. Eleven of 13 Top Candidate Sgcg interactors, as well as 3 of 5 Other Candidate interactors (Fig. 3 ), were assigned to either the TP53/ESR2/TRIM25-associated signaling network or to the sarcoglycan, dystrophin, dystroglycan-associated sarcolemmal network. Colors highlight SGCG (magenta), SVIL (yellow), NKCC1/SLC12A2 (green), additional Top Candidate Interactors (blue) and Other Candidate Interactors (gray). Additional genes (white) and direct (solid lines) and indirect (dashed lines) interactions were added by the IPA software. Interactions involving the B-Raf, MEK1/2, and ERK1/2 signaling cascade (orange) with β-dystroglycan/DAG [ 88 ] and SVIL [ 30 ] were added manually

    Techniques Used: Binding Assay, Indirect Immunoperoxidase Assay, Software

    HA-CFP-NKCC1-cytoplasmic domains appear to be loosely associated with Flag-tagged SC proteins. RH30 cells were co-transfected in parallel with Flag-tagged sarcoglycans and stained as in Fig. 4 . A HA-CFP-NKCC1-cytoplasmic domains and B HA-CFP (negative control; panels a, a’; blue in merges) were visualized with Flag-tagged sarcoglycans (panels b, b’; red in merges) and F-actin (panels c, c’; green in merges). After pre-extraction with 0.1% Triton X-100, C signal from residual HA-CFP-NKCC1-cytoplasmic domain was indistinguishable from D residual HA-CFP. Overlapping HA and Flag signals in magenta (arrows). Bars (d), 20 μm; bar (d’), 5 μm
    Figure Legend Snippet: HA-CFP-NKCC1-cytoplasmic domains appear to be loosely associated with Flag-tagged SC proteins. RH30 cells were co-transfected in parallel with Flag-tagged sarcoglycans and stained as in Fig. 4 . A HA-CFP-NKCC1-cytoplasmic domains and B HA-CFP (negative control; panels a, a’; blue in merges) were visualized with Flag-tagged sarcoglycans (panels b, b’; red in merges) and F-actin (panels c, c’; green in merges). After pre-extraction with 0.1% Triton X-100, C signal from residual HA-CFP-NKCC1-cytoplasmic domain was indistinguishable from D residual HA-CFP. Overlapping HA and Flag signals in magenta (arrows). Bars (d), 20 μm; bar (d’), 5 μm

    Techniques Used: Transfection, Staining, Negative Control

    Effects of NKCC1 inhibition on muscle force generation and ERK phosphorylation. A Isometric tetanic force generation of EDL muscles is not altered by bumetanide (BUM) incubation, as compared with vehicle (VEH) control. Raw values showing forces in Ringer’s solution as pre-treatment (Pre-Tx), and the forces following 20–30-min incubation in 50 μM bumetanide or vehicle (ethanol) as post-treatment (Post-Tx). B Decrement of force following eccentric contractions (ECC) is not affected by bumetanide incubation. Forces are relative to the initial force in the first ECC. Means shown; error bars SEM. C levels of phosphorylated ERK are elevated in resting EDL muscles from wild-type mice, but the P-ERK response to ECC is unaffected. (*, P
    Figure Legend Snippet: Effects of NKCC1 inhibition on muscle force generation and ERK phosphorylation. A Isometric tetanic force generation of EDL muscles is not altered by bumetanide (BUM) incubation, as compared with vehicle (VEH) control. Raw values showing forces in Ringer’s solution as pre-treatment (Pre-Tx), and the forces following 20–30-min incubation in 50 μM bumetanide or vehicle (ethanol) as post-treatment (Post-Tx). B Decrement of force following eccentric contractions (ECC) is not affected by bumetanide incubation. Forces are relative to the initial force in the first ECC. Means shown; error bars SEM. C levels of phosphorylated ERK are elevated in resting EDL muscles from wild-type mice, but the P-ERK response to ECC is unaffected. (*, P

