polyclonal antibody  (Alomone Labs)


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    Alomone Labs polyclonal antibody
    Expression of SERT, TPH1 and 5-HT in 3 independent tumors from the MMTV-Neu transgenic strain ( A ) Independent tumor sections were incubated with a <t>polyclonal</t> antibody to SERT without or with a blocking peptide, the antigen used to elicit antibody production in rabbits. ( B ) Independent tumor sections were incubated with an antibody to TPH1. ( C ) Independent tumor sections stained with an antibody that specifically binds to 5-HT. Primary antibodies to SERT (red), TPH1 (red) and 5-HT (green) were used in combination with fluor-labeled secondary antibodies as described in Materials and Methods. The scale bar represents 50 micrometers (μm).
    Polyclonal Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Serotonin transporter antagonists target tumor-initiating cells in a transgenic mouse model of breast cancer"

    Article Title: Serotonin transporter antagonists target tumor-initiating cells in a transgenic mouse model of breast cancer

    Journal: Oncotarget

    doi: 10.18632/oncotarget.10614

    Expression of SERT, TPH1 and 5-HT in 3 independent tumors from the MMTV-Neu transgenic strain ( A ) Independent tumor sections were incubated with a polyclonal antibody to SERT without or with a blocking peptide, the antigen used to elicit antibody production in rabbits. ( B ) Independent tumor sections were incubated with an antibody to TPH1. ( C ) Independent tumor sections stained with an antibody that specifically binds to 5-HT. Primary antibodies to SERT (red), TPH1 (red) and 5-HT (green) were used in combination with fluor-labeled secondary antibodies as described in Materials and Methods. The scale bar represents 50 micrometers (μm).
    Figure Legend Snippet: Expression of SERT, TPH1 and 5-HT in 3 independent tumors from the MMTV-Neu transgenic strain ( A ) Independent tumor sections were incubated with a polyclonal antibody to SERT without or with a blocking peptide, the antigen used to elicit antibody production in rabbits. ( B ) Independent tumor sections were incubated with an antibody to TPH1. ( C ) Independent tumor sections stained with an antibody that specifically binds to 5-HT. Primary antibodies to SERT (red), TPH1 (red) and 5-HT (green) were used in combination with fluor-labeled secondary antibodies as described in Materials and Methods. The scale bar represents 50 micrometers (μm).

    Techniques Used: Expressing, Transgenic Assay, Incubation, Blocking Assay, Staining, Labeling

    2) Product Images from "Serotonergic system antagonists target breast tumor initiating cells and synergize with chemotherapy to shrink human breast tumor xenografts"

    Article Title: Serotonergic system antagonists target breast tumor initiating cells and synergize with chemotherapy to shrink human breast tumor xenografts

    Journal: Oncotarget

    doi: 10.18632/oncotarget.16646

    SERT is expressed in breast tumor cell lines representative of all the molecular subtypes of breast cancer Western blot performed with breast tumor cell line lysates (35 μg) and mouse brain tissue after electrophoresis in 5-15% gradient polyacrylamide gels reveal that the rabbit polyclonal antibody identifies SERT species that migrate between molecular mass markers of 63 kDa and 75 kDa, and between 48 kDa and 63 kDa. The arrowheads identify the glycosylated and non-glycosylated SERT species. Non-glycosylated SERT co-migrated with α-tubulin, the loading control, which is shown in the bottom-most panel.
    Figure Legend Snippet: SERT is expressed in breast tumor cell lines representative of all the molecular subtypes of breast cancer Western blot performed with breast tumor cell line lysates (35 μg) and mouse brain tissue after electrophoresis in 5-15% gradient polyacrylamide gels reveal that the rabbit polyclonal antibody identifies SERT species that migrate between molecular mass markers of 63 kDa and 75 kDa, and between 48 kDa and 63 kDa. The arrowheads identify the glycosylated and non-glycosylated SERT species. Non-glycosylated SERT co-migrated with α-tubulin, the loading control, which is shown in the bottom-most panel.

    Techniques Used: Western Blot, Electrophoresis

    Patient-derived breast tumor xenografts recapitulate the phenotypic heterogeneity of the primary tumor from which they were derived and express SERT (a) Six primary human breast tumor samples and companion xenografts (b) were stained with H E to reveal their histology. (c) SERT expression was detected by IHC in the PDX sections with the SERT-selective rabbit polyclonal antibody. The arrows identify tumor cells that express higher levels of SERT than the majority of the SERT-positive tumor cells in the same field. The scale bars represent 50 μm.
    Figure Legend Snippet: Patient-derived breast tumor xenografts recapitulate the phenotypic heterogeneity of the primary tumor from which they were derived and express SERT (a) Six primary human breast tumor samples and companion xenografts (b) were stained with H E to reveal their histology. (c) SERT expression was detected by IHC in the PDX sections with the SERT-selective rabbit polyclonal antibody. The arrows identify tumor cells that express higher levels of SERT than the majority of the SERT-positive tumor cells in the same field. The scale bars represent 50 μm.

