ngf  (Alomone Labs)


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    Structured Review

    Alomone Labs ngf
    Ngf, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ngf/product/Alomone Labs
    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    ngf - by Bioz Stars, 2022-08
    94/100 stars

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    Alomone Labs nerve growth factor ngf
    <t>BDNF-induced</t> NR2C upregulation by TrkB activation. Cells were cultured in low KCl and treated with or without BDNF (100 ng/ml in A and 50 ng/ml in B-D and F ) for 96 h. A , Levels of indicated mRNAs were quantitated by RNA blotting ( n = 4). B , Cell lysates (40 μg) were immunoblotted with anti-panNR2 antibody or anti-NR1 antibody. Molecular sizes (kilodaltons) of protein makers are indicated on the left. C , P2 membrane fractions were isolated, solubilized, and immunoprecipitated (IP) with anti-NR1 antibody, followed by immnoblotting with anti-panNR2 antibody. D , Cell-surface proteins were biotinylated with Sulfo-NHS-SS-Biotin. Cell lysates were solubilized, precipitated with NeutrAvidin beads, and immunoblotted with anti-panNR2 antibody. E , Cells were cultured in low KCl and treated with BDNF, <t>NGF,</t> NT-3, or NT-4 (50 ng/ml each) for 96 h. Levels of NR2C mRNA were quantitated ( n = 4). F , Granule cells were prepared from TrkB - / - knock-out mice(KO) and their wild-type (WT) littermates. NR2C and TrkB mRNAs were analyzed by RNA blotting. Ethidium bromide-stained 18s rRNA is also indicated. * p
    Nerve Growth Factor Ngf, 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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    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    97
    Alomone Labs n m bdnf pro domain
    Differential binding of <t>pro-BDNF</t> and neurotension to sortilin and pro-sortilin. A , SPR analysis showing that unprocessed pro-BDNF (50 <t>n</t> m ) binds nearly as efficiently to the receptor in the presence (pro-sortilin) as in the absence (sortilin) of the receptor
    N M Bdnf Pro Domain, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n m bdnf pro domain/product/Alomone Labs
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    n m bdnf pro domain - by Bioz Stars, 2022-08
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    BDNF-induced NR2C upregulation by TrkB activation. Cells were cultured in low KCl and treated with or without BDNF (100 ng/ml in A and 50 ng/ml in B-D and F ) for 96 h. A , Levels of indicated mRNAs were quantitated by RNA blotting ( n = 4). B , Cell lysates (40 μg) were immunoblotted with anti-panNR2 antibody or anti-NR1 antibody. Molecular sizes (kilodaltons) of protein makers are indicated on the left. C , P2 membrane fractions were isolated, solubilized, and immunoprecipitated (IP) with anti-NR1 antibody, followed by immnoblotting with anti-panNR2 antibody. D , Cell-surface proteins were biotinylated with Sulfo-NHS-SS-Biotin. Cell lysates were solubilized, precipitated with NeutrAvidin beads, and immunoblotted with anti-panNR2 antibody. E , Cells were cultured in low KCl and treated with BDNF, NGF, NT-3, or NT-4 (50 ng/ml each) for 96 h. Levels of NR2C mRNA were quantitated ( n = 4). F , Granule cells were prepared from TrkB - / - knock-out mice(KO) and their wild-type (WT) littermates. NR2C and TrkB mRNAs were analyzed by RNA blotting. Ethidium bromide-stained 18s rRNA is also indicated. * p

    Journal: The Journal of Neuroscience

    Article Title: Neuronal Depolarization Controls Brain-Derived Neurotrophic Factor-Induced Upregulation of NR2C NMDA Receptor via Calcineurin Signaling

    doi: 10.1523/JNEUROSCI.2191-05.2005

    Figure Lengend Snippet: BDNF-induced NR2C upregulation by TrkB activation. Cells were cultured in low KCl and treated with or without BDNF (100 ng/ml in A and 50 ng/ml in B-D and F ) for 96 h. A , Levels of indicated mRNAs were quantitated by RNA blotting ( n = 4). B , Cell lysates (40 μg) were immunoblotted with anti-panNR2 antibody or anti-NR1 antibody. Molecular sizes (kilodaltons) of protein makers are indicated on the left. C , P2 membrane fractions were isolated, solubilized, and immunoprecipitated (IP) with anti-NR1 antibody, followed by immnoblotting with anti-panNR2 antibody. D , Cell-surface proteins were biotinylated with Sulfo-NHS-SS-Biotin. Cell lysates were solubilized, precipitated with NeutrAvidin beads, and immunoblotted with anti-panNR2 antibody. E , Cells were cultured in low KCl and treated with BDNF, NGF, NT-3, or NT-4 (50 ng/ml each) for 96 h. Levels of NR2C mRNA were quantitated ( n = 4). F , Granule cells were prepared from TrkB - / - knock-out mice(KO) and their wild-type (WT) littermates. NR2C and TrkB mRNAs were analyzed by RNA blotting. Ethidium bromide-stained 18s rRNA is also indicated. * p