    Techniques Used: Inhibition, Incubation, Mouse Assay

    Flag-tagged Sgcg directly or indirectly associates with HA-CFP-tagged NKCC1 proteins. A Immunoblot of the most successful co-IP, showing more Sgcg-Flag sedimenting with the NKCC1 and NKCC1-cyto (bound), compared to the HA-CFP negative control; corresponding decreases were observed in supernatants after sedimentation (Unbound). Sgcg-Flag amounts in cell lysates also are shown (Input). Flag-tagged Sgcg, Sgcb, and Sgcd proteins were co-expressed with either HA-CFP-NKCC1 (lane 1), HA-CFP (lane 2), or HA-CFP-NKCC1 cytoplasmic domains (NKCC1-cyto, lane 3) in RH-30 cells and immunoprecipitated with anti-HA. Bound NKCC1 proteins were visualized with anti-HA (asterisks); bead-bound rabbit anti-HA heavy chain (IgG). B Densitometric quantification of Unbound/Input ratios of Sgcg-Flag from supernatant-depletion assays, such as those shown in C , and analysis by one-way ANOVA with Tukey’s multiple comparisons test. P values for the mean differences between HA-CFP control and HA-CFP-NKCC1 and HA-CFP-NKCC1-cyto were 0.12 and 0.02, respectively (* P
    Figure Legend Snippet: Flag-tagged Sgcg directly or indirectly associates with HA-CFP-tagged NKCC1 proteins. A Immunoblot of the most successful co-IP, showing more Sgcg-Flag sedimenting with the NKCC1 and NKCC1-cyto (bound), compared to the HA-CFP negative control; corresponding decreases were observed in supernatants after sedimentation (Unbound). Sgcg-Flag amounts in cell lysates also are shown (Input). Flag-tagged Sgcg, Sgcb, and Sgcd proteins were co-expressed with either HA-CFP-NKCC1 (lane 1), HA-CFP (lane 2), or HA-CFP-NKCC1 cytoplasmic domains (NKCC1-cyto, lane 3) in RH-30 cells and immunoprecipitated with anti-HA. Bound NKCC1 proteins were visualized with anti-HA (asterisks); bead-bound rabbit anti-HA heavy chain (IgG). B Densitometric quantification of Unbound/Input ratios of Sgcg-Flag from supernatant-depletion assays, such as those shown in C , and analysis by one-way ANOVA with Tukey’s multiple comparisons test. P values for the mean differences between HA-CFP control and HA-CFP-NKCC1 and HA-CFP-NKCC1-cyto were 0.12 and 0.02, respectively (* P

    Techniques Used: Co-Immunoprecipitation Assay, Negative Control, Sedimentation, Immunoprecipitation

    Confocal microscopy of NKCC1 and dystrophin in EDL muscles from WT and Sgcg − / − mice. A – H Cross sections show overlapping signals at the sarcolemma (arrowheads; yellow in merges), as well as internal myofibrillar NKCC1 staining in both genotypes. I – P In longitudinal sections, the internal staining suggests an association with T-tubules, which end at dystrophin-associated costameres in the sarcolemma [ 8 , 9 , 82 ]. I’ – L’ Enlargements of the area boxed in L . Q – T Sections stained with only secondary antibodies. Bars are A – H 50 μm; I – T 20 μm; I’ – L’ 5 μm
    Figure Legend Snippet: Confocal microscopy of NKCC1 and dystrophin in EDL muscles from WT and Sgcg − / − mice. A – H Cross sections show overlapping signals at the sarcolemma (arrowheads; yellow in merges), as well as internal myofibrillar NKCC1 staining in both genotypes. I – P In longitudinal sections, the internal staining suggests an association with T-tubules, which end at dystrophin-associated costameres in the sarcolemma [ 8 , 9 , 82 ]. I’ – L’ Enlargements of the area boxed in L . Q – T Sections stained with only secondary antibodies. Bars are A – H 50 μm; I – T 20 μm; I’ – L’ 5 μm