    Techniques Used: Derivative Assay, Staining, Expressing, Immunohistochemistry

    3) Product Images from "Extrasynaptic Localization of Inactivating Calcium-Activated Potassium Channels in Mouse Inner Hair Cells"

    Article Title: Extrasynaptic Localization of Inactivating Calcium-Activated Potassium Channels in Mouse Inner Hair Cells

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.3162-04.2004

    Electrophysiology and antibody staining reveal a corresponding developmental increase in BK current and BK channel immunoreactivity. BK currents in response to depolarizations from -60 to 40 mV in 10 mV steps were isolated from recordings from mice IHCs of various ages as described in Materials and Methods. A , Little BK current is detected from IHCs from mice before the onset of hearing (P10), whereas the peak BK current increases in IHCs from mice after the onset of hearing (P14) and further increases in IHCs from mice with mature hearing (P20). C , The maximum BK current detected at each command potential is compared for the three developmental time points. B , Similarly, immunostaining with a polyclonal BK channel antibody shows little immunoreactivity in IHCs from P10 mice with increasing immunoreactivity just after the onset (P14) to the maturation (P20) of hearing. D , Comparison of the peak BK currents detected at 40 mV to the number of immunofluorescent puncta per field of view normalized to their respective values for P20 samples shows that the assessments of the developmental acquisition of the BK channel by both electrophysiology and immunoreactivity are comparable.
    Figure Legend Snippet: Electrophysiology and antibody staining reveal a corresponding developmental increase in BK current and BK channel immunoreactivity. BK currents in response to depolarizations from -60 to 40 mV in 10 mV steps were isolated from recordings from mice IHCs of various ages as described in Materials and Methods. A , Little BK current is detected from IHCs from mice before the onset of hearing (P10), whereas the peak BK current increases in IHCs from mice after the onset of hearing (P14) and further increases in IHCs from mice with mature hearing (P20). C , The maximum BK current detected at each command potential is compared for the three developmental time points. B , Similarly, immunostaining with a polyclonal BK channel antibody shows little immunoreactivity in IHCs from P10 mice with increasing immunoreactivity just after the onset (P14) to the maturation (P20) of hearing. D , Comparison of the peak BK currents detected at 40 mV to the number of immunofluorescent puncta per field of view normalized to their respective values for P20 samples shows that the assessments of the developmental acquisition of the BK channel by both electrophysiology and immunoreactivity are comparable.

    Techniques Used: Staining, Isolation, Mouse Assay, Immunostaining

    Antibody staining reveals extrasynaptic localization of BK channels near the apex of mIHCs. Three-dimensional reconstructions of immunostained IHCs from P20 mice were generated from stacks of confocal micrographs as described in Materials and Methods. Various angles of rotation are shown for IHCs double immunostained with either a monoclonal calretinin antibody (green), to label IHCs, and a polyclonal BK channel antibody (red; A ) or IHCs triple-immunostained with a polyclonal calretinin antibody (green), monoclonal NF200 antibody (isotype IgG 1 ; cyan), to stain afferent nerve fibers that contact the IHCs, and a monoclonal BK channel antibody (isotype IgG 2A ; red; B ). Reconstructions reveal extrasynaptic localization of BK channels near the apex of mIHCs.
    Figure Legend Snippet: Antibody staining reveals extrasynaptic localization of BK channels near the apex of mIHCs. Three-dimensional reconstructions of immunostained IHCs from P20 mice were generated from stacks of confocal micrographs as described in Materials and Methods. Various angles of rotation are shown for IHCs double immunostained with either a monoclonal calretinin antibody (green), to label IHCs, and a polyclonal BK channel antibody (red; A ) or IHCs triple-immunostained with a polyclonal calretinin antibody (green), monoclonal NF200 antibody (isotype IgG 1 ; cyan), to stain afferent nerve fibers that contact the IHCs, and a monoclonal BK channel antibody (isotype IgG 2A ; red; B ). Reconstructions reveal extrasynaptic localization of BK channels near the apex of mIHCs.