    Article Snippet: Slices were treated with or without 1 μ m FK506 for 96 h, and 0.5 vol of the culture medium was changed every 2 d. Reagents and inhibitors were purchased from the following sources: BDNF (Peprotech, London, UK); neurotrophin-3 (NT-3), NT-4, and nerve growth factor (NGF) (Alomone Laboratories, Jerusalem, Israel); neuregulin-β (NeoMarkers, Fremont, CA); nifedipine (Nacalai Tesque, Kyoto, Japan); KN62 (Tocris, Bristol, UK); and U0126, SB203580, FK506, K252a, , PD98059, cyclosporin A, rapamycin, and bisindolylmaleimide I (Calbiochem, San Diego, CA).

    Techniques: Activation Assay, Cell Culture, Isolation, Immunoprecipitation, Knock-Out, Mouse Assay, Staining

    Electrical stimulation based bFGF release and bioactivity assay (A) bFGF release profile during sequential electrical stimulation (200 mV/mm, 1Hz, 5 min) and incubation (5 min) periods (B) Bioactivity of released bFGF complexes compared to recombinant human bFGF, biotinylated bFGF, and control groups with no growth factor based on BALB/c cell proliferation (* p

    Journal: Frontiers in Chemistry

    Article Title: Electrically Stimulated Tunable Drug Delivery From Polypyrrole-Coated Polyvinylidene Fluoride

    doi: 10.3389/fchem.2021.599631

    Figure Lengend Snippet: Electrical stimulation based bFGF release and bioactivity assay (A) bFGF release profile during sequential electrical stimulation (200 mV/mm, 1Hz, 5 min) and incubation (5 min) periods (B) Bioactivity of released bFGF complexes compared to recombinant human bFGF, biotinylated bFGF, and control groups with no growth factor based on BALB/c cell proliferation (* p

    Article Snippet: A similar procedure was used for loading a solution of biotinylated Nerve Growth Factor (NGF, Alomone Labs, Jerusalem, Israel) at a concentration of 120 ng/ml in deionized water into a different group of PPy-coated PVDF fibers. illustrates the final schematic of the chemical structure of drug carrier platform containing streptavidin conjugated to biotinylated growth factor and anchored to the biotin incorporated within the PPy coating on the PVDF fibers.

    Techniques: Incubation, Recombinant

    Schematic representation of electrosensitive drug delivery coating. Illustration of the chemical structure of the PPy coating containing sodium p -toluenesulfate (SPTS) and biotin as the primary and secondary doping agents. Streptavidin, with four potential binding sites, covalently binds to the biotin incorporated in the PPy-coating at one site and up to three biotinylated growth factors at the other sites, to function as the drug-complex carrier.

    Journal: Frontiers in Chemistry

    Article Title: Electrically Stimulated Tunable Drug Delivery From Polypyrrole-Coated Polyvinylidene Fluoride

    doi: 10.3389/fchem.2021.599631

    Figure Lengend Snippet: Schematic representation of electrosensitive drug delivery coating. Illustration of the chemical structure of the PPy coating containing sodium p -toluenesulfate (SPTS) and biotin as the primary and secondary doping agents. Streptavidin, with four potential binding sites, covalently binds to the biotin incorporated in the PPy-coating at one site and up to three biotinylated growth factors at the other sites, to function as the drug-complex carrier.

    Article Snippet: A similar procedure was used for loading a solution of biotinylated Nerve Growth Factor (NGF, Alomone Labs, Jerusalem, Israel) at a concentration of 120 ng/ml in deionized water into a different group of PPy-coated PVDF fibers. illustrates the final schematic of the chemical structure of drug carrier platform containing streptavidin conjugated to biotinylated growth factor and anchored to the biotin incorporated within the PPy coating on the PVDF fibers.