    Techniques Used: Confocal Microscopy, Mouse Assay, Staining

    NKCC1 co-localizes with the sarcoglycan complex in large, detergent-stable vesicular structures. A , B HA-CFP-tagged NKCC1 (panels a, a’, blue in merges) co-localizes in punctae visualized with both A our affinity-purified anti-Sgcg and B anti-Sgcg from Proteintech Group (PTG) (panels b, b’, red in merges) after expression in RH30 rhabdomyosarcoma cells with Flag-tagged Sgcg, Sgcd, and Sgcb. Enlargements shown (a’–d’) of the boxed areas in panels a–d. C Specificity control with nonimmune rabbit (Rb) IgG substituted for anti-Sgcg. D Signal overlaps of HA-CFP-NKCC1 (panels a, a’, blue in merges) and the sarcoglycan complex (panels a, a’, red in merges) persist even when cells are briefly extracted with 0.1% Triton X-100 before fixation. E The HA-CFP tag alone (panel a, blue in merge) does not persist in pre-extracted RH30 cells co-transfected with Flag-tagged Sgcg, Sgcd, and Sgcb (panel a, red in merge). A – E Phalloidin-stained actin filaments delineate cell boundaries (panels c, c’, green in merges). Bars (d), 20 μm; bars (d’), 5 μm. Overlapping HA and Flag signals in magenta (arrows)
    Figure Legend Snippet: NKCC1 co-localizes with the sarcoglycan complex in large, detergent-stable vesicular structures. A , B HA-CFP-tagged NKCC1 (panels a, a’, blue in merges) co-localizes in punctae visualized with both A our affinity-purified anti-Sgcg and B anti-Sgcg from Proteintech Group (PTG) (panels b, b’, red in merges) after expression in RH30 rhabdomyosarcoma cells with Flag-tagged Sgcg, Sgcd, and Sgcb. Enlargements shown (a’–d’) of the boxed areas in panels a–d. C Specificity control with nonimmune rabbit (Rb) IgG substituted for anti-Sgcg. D Signal overlaps of HA-CFP-NKCC1 (panels a, a’, blue in merges) and the sarcoglycan complex (panels a, a’, red in merges) persist even when cells are briefly extracted with 0.1% Triton X-100 before fixation. E The HA-CFP tag alone (panel a, blue in merge) does not persist in pre-extracted RH30 cells co-transfected with Flag-tagged Sgcg, Sgcd, and Sgcb (panel a, red in merge). A – E Phalloidin-stained actin filaments delineate cell boundaries (panels c, c’, green in merges). Bars (d), 20 μm; bars (d’), 5 μm. Overlapping HA and Flag signals in magenta (arrows)

    Techniques Used: Affinity Purification, Expressing, Transfection, Staining

    4) Product Images from "Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus"

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    Journal: bioRxiv

    doi: 10.1101/2022.02.21.481301

    Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.
    Figure Legend Snippet: Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.

    Techniques Used: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    5) Product Images from "KCC2 expression supersedes NKCC1 in mature fiber cells in mouse and rabbit lenses "

    Article Title: KCC2 expression supersedes NKCC1 in mature fiber cells in mouse and rabbit lenses

    Journal: Molecular Vision

    doi:

    NKCC1 and KCC2b in situ immunofluorescence detection in young adult rabbit lens. A , B : NKCC1 mAb and anti-KCC2 antibody detection in young adult rabbit lens (100X). C – E : NKCC1 expression in the cortical fiber cells is decreased as fiber cells mature in the lens interior. KCC2 is detected in fiber cells closer to the lens center. Merged images C , D are shown in panel E (200X). F : KCC2b is detected at the fiber cell membrane borders in mature interior fiber cells (200X). G : KCC2b viewed at 600X magnification. Rabbit fiber cells are about 10 μm across in their longest dimension. The asterisks identify comparable positions in the panels.
    Figure Legend Snippet: NKCC1 and KCC2b in situ immunofluorescence detection in young adult rabbit lens. A , B : NKCC1 mAb and anti-KCC2 antibody detection in young adult rabbit lens (100X). C – E : NKCC1 expression in the cortical fiber cells is decreased as fiber cells mature in the lens interior. KCC2 is detected in fiber cells closer to the lens center. Merged images C , D are shown in panel E (200X). F : KCC2b is detected at the fiber cell membrane borders in mature interior fiber cells (200X). G : KCC2b viewed at 600X magnification. Rabbit fiber cells are about 10 μm across in their longest dimension. The asterisks identify comparable positions in the panels.

