sterol binding compound filipin  (Millipore)


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    Structured Review

    Millipore sterol binding compound filipin
    Specific tissues and membrane regions retain sterols preferentially. ( A-T ) Second instar larval tissues (represented diagrammatically in A,F,K,P) stained with <t>filipin.</t> The CNS (A-E), salivary glands (F-J), fat bodies (K-O) and midguts (P-T) from wild-type
    Sterol Binding Compound Filipin, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sterol binding compound filipin/product/Millipore
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sterol binding compound filipin - by Bioz Stars, 2020-04
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    vectashield mounting medium

    Images

    1) Product Images from "Survival strategies of a sterol auxotroph"

    Article Title: Survival strategies of a sterol auxotroph

    Journal: Development (Cambridge, England)

    doi: 10.1242/dev.044560

    Specific tissues and membrane regions retain sterols preferentially. ( A-T ) Second instar larval tissues (represented diagrammatically in A,F,K,P) stained with filipin. The CNS (A-E), salivary glands (F-J), fat bodies (K-O) and midguts (P-T) from wild-type
    Figure Legend Snippet: Specific tissues and membrane regions retain sterols preferentially. ( A-T ) Second instar larval tissues (represented diagrammatically in A,F,K,P) stained with filipin. The CNS (A-E), salivary glands (F-J), fat bodies (K-O) and midguts (P-T) from wild-type

    Techniques Used: Staining

    Related Articles

    Staining:

    Article Title: Survival strategies of a sterol auxotroph
    Article Snippet: .. Tissues were fixed and stained with the fluorescent sterol-binding compound filipin (Sigma) as described previously ( ) and mounted using VECTASHIELD mounting medium (Vector Laboratories). .. Second instar fat bodies were removed on ice in PBS containing protease inhibitors (Roche) on ice, immediately transferred to 4% formaldehyde in PBS, then stained as described previously ( ).

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    Millipore filipin
    StarD5 deletion lowers PM cholesterol in macrophages and ABCA1-dependent cholesterol efflux. A: Primary peritoneal macrophages from WT and StarD5 −/− mice were imaged following staining with <t>filipin</t> and BODIPY 493-503, as indicated, as well as by differential interference contrast for those stained with BODIPY 493-503. B: Total, free, esterified, and PM cholesterol were quantified as described in the Materials and Methods (n = 4). C: Accessible PM cholesterol was quantified as described in the Materials and Methods (n = 3, * P ≤ 0.05 for WT versus StarD5 −/− ). D: Primary peritoneal macrophages from WT and StarD5 −/− mice were used in cholesterol efflux assays as described in the Materials and Methods in the absence or presence of cAMP or cyclosporine A. Cholesterol efflux was calculated as the percentage of total cell 3 H-cholesterol content, which was about 5% of the total cholesterol (total effluxed 3 H-cholesterol + cell-associated 3 H-cholesterol) and represented as a percentage of the effluxed cholesterol in WT macrophages in the presence of cAMP. Primary peritoneal macrophages from StarD5 −/− mice infected with Ad-StarD5 (MOI of 200) were also used. The values represent the average ± SD (n = 4, * P
    Filipin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/filipin/product/Millipore
    Average 99 stars, based on 83 article reviews
    Price from $9.99 to $1999.99
    filipin - by Bioz Stars, 2020-04
    99/100 stars
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    StarD5 deletion lowers PM cholesterol in macrophages and ABCA1-dependent cholesterol efflux. A: Primary peritoneal macrophages from WT and StarD5 −/− mice were imaged following staining with filipin and BODIPY 493-503, as indicated, as well as by differential interference contrast for those stained with BODIPY 493-503. B: Total, free, esterified, and PM cholesterol were quantified as described in the Materials and Methods (n = 4). C: Accessible PM cholesterol was quantified as described in the Materials and Methods (n = 3, * P ≤ 0.05 for WT versus StarD5 −/− ). D: Primary peritoneal macrophages from WT and StarD5 −/− mice were used in cholesterol efflux assays as described in the Materials and Methods in the absence or presence of cAMP or cyclosporine A. Cholesterol efflux was calculated as the percentage of total cell 3 H-cholesterol content, which was about 5% of the total cholesterol (total effluxed 3 H-cholesterol + cell-associated 3 H-cholesterol) and represented as a percentage of the effluxed cholesterol in WT macrophages in the presence of cAMP. Primary peritoneal macrophages from StarD5 −/− mice infected with Ad-StarD5 (MOI of 200) were also used. The values represent the average ± SD (n = 4, * P