    Techniques: Binding Assay

    Electrical stimulation based NGF release and bioactivity assay (A) Streptavidin tethered biotinylated NGF release from PPy coated PVDF fibers during sequential electrical stimulation at 200 mV/mm, for 5 min and 5 min of incubation without stimulation (B) Bioactivity of released NGF compared to recombinant human NGF, biotinylated NGF, and control groups based on PC12 cell proliferation (*, p

    Journal: Frontiers in Chemistry

    Article Title: Electrically Stimulated Tunable Drug Delivery From Polypyrrole-Coated Polyvinylidene Fluoride

    doi: 10.3389/fchem.2021.599631

    Figure Lengend Snippet: Electrical stimulation based NGF release and bioactivity assay (A) Streptavidin tethered biotinylated NGF release from PPy coated PVDF fibers during sequential electrical stimulation at 200 mV/mm, for 5 min and 5 min of incubation without stimulation (B) Bioactivity of released NGF compared to recombinant human NGF, biotinylated NGF, and control groups based on PC12 cell proliferation (*, p

    Article Snippet: A similar procedure was used for loading a solution of biotinylated Nerve Growth Factor (NGF, Alomone Labs, Jerusalem, Israel) at a concentration of 120 ng/ml in deionized water into a different group of PPy-coated PVDF fibers. illustrates the final schematic of the chemical structure of drug carrier platform containing streptavidin conjugated to biotinylated growth factor and anchored to the biotin incorporated within the PPy coating on the PVDF fibers.

    Techniques: Incubation, Recombinant

    Stimulation of GCs with proNGF and NGF has no effects on the viability and the apoptosis of human GCs (A and B) and presence of the receptors for NGF and proNGF in human GCs (C – E) A: Results of ATP assays with human GCs. The stimulation was performed on day 2-3 for 24 h with different concentrations of proNGF and NGF. Staurosporin (10 μM) was used as positive control. Both recombinant proteins did not significantly affect viability of GCs. Each column represents the relative luminescence of four independent experiments (mean ± SEM) per group. Different letters indicate statistically significant differences between the staurosporine-group and the other groups (p

    Journal: Hormone molecular biology and clinical investigation

    Article Title: Pro-nerve growth factor in the ovary and human granulosa cells

    doi: 10.1515/hmbci-2015-0028

    Figure Lengend Snippet: Stimulation of GCs with proNGF and NGF has no effects on the viability and the apoptosis of human GCs (A and B) and presence of the receptors for NGF and proNGF in human GCs (C – E) A: Results of ATP assays with human GCs. The stimulation was performed on day 2-3 for 24 h with different concentrations of proNGF and NGF. Staurosporin (10 μM) was used as positive control. Both recombinant proteins did not significantly affect viability of GCs. Each column represents the relative luminescence of four independent experiments (mean ± SEM) per group. Different letters indicate statistically significant differences between the staurosporine-group and the other groups (p

    Article Snippet: Human GCs were incubated with recombinant proNGF (Cedarlane, Burlington, Canada) and recombinant NGF (Alomone Labs, Jerusalem, Israel) each with 50 ng/ml for 1 h or 24 h in DMEM/Ham's F12 media without FCS, to examine downstream effects on early growth response 1 (EGR1) and choline acetyl-transferase (CHAT) level exerted by the factors.

    Techniques: Positive Control, Recombinant

    ProNGF and NGF in human GCs Left panel: Example of a Western blot: ProNGF is detected in human GCs (cells cultured for 2 and 3 days are shown); middle panel: Control blot, in which pre-adsorbed anti-proNGF antiserum was used; right panel: Example of a Western blot, in which an antiserum to NGF was used. Note that this antiserum, as expected, recognizes both NGF and proNGF and that the GCs shown contain abundant proNGF, while NGF was much less abundant.

    Journal: Hormone molecular biology and clinical investigation

    Article Title: Pro-nerve growth factor in the ovary and human granulosa cells

    doi: 10.1515/hmbci-2015-0028

    Figure Lengend Snippet: ProNGF and NGF in human GCs Left panel: Example of a Western blot: ProNGF is detected in human GCs (cells cultured for 2 and 3 days are shown); middle panel: Control blot, in which pre-adsorbed anti-proNGF antiserum was used; right panel: Example of a Western blot, in which an antiserum to NGF was used. Note that this antiserum, as expected, recognizes both NGF and proNGF and that the GCs shown contain abundant proNGF, while NGF was much less abundant.

    Article Snippet: Human GCs were incubated with recombinant proNGF (Cedarlane, Burlington, Canada) and recombinant NGF (Alomone Labs, Jerusalem, Israel) each with 50 ng/ml for 1 h or 24 h in DMEM/Ham's F12 media without FCS, to examine downstream effects on early growth response 1 (EGR1) and choline acetyl-transferase (CHAT) level exerted by the factors.