    Techniques Used: In Situ, Immunofluorescence, Expressing

    KCC2 and NKCC1 expression in a 30-day-old mouse lens. A : KCC2 mAb immunofluorescence detection (400X magnification) in mouse lens corresponds to the arrowhead in panel D . The lens perimeter is at the left. B : Anti-KCC2b (400X magnification; inset plus ~ 2X photomagnification). KCC2 is detected at the fiber cell borders in the interior lens fiber cells in the inset photo. Mouse lens fiber cells are about 7 μm in their longest dimension. C : Anti-KCC2b (600×, 3X photomagnification) identifies expression in cortical fiber cells as they terminally differentiate to mature fiber cells (arrowheads indicate the sites of the unstained cell nuclei). D : KCC2 is detected in interior fiber cells in the mouse lens (100X). The asterisk identifies the corresponding position in panel E and identifies KCC2 expression in the lens interior. The arrow at the lower left indicates the lens perimeter. E : NKCC1 mAb (monoclonal Ab) detection of cortical fiber cells with little detection in the interior lens nucleus. F : Lower exposure photo showing anti-NKCC1 polyclonal antibody detection restricted to lens cortical fibers in the mouse lens (200X, original magnification). G : KCC2b lower exposure detects protein in the cortical fiber cells. H : No primary antibody control. I : KCC2 detected at a site corresponding to the arrowhead in panel D . J : Actin detected in the same view as in panel H . K : I , J merged images. L : Immunoblot identifies KCC2b expression in the total mouse lens protein samples.
    Figure Legend Snippet: KCC2 and NKCC1 expression in a 30-day-old mouse lens. A : KCC2 mAb immunofluorescence detection (400X magnification) in mouse lens corresponds to the arrowhead in panel D . The lens perimeter is at the left. B : Anti-KCC2b (400X magnification; inset plus ~ 2X photomagnification). KCC2 is detected at the fiber cell borders in the interior lens fiber cells in the inset photo. Mouse lens fiber cells are about 7 μm in their longest dimension. C : Anti-KCC2b (600×, 3X photomagnification) identifies expression in cortical fiber cells as they terminally differentiate to mature fiber cells (arrowheads indicate the sites of the unstained cell nuclei). D : KCC2 is detected in interior fiber cells in the mouse lens (100X). The asterisk identifies the corresponding position in panel E and identifies KCC2 expression in the lens interior. The arrow at the lower left indicates the lens perimeter. E : NKCC1 mAb (monoclonal Ab) detection of cortical fiber cells with little detection in the interior lens nucleus. F : Lower exposure photo showing anti-NKCC1 polyclonal antibody detection restricted to lens cortical fibers in the mouse lens (200X, original magnification). G : KCC2b lower exposure detects protein in the cortical fiber cells. H : No primary antibody control. I : KCC2 detected at a site corresponding to the arrowhead in panel D . J : Actin detected in the same view as in panel H . K : I , J merged images. L : Immunoblot identifies KCC2b expression in the total mouse lens protein samples.

    Techniques Used: Expressing, Immunofluorescence

    6) Product Images from "Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus"

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    Journal: Fluids and Barriers of the CNS

    doi: 10.1186/s12987-022-00335-x

    Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side
    Figure Legend Snippet: Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side

    Techniques Used: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Alomone Labs anti nkcc1 slc12a2 extracellular antibody
    Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary <t>anti-NKCC1</t> antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.
    Anti Nkcc1 Slc12a2 Extracellular Antibody, 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 nkcc1 slc12a2 extracellular antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti nkcc1 slc12a2 extracellular antibody - by Bioz Stars, 2022-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.

    Journal: bioRxiv

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    doi: 10.1101/2022.02.21.481301

    Figure Lengend Snippet: Choroid plexus transcriptomic profile similar to FACS choroid plexus epithelial cells. a-d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner (a-c). d Immunohistochemical staining of the captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e-g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f, for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side.

    Article Snippet: The cells were triturated 20 times with a 1000 µl pipette and filtered through a 70 μm filter (pluriStrainer, Mini 70 µm, PluriSelect, Leipzig, Germany), prior to incubation with an anti-NKCC1 antibody with an extracellular epitope (1:200 in aCSF-HEPES, #ANT-071, Alomone Labs™, Jerusalem, Israel) for 30 minutes at 4°C.

    Techniques: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side

    Journal: Fluids and Barriers of the CNS

    Article Title: Transcriptional profiling of transport mechanisms and regulatory pathways in rat choroid plexus

    doi: 10.1186/s12987-022-00335-x

    Figure Lengend Snippet: Choroid plexus transcriptomic profile is similar to FACS choroid plexus epithelial cells. a – d FACS with fluorescence emission intensity (y-axis) and forward scatter (FSC) (x-axis). a The cell suspension obtained by FACS with primary anti-NKCC1 antibody and secondary antibody, b in the absence of antibody inclusion in the FACS procedure, or c in the absence of primary antibody, but with inclusion of secondary antibody. The target area of capture (cells with high fluorescence emission intensity and large cell size) is defined in a black square in the top right corner ( a – c ). d Immunohistochemical staining of captured cells with anti-AQP1 (green), marker of F-actin; phalloidin (red), and nucleus marker; DAPI (blue). e – g Depiction of the shared transcribed genes in the pure fraction of choroid plexus epithelial cells versus the whole choroid plexus, e for all genes, f for genes encoding membrane transporters and pumps, and g for genes encoding membrane water and ion channels. Shared genes (in percentages and number) in the sphere center, with the number of non-shared genes depicted on either side