    Techniques Used: Staining, Mouse Assay, Generated

    Antibody staining against the BK channel reveals punctate staining on mIHCs. Intact organs of Corti from P20 mice were immunostained as described in Materials and Methods. A , Immunostaining with a monoclonal calretinin antibody (green) and polyclonal BK channel antibody (red) shows the organization of the hair cells into three rows of outer hair cells and one row of IHCs that additionally shows punctate staining for the BK channel. B , The monoclonal BK channel antibody recognizes the same protein as the polyclonal antibody as evidenced by colocalized immunoreactivity in samples immunostained with both the polyclonal (green) and monoclonal (red) BK channel antibodies. C , Preabsorption of either the polyclonal or monoclonal BK channel antibody abolishes immunoreactivity on the IHCs.
    Figure Legend Snippet: Antibody staining against the BK channel reveals punctate staining on mIHCs. Intact organs of Corti from P20 mice were immunostained as described in Materials and Methods. A , Immunostaining with a monoclonal calretinin antibody (green) and polyclonal BK channel antibody (red) shows the organization of the hair cells into three rows of outer hair cells and one row of IHCs that additionally shows punctate staining for the BK channel. B , The monoclonal BK channel antibody recognizes the same protein as the polyclonal antibody as evidenced by colocalized immunoreactivity in samples immunostained with both the polyclonal (green) and monoclonal (red) BK channel antibodies. C , Preabsorption of either the polyclonal or monoclonal BK channel antibody abolishes immunoreactivity on the IHCs.

    Techniques Used: Staining, Mouse Assay, Immunostaining

    4) Product Images from "Serotonergic system antagonists target breast tumor initiating cells and synergize with chemotherapy to shrink human breast tumor xenografts"

    Article Title: Serotonergic system antagonists target breast tumor initiating cells and synergize with chemotherapy to shrink human breast tumor xenografts

    Journal: Oncotarget

    doi: 10.18632/oncotarget.16646

    SERT is expressed in breast tumor cell lines representative of all the molecular subtypes of breast cancer Western blot performed with breast tumor cell line lysates (35 μg) and mouse brain tissue after electrophoresis in 5-15% gradient polyacrylamide gels reveal that the rabbit polyclonal antibody identifies SERT species that migrate between molecular mass markers of 63 kDa and 75 kDa, and between 48 kDa and 63 kDa. The arrowheads identify the glycosylated and non-glycosylated SERT species. Non-glycosylated SERT co-migrated with α-tubulin, the loading control, which is shown in the bottom-most panel.
    Figure Legend Snippet: SERT is expressed in breast tumor cell lines representative of all the molecular subtypes of breast cancer Western blot performed with breast tumor cell line lysates (35 μg) and mouse brain tissue after electrophoresis in 5-15% gradient polyacrylamide gels reveal that the rabbit polyclonal antibody identifies SERT species that migrate between molecular mass markers of 63 kDa and 75 kDa, and between 48 kDa and 63 kDa. The arrowheads identify the glycosylated and non-glycosylated SERT species. Non-glycosylated SERT co-migrated with α-tubulin, the loading control, which is shown in the bottom-most panel.

    Techniques Used: Western Blot, Electrophoresis

    Patient-derived breast tumor xenografts recapitulate the phenotypic heterogeneity of the primary tumor from which they were derived and express SERT (a) Six primary human breast tumor samples and companion xenografts (b) were stained with H E to reveal their histology. (c) SERT expression was detected by IHC in the PDX sections with the SERT-selective rabbit polyclonal antibody. The arrows identify tumor cells that express higher levels of SERT than the majority of the SERT-positive tumor cells in the same field. The scale bars represent 50 μm.
    Figure Legend Snippet: Patient-derived breast tumor xenografts recapitulate the phenotypic heterogeneity of the primary tumor from which they were derived and express SERT (a) Six primary human breast tumor samples and companion xenografts (b) were stained with H E to reveal their histology. (c) SERT expression was detected by IHC in the PDX sections with the SERT-selective rabbit polyclonal antibody. The arrows identify tumor cells that express higher levels of SERT than the majority of the SERT-positive tumor cells in the same field. The scale bars represent 50 μm.