    Techniques: Western Blot, Cell Culture

    EGR1 and CHAT level increase in human GCs after stimulation with NGF A: Example of a Western blot with human GCs on day 2 of culture; stimulation of human GCs with NGF (50 ng/ml) for 1 h led to an increase in EGR1 levels whereas proNGF stimulation (50 ng/ml) did not. EGR1 pre-adsorption was used as control and β-actin as internal standard. B: Densitometric analysis of the experiments performed on day 2 of human GC culture. Each column represents the ratio of EGR1 to untreated control (mean ± SEM) of four independent experiments. *, p

    Journal: Hormone molecular biology and clinical investigation

    Article Title: Pro-nerve growth factor in the ovary and human granulosa cells

    doi: 10.1515/hmbci-2015-0028

    Figure Lengend Snippet: EGR1 and CHAT level increase in human GCs after stimulation with NGF A: Example of a Western blot with human GCs on day 2 of culture; stimulation of human GCs with NGF (50 ng/ml) for 1 h led to an increase in EGR1 levels whereas proNGF stimulation (50 ng/ml) did not. EGR1 pre-adsorption was used as control and β-actin as internal standard. B: Densitometric analysis of the experiments performed on day 2 of human GC culture. Each column represents the ratio of EGR1 to untreated control (mean ± SEM) of four independent experiments. *, p

    Article Snippet: Human GCs were incubated with recombinant proNGF (Cedarlane, Burlington, Canada) and recombinant NGF (Alomone Labs, Jerusalem, Israel) each with 50 ng/ml for 1 h or 24 h in DMEM/Ham's F12 media without FCS, to examine downstream effects on early growth response 1 (EGR1) and choline acetyl-transferase (CHAT) level exerted by the factors.

    Techniques: Western Blot, Adsorption

    The NGF precursor proNGF (A) and mature NGF (B) are present in the cells of the follicular wall in human ovaries Immunohistochemical staining of sections of human ovaries reveals that proNGF is present in cells of a large antral follicle, namely in GCs and theca cells (TCs). Positive staining reaction is indicated by the brown color. Note that the antiserum is specific for the pro-region of the proNGF molecule and does not recognize mature NGF. Bar: 30 μm. Insert control: Result of an experiment in which the proNGF antiserum was pre-adsorbed.

    Journal: Hormone molecular biology and clinical investigation

    Article Title: Pro-nerve growth factor in the ovary and human granulosa cells

    doi: 10.1515/hmbci-2015-0028

    Figure Lengend Snippet: The NGF precursor proNGF (A) and mature NGF (B) are present in the cells of the follicular wall in human ovaries Immunohistochemical staining of sections of human ovaries reveals that proNGF is present in cells of a large antral follicle, namely in GCs and theca cells (TCs). Positive staining reaction is indicated by the brown color. Note that the antiserum is specific for the pro-region of the proNGF molecule and does not recognize mature NGF. Bar: 30 μm. Insert control: Result of an experiment in which the proNGF antiserum was pre-adsorbed.

    Article Snippet: Human GCs were incubated with recombinant proNGF (Cedarlane, Burlington, Canada) and recombinant NGF (Alomone Labs, Jerusalem, Israel) each with 50 ng/ml for 1 h or 24 h in DMEM/Ham's F12 media without FCS, to examine downstream effects on early growth response 1 (EGR1) and choline acetyl-transferase (CHAT) level exerted by the factors.

    Techniques: Immunohistochemistry, Staining

    Differential binding of pro-BDNF and neurotension to sortilin and pro-sortilin. A , SPR analysis showing that unprocessed pro-BDNF (50 n m ) binds nearly as efficiently to the receptor in the presence (pro-sortilin) as in the absence (sortilin) of the receptor

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Differential binding of pro-BDNF and neurotension to sortilin and pro-sortilin. A , SPR analysis showing that unprocessed pro-BDNF (50 n m ) binds nearly as efficiently to the receptor in the presence (pro-sortilin) as in the absence (sortilin) of the receptor

    Article Snippet: Internalization of bound ligands was studied by the incubation of cells for 30 min at 37 °C with anti-sortilin polyclonal antibodies (10 μg/ml), GST-NGFpro (1 μg/ml), or 100 n m BDNF pro-domain (Alomone) diluted in culture medium.

    Techniques: Binding Assay, SPR Assay

    Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181

    Article Snippet: Internalization of bound ligands was studied by the incubation of cells for 30 min at 37 °C with anti-sortilin polyclonal antibodies (10 μg/ml), GST-NGFpro (1 μg/ml), or 100 n m BDNF pro-domain (Alomone) diluted in culture medium.

    Techniques: Derivative Assay, SPR Assay, Binding Assay

    Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared

    Article Snippet: Internalization of bound ligands was studied by the incubation of cells for 30 min at 37 °C with anti-sortilin polyclonal antibodies (10 μg/ml), GST-NGFpro (1 μg/ml), or 100 n m BDNF pro-domain (Alomone) diluted in culture medium.

    Techniques: Mutagenesis, Binding Assay, SPR Assay, Concentration Assay