    Article Snippet: The cells were triturated 20 times with a 1000 µl pipette and filtered through a 70 μm filter (pluriStrainer, Mini 70 µm, PluriSelect, Leipzig, Germany), prior to incubation with an anti-NKCC1 antibody with an extracellular epitope (1:200 in aCSF-HEPES, #ANT-071, Alomone Labs™, Jerusalem, Israel) for 30 min at 4 °C.

    Techniques: FACS, Fluorescence, Immunohistochemistry, Staining, Marker

    Pathway analysis suggests cross-talk between interconnected survival signaling pathways and sarcolemmal sarcoglycans, dystrophin, and archvillin. The gene names of proteins co-immunoprecipitating with or binding to Sgcg as shown here were arranged in the default Organic View using IPA software. Eleven of 13 Top Candidate Sgcg interactors, as well as 3 of 5 Other Candidate interactors (Fig. 3 ), were assigned to either the TP53/ESR2/TRIM25-associated signaling network or to the sarcoglycan, dystrophin, dystroglycan-associated sarcolemmal network. Colors highlight SGCG (magenta), SVIL (yellow), NKCC1/SLC12A2 (green), additional Top Candidate Interactors (blue) and Other Candidate Interactors (gray). Additional genes (white) and direct (solid lines) and indirect (dashed lines) interactions were added by the IPA software. Interactions involving the B-Raf, MEK1/2, and ERK1/2 signaling cascade (orange) with β-dystroglycan/DAG [ 88 ] and SVIL [ 30 ] were added manually

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: Pathway analysis suggests cross-talk between interconnected survival signaling pathways and sarcolemmal sarcoglycans, dystrophin, and archvillin. The gene names of proteins co-immunoprecipitating with or binding to Sgcg as shown here were arranged in the default Organic View using IPA software. Eleven of 13 Top Candidate Sgcg interactors, as well as 3 of 5 Other Candidate interactors (Fig. 3 ), were assigned to either the TP53/ESR2/TRIM25-associated signaling network or to the sarcoglycan, dystrophin, dystroglycan-associated sarcolemmal network. Colors highlight SGCG (magenta), SVIL (yellow), NKCC1/SLC12A2 (green), additional Top Candidate Interactors (blue) and Other Candidate Interactors (gray). Additional genes (white) and direct (solid lines) and indirect (dashed lines) interactions were added by the IPA software. Interactions involving the B-Raf, MEK1/2, and ERK1/2 signaling cascade (orange) with β-dystroglycan/DAG [ 88 ] and SVIL [ 30 ] were added manually

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Binding Assay, Indirect Immunoperoxidase Assay, Software

    HA-CFP-NKCC1-cytoplasmic domains appear to be loosely associated with Flag-tagged SC proteins. RH30 cells were co-transfected in parallel with Flag-tagged sarcoglycans and stained as in Fig. 4 . A HA-CFP-NKCC1-cytoplasmic domains and B HA-CFP (negative control; panels a, a’; blue in merges) were visualized with Flag-tagged sarcoglycans (panels b, b’; red in merges) and F-actin (panels c, c’; green in merges). After pre-extraction with 0.1% Triton X-100, C signal from residual HA-CFP-NKCC1-cytoplasmic domain was indistinguishable from D residual HA-CFP. Overlapping HA and Flag signals in magenta (arrows). Bars (d), 20 μm; bar (d’), 5 μm

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: HA-CFP-NKCC1-cytoplasmic domains appear to be loosely associated with Flag-tagged SC proteins. RH30 cells were co-transfected in parallel with Flag-tagged sarcoglycans and stained as in Fig. 4 . A HA-CFP-NKCC1-cytoplasmic domains and B HA-CFP (negative control; panels a, a’; blue in merges) were visualized with Flag-tagged sarcoglycans (panels b, b’; red in merges) and F-actin (panels c, c’; green in merges). After pre-extraction with 0.1% Triton X-100, C signal from residual HA-CFP-NKCC1-cytoplasmic domain was indistinguishable from D residual HA-CFP. Overlapping HA and Flag signals in magenta (arrows). Bars (d), 20 μm; bar (d’), 5 μm