    Techniques Used: Derivative Assay, Staining, Expressing, Immunohistochemistry

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    • rabbit polyclonal antibody  (Alomone Labs)
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    Alomone Labs rabbit polyclonal antibody
    Immunoprecipitation of DPPX In cultures of dissociated rat hippocampal neurons, patients’ antibodies showed intense reactivity with the neuronal cell surface (A), bar = 10 μm. Immunoprecipitation of the antigen with serum of the index case is shown in B, where the precipitated proteins were run in a gel and subsequently stained with EZblue. Note that patient’s antibodies precipitated a protein (band close to 102 kDa in lane P), which was excised from the gel and analyzed by mass spectrometry, demonstrating sequences of DPPX. Lane N is the precipitate obtained from control serum. Immunoblot of these proteins with a rabbit <t>polyclonal</t> antibody against DPPX (1:1000, developed by BR) confirmed that the band corresponded to DPPX (C).
    Rabbit Polyclonal Antibody, 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
    https://www.bioz.com/result/rabbit polyclonal antibody/product/Alomone Labs
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    trpc5  (Alomone Labs)
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    Alomone Labs trpc5
    Effect of candesartan or telmisartan but not amlodipine on TRPC expression in mesenteric arterioles. Long-term administration of angiotensin AT1 receptor antagonist telmisartan or candesartan, but not of calcium channel blocker amlodipine reduces TRPC1, TRPC3 and <t>TRPC5</t> channel protein expression in vivo. The angiotensin AT1 receptor antagonist telmisartan (5 mg/kg per day) or candesartan (4 mg/kg per day), calcium channel blocker amlodipine (10 mg/kg per day), or placebo were administered to SHR by gavage for 16 weeks. Representative immunoblottings of TRPC channel protein expressions in mesenteric arterioles from treated SHR (Fig. 7A) and summary data are shown (Fig. 7B). * P
    Trpc5, 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
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    hcn2  (Alomone Labs)
    94
    Alomone Labs hcn2
    MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, <t>HCN2</t> and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P
    Hcn2, 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
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    ep2  (Alomone Labs)
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    Alomone Labs ep2
    Chemotaxis and adhesion assays with human blood eosinophils. Eosinophils from healthy donors were incubated with 100 nM of EP4 agonist ONO-AE1-329 or with 100 nM of the EP4 antagonist ONO-AE3-208 ( a ), with 100 and 300 nM of <t>EP2</t> agonist butaprost ( b ), or with 100 nM of DP1 agonist BW245C and 1 µM of DP1 antagonist MK0524 ( c ), and chemotaxis was assessed using esophageal epithelial cell supernatant for chemoattraction. n = 6–12 (for a , and b ) and n = 3 ( c ); values are mean ± SEM; one-way ANOVA; Tukey’s post hoc test. *** p values
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    Image Search Results


    Immunoprecipitation of DPPX In cultures of dissociated rat hippocampal neurons, patients’ antibodies showed intense reactivity with the neuronal cell surface (A), bar = 10 μm. Immunoprecipitation of the antigen with serum of the index case is shown in B, where the precipitated proteins were run in a gel and subsequently stained with EZblue. Note that patient’s antibodies precipitated a protein (band close to 102 kDa in lane P), which was excised from the gel and analyzed by mass spectrometry, demonstrating sequences of DPPX. Lane N is the precipitate obtained from control serum. Immunoblot of these proteins with a rabbit polyclonal antibody against DPPX (1:1000, developed by BR) confirmed that the band corresponded to DPPX (C).

    Journal: Annals of neurology

    Article Title: Encephalitis and antibodies to DPPX, a subunit of Kv4.2 potassium channels

    doi: 10.1002/ana.23756

    Figure Lengend Snippet: Immunoprecipitation of DPPX In cultures of dissociated rat hippocampal neurons, patients’ antibodies showed intense reactivity with the neuronal cell surface (A), bar = 10 μm. Immunoprecipitation of the antigen with serum of the index case is shown in B, where the precipitated proteins were run in a gel and subsequently stained with EZblue. Note that patient’s antibodies precipitated a protein (band close to 102 kDa in lane P), which was excised from the gel and analyzed by mass spectrometry, demonstrating sequences of DPPX. Lane N is the precipitate obtained from control serum. Immunoblot of these proteins with a rabbit polyclonal antibody against DPPX (1:1000, developed by BR) confirmed that the band corresponded to DPPX (C).

    Article Snippet: Similar studies comparing the serum of a healthy individual and the rabbit polyclonal antibody are shown in M and N, and the merged images in O.