    Journal: Journal of Lipid Research

    Article Title: StarD5: an ER stress protein regulates plasma membrane and intracellular cholesterol homeostasis [S]

    doi: 10.1194/jlr.M091967

    Figure Lengend Snippet: StarD5 deletion lowers PM cholesterol in macrophages and ABCA1-dependent cholesterol efflux. A: Primary peritoneal macrophages from WT and StarD5 −/− mice were imaged following staining with filipin and BODIPY 493-503, as indicated, as well as by differential interference contrast for those stained with BODIPY 493-503. B: Total, free, esterified, and PM cholesterol were quantified as described in the Materials and Methods (n = 4). C: Accessible PM cholesterol was quantified as described in the Materials and Methods (n = 3, * P ≤ 0.05 for WT versus StarD5 −/− ). D: Primary peritoneal macrophages from WT and StarD5 −/− mice were used in cholesterol efflux assays as described in the Materials and Methods in the absence or presence of cAMP or cyclosporine A. Cholesterol efflux was calculated as the percentage of total cell 3 H-cholesterol content, which was about 5% of the total cholesterol (total effluxed 3 H-cholesterol + cell-associated 3 H-cholesterol) and represented as a percentage of the effluxed cholesterol in WT macrophages in the presence of cAMP. Primary peritoneal macrophages from StarD5 −/− mice infected with Ad-StarD5 (MOI of 200) were also used. The values represent the average ± SD (n = 4, * P

    Article Snippet: Filipin was from Cayman Biochemicals; cholesterol oxidase was from Calbiochem, BODIPY 493/503 was from Fisher Scientific; cAMP, cyclosporin A, and other general chemicals were from Sigma.

    Techniques: Mouse Assay, Staining, Infection

    Disruption of lipid rafts inhibits the antiproliferative effects of GPR55 activation. ( A ) Mz-ChA-1 cells were pretreated with lipid raft disrupters 0.1 mM β–methylcyclodextrin, or 1 μg/mL filipin III for 1 hr prior to the addition of O-1602 (10 −5 M). Cell viability was determined by MTS assays. Data are expressed as average ± SEM (*p

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Anandamide exerts its antiproliferative actions on cholangiocarcinoma by activation of the GPR55 receptor

    doi: 10.1038/labinvest.2011.62

    Figure Lengend Snippet: Disruption of lipid rafts inhibits the antiproliferative effects of GPR55 activation. ( A ) Mz-ChA-1 cells were pretreated with lipid raft disrupters 0.1 mM β–methylcyclodextrin, or 1 μg/mL filipin III for 1 hr prior to the addition of O-1602 (10 −5 M). Cell viability was determined by MTS assays. Data are expressed as average ± SEM (*p

    Article Snippet: The inhibitors utilized were the lipid raft disruptors, methyl-β-cyclodextrin (0.1 mM), , and filipin III (1 mg/mL) ( , ), and the JNK inhibitor (10−7 M; SP600125; EMD Chemicals, Gibbstown, NJ) ( ).

    Techniques: Activation Assay

    Overall structures of CYP105P1-filipin I complex ( A ) and unliganded CYP105D6 ( B ), illustrated by ribbon representation. Heme and ligands are shown as stick models. The BC and FG loop regions are shown in dark gray. a.a. , amino acids.

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Overall structures of CYP105P1-filipin I complex ( A ) and unliganded CYP105D6 ( B ), illustrated by ribbon representation. Heme and ligands are shown as stick models. The BC and FG loop regions are shown in dark gray. a.a. , amino acids.

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques:

    Spectral changes of CYP105P1 (ferric resting state) upon the addition of increasing concentrations of filipin I ( A ), its difference spectra ( B ), and the titration curve calculated using the values of absorption differences at 387 and 422 nm ( C ).

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Spectral changes of CYP105P1 (ferric resting state) upon the addition of increasing concentrations of filipin I ( A ), its difference spectra ( B ), and the titration curve calculated using the values of absorption differences at 387 and 422 nm ( C ).