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Transfection, Staining, Negative Control

    Effects of NKCC1 inhibition on muscle force generation and ERK phosphorylation. A Isometric tetanic force generation of EDL muscles is not altered by bumetanide (BUM) incubation, as compared with vehicle (VEH) control. Raw values showing forces in Ringer’s solution as pre-treatment (Pre-Tx), and the forces following 20–30-min incubation in 50 μM bumetanide or vehicle (ethanol) as post-treatment (Post-Tx). B Decrement of force following eccentric contractions (ECC) is not affected by bumetanide incubation. Forces are relative to the initial force in the first ECC. Means shown; error bars SEM. C levels of phosphorylated ERK are elevated in resting EDL muscles from wild-type mice, but the P-ERK response to ECC is unaffected. (*, P

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: Effects of NKCC1 inhibition on muscle force generation and ERK phosphorylation. A Isometric tetanic force generation of EDL muscles is not altered by bumetanide (BUM) incubation, as compared with vehicle (VEH) control. Raw values showing forces in Ringer’s solution as pre-treatment (Pre-Tx), and the forces following 20–30-min incubation in 50 μM bumetanide or vehicle (ethanol) as post-treatment (Post-Tx). B Decrement of force following eccentric contractions (ECC) is not affected by bumetanide incubation. Forces are relative to the initial force in the first ECC. Means shown; error bars SEM. C levels of phosphorylated ERK are elevated in resting EDL muscles from wild-type mice, but the P-ERK response to ECC is unaffected. (*, P

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Inhibition, Incubation, Mouse Assay

    Flag-tagged Sgcg directly or indirectly associates with HA-CFP-tagged NKCC1 proteins. A Immunoblot of the most successful co-IP, showing more Sgcg-Flag sedimenting with the NKCC1 and NKCC1-cyto (bound), compared to the HA-CFP negative control; corresponding decreases were observed in supernatants after sedimentation (Unbound). Sgcg-Flag amounts in cell lysates also are shown (Input). Flag-tagged Sgcg, Sgcb, and Sgcd proteins were co-expressed with either HA-CFP-NKCC1 (lane 1), HA-CFP (lane 2), or HA-CFP-NKCC1 cytoplasmic domains (NKCC1-cyto, lane 3) in RH-30 cells and immunoprecipitated with anti-HA. Bound NKCC1 proteins were visualized with anti-HA (asterisks); bead-bound rabbit anti-HA heavy chain (IgG). B Densitometric quantification of Unbound/Input ratios of Sgcg-Flag from supernatant-depletion assays, such as those shown in C , and analysis by one-way ANOVA with Tukey’s multiple comparisons test. P values for the mean differences between HA-CFP control and HA-CFP-NKCC1 and HA-CFP-NKCC1-cyto were 0.12 and 0.02, respectively (* P

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: Flag-tagged Sgcg directly or indirectly associates with HA-CFP-tagged NKCC1 proteins. A Immunoblot of the most successful co-IP, showing more Sgcg-Flag sedimenting with the NKCC1 and NKCC1-cyto (bound), compared to the HA-CFP negative control; corresponding decreases were observed in supernatants after sedimentation (Unbound). Sgcg-Flag amounts in cell lysates also are shown (Input). Flag-tagged Sgcg, Sgcb, and Sgcd proteins were co-expressed with either HA-CFP-NKCC1 (lane 1), HA-CFP (lane 2), or HA-CFP-NKCC1 cytoplasmic domains (NKCC1-cyto, lane 3) in RH-30 cells and immunoprecipitated with anti-HA. Bound NKCC1 proteins were visualized with anti-HA (asterisks); bead-bound rabbit anti-HA heavy chain (IgG). B Densitometric quantification of Unbound/Input ratios of Sgcg-Flag from supernatant-depletion assays, such as those shown in C , and analysis by one-way ANOVA with Tukey’s multiple comparisons test. P values for the mean differences between HA-CFP control and HA-CFP-NKCC1 and HA-CFP-NKCC1-cyto were 0.12 and 0.02, respectively (* P