    Techniques: Immunoprecipitation, Staining, Mass Spectrometry

    Expression of DPPX in myenteric plexus Transverse section of small bowel of rat showing the longitudinal muscular layer (LM), circular muscular layer (CM), submucosal layer (SM), and glans (G). The myenteric plexus (Plex) is revealed as clusters of large neurons between the two muscular layers. In the 3 panels (A–C) the nuclei of the neurons (red) was labeled with anti-Hu (a highly specific neuronal marker). Panel A, shows in green the DPPX immunostaining using a rabbit polyclonal antibody (1:1000, developed by BD); panel B shows the DPPX reactivity of serum from one of the patients with encephalitis, and panel C shows the lack of reactivity of serum from a healthy subject. Note that DPPX is predominantly expressed in the cytoplasm-membrane of the large clustered neurons of the myenteric plexus, and is also detected in a fine longitudinal pattern in CM and SM where the submucosal plexus is located. Bar = 20μm.

    Journal: Annals of neurology

    Article Title: Encephalitis and antibodies to DPPX, a subunit of Kv4.2 potassium channels

    doi: 10.1002/ana.23756

    Figure Lengend Snippet: Expression of DPPX in myenteric plexus Transverse section of small bowel of rat showing the longitudinal muscular layer (LM), circular muscular layer (CM), submucosal layer (SM), and glans (G). The myenteric plexus (Plex) is revealed as clusters of large neurons between the two muscular layers. In the 3 panels (A–C) the nuclei of the neurons (red) was labeled with anti-Hu (a highly specific neuronal marker). Panel A, shows in green the DPPX immunostaining using a rabbit polyclonal antibody (1:1000, developed by BD); panel B shows the DPPX reactivity of serum from one of the patients with encephalitis, and panel C shows the lack of reactivity of serum from a healthy subject. Note that DPPX is predominantly expressed in the cytoplasm-membrane of the large clustered neurons of the myenteric plexus, and is also detected in a fine longitudinal pattern in CM and SM where the submucosal plexus is located. Bar = 20μm.

    Article Snippet: Similar studies comparing the serum of a healthy individual and the rabbit polyclonal antibody are shown in M and N, and the merged images in O.

    Techniques: Expressing, Labeling, Marker, Immunostaining

    Effect of candesartan or telmisartan but not amlodipine on TRPC expression in mesenteric arterioles. Long-term administration of angiotensin AT1 receptor antagonist telmisartan or candesartan, but not of calcium channel blocker amlodipine reduces TRPC1, TRPC3 and TRPC5 channel protein expression in vivo. The angiotensin AT1 receptor antagonist telmisartan (5 mg/kg per day) or candesartan (4 mg/kg per day), calcium channel blocker amlodipine (10 mg/kg per day), or placebo were administered to SHR by gavage for 16 weeks. Representative immunoblottings of TRPC channel protein expressions in mesenteric arterioles from treated SHR (Fig. 7A) and summary data are shown (Fig. 7B). * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Increased rhythmicity in hypertensive arterial smooth muscle is linked to transient receptor potential canonical channels

    doi: 10.1111/j.1582-4934.2009.00890.x

    Figure Lengend Snippet: Effect of candesartan or telmisartan but not amlodipine on TRPC expression in mesenteric arterioles. Long-term administration of angiotensin AT1 receptor antagonist telmisartan or candesartan, but not of calcium channel blocker amlodipine reduces TRPC1, TRPC3 and TRPC5 channel protein expression in vivo. The angiotensin AT1 receptor antagonist telmisartan (5 mg/kg per day) or candesartan (4 mg/kg per day), calcium channel blocker amlodipine (10 mg/kg per day), or placebo were administered to SHR by gavage for 16 weeks. Representative immunoblottings of TRPC channel protein expressions in mesenteric arterioles from treated SHR (Fig. 7A) and summary data are shown (Fig. 7B). * P

    Article Snippet: The membranes were incubated with primary rabbit antibodies against TRPC1, TRPC3, TRPC4, TRPC5 and TRPC6 (1:200; Alomone Labs), followed by incubation with goat anti-rabbit horseradish peroxidase-conjugated secondary antibody.

    Techniques: Expressing, In Vivo

    Inhibition of norepinephrine-induced vasomotion in mesenteric arterioles from SHR by specific anti-TRPC antibodies Representative tracings of norepinephrine-induced vasomotion in mesenteric arterioles from SHR under control conditions (A), in the presence of anti-TRPC1 antibodies (B), anti-TRPC3 antibodies (C), anti-TRPC3 antibodies with antigenic peptide (D), anti-TRPC5 antibodies (E), anti-TRPC1 plus anti-TRPC3 antibodies (F) or in the presence of anti-β-actin antibodies (G). Representative tracings of norepinephrine-induced vasomotion in mesenteric arterioles from SHR under control conditions after short-term exposure to hypotonic 0.45% NaCl without antibody (H), or after short-term exposure to hypotonic 0.45% NaCl plus TRPC3 antibody (I). Summary data (J) show that inhibition of TRPC channels by specific anti-TRPC antibodies significantly attenuates norepinephrine-induced vasomotion in SHR. Data are mean ± S.E.M. of n = 6 independent experiments. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Increased rhythmicity in hypertensive arterial smooth muscle is linked to transient receptor potential canonical channels

    doi: 10.1111/j.1582-4934.2009.00890.x

    Figure Lengend Snippet: Inhibition of norepinephrine-induced vasomotion in mesenteric arterioles from SHR by specific anti-TRPC antibodies Representative tracings of norepinephrine-induced vasomotion in mesenteric arterioles from SHR under control conditions (A), in the presence of anti-TRPC1 antibodies (B), anti-TRPC3 antibodies (C), anti-TRPC3 antibodies with antigenic peptide (D), anti-TRPC5 antibodies (E), anti-TRPC1 plus anti-TRPC3 antibodies (F) or in the presence of anti-β-actin antibodies (G). Representative tracings of norepinephrine-induced vasomotion in mesenteric arterioles from SHR under control conditions after short-term exposure to hypotonic 0.45% NaCl without antibody (H), or after short-term exposure to hypotonic 0.45% NaCl plus TRPC3 antibody (I). Summary data (J) show that inhibition of TRPC channels by specific anti-TRPC antibodies significantly attenuates norepinephrine-induced vasomotion in SHR. Data are mean ± S.E.M. of n = 6 independent experiments. * P

    Article Snippet: The membranes were incubated with primary rabbit antibodies against TRPC1, TRPC3, TRPC4, TRPC5 and TRPC6 (1:200; Alomone Labs), followed by incubation with goat anti-rabbit horseradish peroxidase-conjugated secondary antibody.

    Techniques: Inhibition

    Expression of TRPC1, TRPC3 and TRPC5 channels in mesenteric arterioles from SHR. Representative immunoblottings (A) and summary data (B) of TRPC1, TRPC3, TRPC4, TRPC5,TRPC6 channels and TRPC3 antibody with its respective antigenic peptide the protein expression in mesenteric arterioles from WKY (open bars) and SHR (filled bars). Data are mean ± S.E.M. of n = 4 independent experiments. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Increased rhythmicity in hypertensive arterial smooth muscle is linked to transient receptor potential canonical channels

    doi: 10.1111/j.1582-4934.2009.00890.x

    Figure Lengend Snippet: Expression of TRPC1, TRPC3 and TRPC5 channels in mesenteric arterioles from SHR. Representative immunoblottings (A) and summary data (B) of TRPC1, TRPC3, TRPC4, TRPC5,TRPC6 channels and TRPC3 antibody with its respective antigenic peptide the protein expression in mesenteric arterioles from WKY (open bars) and SHR (filled bars). Data are mean ± S.E.M. of n = 4 independent experiments. * P

    Article Snippet: The membranes were incubated with primary rabbit antibodies against TRPC1, TRPC3, TRPC4, TRPC5 and TRPC6 (1:200; Alomone Labs), followed by incubation with goat anti-rabbit horseradish peroxidase-conjugated secondary antibody.

    Techniques: Expressing

    Inhibition of norepinephrine-induced calcium increase in mesenteric arterioles from SHR by specific anti-TRPC antibodies. Representative tracings of norepinephrine-induced calcium increase in mesenteric arterioles from SHR under control conditions and in the presence of anti-TRPC1 antibodies (A), anti-TRPC3 antibodies (B), anti-TRPC5 antibodies (C), anti-TRPC1 plus anti-TRPC3 plus anti-TRPC5 antibodies (D), anti-TRPC3 antibodies plus TRPC3 antigenic peptide (E) or anti-β-actin antibodies (F). Summary data (G) shows the effects of specific anti-TRPC antibodies on norepinephrine-induced calcium influx in mesenteric arterioles from SHR. Data are mean ± S.E.M. of n = 8 independent experiments. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Increased rhythmicity in hypertensive arterial smooth muscle is linked to transient receptor potential canonical channels

    doi: 10.1111/j.1582-4934.2009.00890.x

    Figure Lengend Snippet: Inhibition of norepinephrine-induced calcium increase in mesenteric arterioles from SHR by specific anti-TRPC antibodies. Representative tracings of norepinephrine-induced calcium increase in mesenteric arterioles from SHR under control conditions and in the presence of anti-TRPC1 antibodies (A), anti-TRPC3 antibodies (B), anti-TRPC5 antibodies (C), anti-TRPC1 plus anti-TRPC3 plus anti-TRPC5 antibodies (D), anti-TRPC3 antibodies plus TRPC3 antigenic peptide (E) or anti-β-actin antibodies (F). Summary data (G) shows the effects of specific anti-TRPC antibodies on norepinephrine-induced calcium influx in mesenteric arterioles from SHR. Data are mean ± S.E.M. of n = 8 independent experiments. * P