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Co-Immunoprecipitation Assay, Negative Control, Sedimentation, Immunoprecipitation

    Confocal microscopy of NKCC1 and dystrophin in EDL muscles from WT and Sgcg − / − mice. A – H Cross sections show overlapping signals at the sarcolemma (arrowheads; yellow in merges), as well as internal myofibrillar NKCC1 staining in both genotypes. I – P In longitudinal sections, the internal staining suggests an association with T-tubules, which end at dystrophin-associated costameres in the sarcolemma [ 8 , 9 , 82 ]. I’ – L’ Enlargements of the area boxed in L . Q – T Sections stained with only secondary antibodies. Bars are A – H 50 μm; I – T 20 μm; I’ – L’ 5 μm

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: Confocal microscopy of NKCC1 and dystrophin in EDL muscles from WT and Sgcg − / − mice. A – H Cross sections show overlapping signals at the sarcolemma (arrowheads; yellow in merges), as well as internal myofibrillar NKCC1 staining in both genotypes. I – P In longitudinal sections, the internal staining suggests an association with T-tubules, which end at dystrophin-associated costameres in the sarcolemma [ 8 , 9 , 82 ]. I’ – L’ Enlargements of the area boxed in L . Q – T Sections stained with only secondary antibodies. Bars are A – H 50 μm; I – T 20 μm; I’ – L’ 5 μm

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Confocal Microscopy, Mouse Assay, Staining

    NKCC1 co-localizes with the sarcoglycan complex in large, detergent-stable vesicular structures. A , B HA-CFP-tagged NKCC1 (panels a, a’, blue in merges) co-localizes in punctae visualized with both A our affinity-purified anti-Sgcg and B anti-Sgcg from Proteintech Group (PTG) (panels b, b’, red in merges) after expression in RH30 rhabdomyosarcoma cells with Flag-tagged Sgcg, Sgcd, and Sgcb. Enlargements shown (a’–d’) of the boxed areas in panels a–d. C Specificity control with nonimmune rabbit (Rb) IgG substituted for anti-Sgcg. D Signal overlaps of HA-CFP-NKCC1 (panels a, a’, blue in merges) and the sarcoglycan complex (panels a, a’, red in merges) persist even when cells are briefly extracted with 0.1% Triton X-100 before fixation. E The HA-CFP tag alone (panel a, blue in merge) does not persist in pre-extracted RH30 cells co-transfected with Flag-tagged Sgcg, Sgcd, and Sgcb (panel a, red in merge). A – E Phalloidin-stained actin filaments delineate cell boundaries (panels c, c’, green in merges). Bars (d), 20 μm; bars (d’), 5 μm. Overlapping HA and Flag signals in magenta (arrows)

    Journal: Skeletal Muscle

    Article Title: Novel γ-sarcoglycan interactors in murine muscle membranes

    doi: 10.1186/s13395-021-00285-2

    Figure Lengend Snippet: NKCC1 co-localizes with the sarcoglycan complex in large, detergent-stable vesicular structures. A , B HA-CFP-tagged NKCC1 (panels a, a’, blue in merges) co-localizes in punctae visualized with both A our affinity-purified anti-Sgcg and B anti-Sgcg from Proteintech Group (PTG) (panels b, b’, red in merges) after expression in RH30 rhabdomyosarcoma cells with Flag-tagged Sgcg, Sgcd, and Sgcb. Enlargements shown (a’–d’) of the boxed areas in panels a–d. C Specificity control with nonimmune rabbit (Rb) IgG substituted for anti-Sgcg. D Signal overlaps of HA-CFP-NKCC1 (panels a, a’, blue in merges) and the sarcoglycan complex (panels a, a’, red in merges) persist even when cells are briefly extracted with 0.1% Triton X-100 before fixation. E The HA-CFP tag alone (panel a, blue in merge) does not persist in pre-extracted RH30 cells co-transfected with Flag-tagged Sgcg, Sgcd, and Sgcb (panel a, red in merge). A – E Phalloidin-stained actin filaments delineate cell boundaries (panels c, c’, green in merges). Bars (d), 20 μm; bars (d’), 5 μm. Overlapping HA and Flag signals in magenta (arrows)

    Article Snippet: Anti-NKCC1 antibodies were from (A, B) Alomone Labs, #ANT-071 and (C, D) Proteintech Group, #13884-1-AP.

    Techniques: Affinity Purification, Expressing, Transfection, Staining