    Article Snippet: The membranes were incubated with primary rabbit antibodies against TRPC1, TRPC3, TRPC4, TRPC5 and TRPC6 (1:200; Alomone Labs), followed by incubation with goat anti-rabbit horseradish peroxidase-conjugated secondary antibody.

    Techniques: Inhibition

    MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, HCN2 and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P

    Journal: Nucleic Acids Research

    Article Title: A single anti-microRNA antisense oligodeoxyribonucleotide (AMO) targeting multiple microRNAs offers an improved approach for microRNA interference

    doi: 10.1093/nar/gkn1053

    Figure Lengend Snippet: MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, HCN2 and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P

    Article Snippet: The sample was incubated overnight at 4°C with primary antibodies for TGFBI, APC and BCL2L11 (Santa Cruz), and for HCN2 and Cav1.2 (Alomone Labs).

    Techniques: Western Blot, Cell Culture, Negative Control

    Chemotaxis and adhesion assays with human blood eosinophils. Eosinophils from healthy donors were incubated with 100 nM of EP4 agonist ONO-AE1-329 or with 100 nM of the EP4 antagonist ONO-AE3-208 ( a ), with 100 and 300 nM of EP2 agonist butaprost ( b ), or with 100 nM of DP1 agonist BW245C and 1 µM of DP1 antagonist MK0524 ( c ), and chemotaxis was assessed using esophageal epithelial cell supernatant for chemoattraction. n = 6–12 (for a , and b ) and n = 3 ( c ); values are mean ± SEM; one-way ANOVA; Tukey’s post hoc test. *** p values

    Journal: Digestive Diseases and Sciences

    Article Title: Involvement of EP2 and EP4 Receptors in Eosinophilic Esophagitis: A Pilot Study

    doi: 10.1007/s10620-019-05623-5

    Figure Lengend Snippet: Chemotaxis and adhesion assays with human blood eosinophils. Eosinophils from healthy donors were incubated with 100 nM of EP4 agonist ONO-AE1-329 or with 100 nM of the EP4 antagonist ONO-AE3-208 ( a ), with 100 and 300 nM of EP2 agonist butaprost ( b ), or with 100 nM of DP1 agonist BW245C and 1 µM of DP1 antagonist MK0524 ( c ), and chemotaxis was assessed using esophageal epithelial cell supernatant for chemoattraction. n = 6–12 (for a , and b ) and n = 3 ( c ); values are mean ± SEM; one-way ANOVA; Tukey’s post hoc test. *** p values

    Article Snippet: For flow cytometric visualization of the EP receptors, cells were incubated with rabbit polyclonal antibodies against EP1, EP2, and EP3 (20 μg/ml; Alomone Labs, Jerusalem, Israel) and mouse polyclonal antibody against EP4 (20 μg/ml; Alomone Labs, Jerusalem, Israel), or normal rabbit or mouse IgG (20 μg/ml; Santa Cruz Biotechnology, Dallas, TX, USA) for 30 min at 4 °C.

    Techniques: Chemotaxis Assay, Incubation

    Immunohistochemistry shows strong DP1 staining in eosinophils ( a , arrows ), while epithelial cells in esophageal mucosal biopsies are practically devoid of staining. EP4 ( b ) and EP2 ( c ) immunostaining is prominent in eosinophils ( arrows ) but also visible in epithelial cells ( arrowheads ). 3-3′-Diaminobenzidine (DAB) was used as visualization substrate for DP1 and EP4 staining (brown precipitates), while for EP2, ImmPact™ NovaRED substrate was used (red precipitate). Calibration bar: 50 µm

    Journal: Digestive Diseases and Sciences

    Article Title: Involvement of EP2 and EP4 Receptors in Eosinophilic Esophagitis: A Pilot Study

    doi: 10.1007/s10620-019-05623-5

    Figure Lengend Snippet: Immunohistochemistry shows strong DP1 staining in eosinophils ( a , arrows ), while epithelial cells in esophageal mucosal biopsies are practically devoid of staining. EP4 ( b ) and EP2 ( c ) immunostaining is prominent in eosinophils ( arrows ) but also visible in epithelial cells ( arrowheads ). 3-3′-Diaminobenzidine (DAB) was used as visualization substrate for DP1 and EP4 staining (brown precipitates), while for EP2, ImmPact™ NovaRED substrate was used (red precipitate). Calibration bar: 50 µm

    Article Snippet: For flow cytometric visualization of the EP receptors, cells were incubated with rabbit polyclonal antibodies against EP1, EP2, and EP3 (20 μg/ml; Alomone Labs, Jerusalem, Israel) and mouse polyclonal antibody against EP4 (20 μg/ml; Alomone Labs, Jerusalem, Israel), or normal rabbit or mouse IgG (20 μg/ml; Santa Cruz Biotechnology, Dallas, TX, USA) for 30 min at 4 °C.

    Techniques: Immunohistochemistry, Staining, Immunostaining

    Flow cytometric evaluation of EP (EP1–4) and DP (DP1, DP2) receptor expression in human blood eosinophils. Changes in receptor expression were recorded as mean fluorescence intensity and data are expressed as fold increase in fluorescence over isotype control. Expression levels of EP2 and EP4 are significantly lower in patients with eosinophilic esophagitis (EoE) compared to healthy control subjects (control). Expression levels of EP1, EP3, DP1, and DP2 do not differ between EoE and controls. Values are mean ± SEM; Student’s t test; n = 6–7. * p

    Journal: Digestive Diseases and Sciences

    Article Title: Involvement of EP2 and EP4 Receptors in Eosinophilic Esophagitis: A Pilot Study

    doi: 10.1007/s10620-019-05623-5

    Figure Lengend Snippet: Flow cytometric evaluation of EP (EP1–4) and DP (DP1, DP2) receptor expression in human blood eosinophils. Changes in receptor expression were recorded as mean fluorescence intensity and data are expressed as fold increase in fluorescence over isotype control. Expression levels of EP2 and EP4 are significantly lower in patients with eosinophilic esophagitis (EoE) compared to healthy control subjects (control). Expression levels of EP1, EP3, DP1, and DP2 do not differ between EoE and controls. Values are mean ± SEM; Student’s t test; n = 6–7. * p

    Article Snippet: For flow cytometric visualization of the EP receptors, cells were incubated with rabbit polyclonal antibodies against EP1, EP2, and EP3 (20 μg/ml; Alomone Labs, Jerusalem, Israel) and mouse polyclonal antibody against EP4 (20 μg/ml; Alomone Labs, Jerusalem, Israel), or normal rabbit or mouse IgG (20 μg/ml; Santa Cruz Biotechnology, Dallas, TX, USA) for 30 min at 4 °C.

    Techniques: Expressing, Fluorescence

    ECIS ® cell impedance assays were performed in esophageal epithelial cells with 10 and 300 nM of EP4 agonist ONO-AE1-329 ( a ) and EP2 agonist butaprost ( b ) (or medium as control). The decrease in resistance correlates with a loss in the monolayer’s integrity indicative of cell barrier decrease. n = 5–9; values are mean ± SEM; one-way-ANOVA; Tukey’s post hoc test; * p

    Journal: Digestive Diseases and Sciences

    Article Title: Involvement of EP2 and EP4 Receptors in Eosinophilic Esophagitis: A Pilot Study

    doi: 10.1007/s10620-019-05623-5

    Figure Lengend Snippet: ECIS ® cell impedance assays were performed in esophageal epithelial cells with 10 and 300 nM of EP4 agonist ONO-AE1-329 ( a ) and EP2 agonist butaprost ( b ) (or medium as control). The decrease in resistance correlates with a loss in the monolayer’s integrity indicative of cell barrier decrease. n = 5–9; values are mean ± SEM; one-way-ANOVA; Tukey’s post hoc test; * p

    Article Snippet: For flow cytometric visualization of the EP receptors, cells were incubated with rabbit polyclonal antibodies against EP1, EP2, and EP3 (20 μg/ml; Alomone Labs, Jerusalem, Israel) and mouse polyclonal antibody against EP4 (20 μg/ml; Alomone Labs, Jerusalem, Israel), or normal rabbit or mouse IgG (20 μg/ml; Santa Cruz Biotechnology, Dallas, TX, USA) for 30 min at 4 °C.

    Techniques: Electric Cell-substrate Impedance Sensing