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques: Titration

    Interactions between CYP105P1 and filipin I. A , shown is an F obs − F calc omit electron density map of the filipin I molecule contoured at 4.0 σ. B , hydrophobic interactions are observed at both sides of the 28-membered ring. Labels for atoms of filipin I are underlined. C , a stereographic figure shows interactions with the BC loop, FG helices, and I helix. The water molecules mediate hydrophilic interactions with the polyol group of filipin I. The extensive hydrogen-bonding network and residues involved in it are shown as dotted lines and stick models, respectively. The distance between the C26 atom of filipin I and the heme iron is 5.0 Å, and the pro-S hydrogen side is directed toward the heme.

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Interactions between CYP105P1 and filipin I. A , shown is an F obs − F calc omit electron density map of the filipin I molecule contoured at 4.0 σ. B , hydrophobic interactions are observed at both sides of the 28-membered ring. Labels for atoms of filipin I are underlined. C , a stereographic figure shows interactions with the BC loop, FG helices, and I helix. The water molecules mediate hydrophilic interactions with the polyol group of filipin I. The extensive hydrogen-bonding network and residues involved in it are shown as dotted lines and stick models, respectively. The distance between the C26 atom of filipin I and the heme iron is 5.0 Å, and the pro-S hydrogen side is directed toward the heme.

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques:

    Active site structures of CYP105P1-filipin I ( green ) superimposed with CYP105D6 ( A , cyan ), P450cam-camphor-O 2 ( B , yellow ), and P450 EryK-erythromycin D ( C , magenta ). Water molecules and the hydroxylation target positions of substrates (C26 of filipin I, C5 of camphor, and C12 of erythromycin D) are shown as spheres . A water molecule is positioned 2.8 Å from the heme iron in the CYP105D6 structure ( A ).

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Active site structures of CYP105P1-filipin I ( green ) superimposed with CYP105D6 ( A , cyan ), P450cam-camphor-O 2 ( B , yellow ), and P450 EryK-erythromycin D ( C , magenta ). Water molecules and the hydroxylation target positions of substrates (C26 of filipin I, C5 of camphor, and C12 of erythromycin D) are shown as spheres . A water molecule is positioned 2.8 Å from the heme iron in the CYP105D6 structure ( A ).

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques:

    Closing motion of CYP105P1. Shown is a stereographic superimposition of the filipin I complex structure with the ligand-free wild-type ( A ) and H72A mutant ( B ) structures. BC loop and FG helices are colored magenta and green in ligand-free and complex structures, respectively. The filipin I molecule is shown as yellow sticks . In the ligand-free wild-type structure ( A ), the side chain of His-72 is ligated to the heme iron as the sixth ligand, and the BC loop sinks into the heme to completely cover the distal pocket.

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Closing motion of CYP105P1. Shown is a stereographic superimposition of the filipin I complex structure with the ligand-free wild-type ( A ) and H72A mutant ( B ) structures. BC loop and FG helices are colored magenta and green in ligand-free and complex structures, respectively. The filipin I molecule is shown as yellow sticks . In the ligand-free wild-type structure ( A ), the side chain of His-72 is ligated to the heme iron as the sixth ligand, and the BC loop sinks into the heme to completely cover the distal pocket.

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques: Mutagenesis

    Spectral changes of CYP105D6 (ferric resting state) upon the addition of increasing concentrations of filipin I ( A ), its difference spectra ( B ), and the titration curve calculated using the values of absorption differences at 387 and 420 nm ( C ). A nonlinear fitting with a quadratic equation was applied to the titration curve.

    Journal: The Journal of Biological Chemistry

    Article Title: Regio- and Stereospecificity of Filipin Hydroxylation Sites Revealed by Crystal Structures of Cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis *

    doi: 10.1074/jbc.M109.092460

    Figure Lengend Snippet: Spectral changes of CYP105D6 (ferric resting state) upon the addition of increasing concentrations of filipin I ( A ), its difference spectra ( B ), and the titration curve calculated using the values of absorption differences at 387 and 420 nm ( C ). A nonlinear fitting with a quadratic equation was applied to the titration curve.

    Article Snippet: Before crystallization, filipin I was dissolved in dimethyl sulfoxide, mixed with a CYP105P1 sample, and concentrated using an Ultrafree Centrifugal Filter Device (Millipore, Billerica, MA).

    Techniques: Titration

    Internalization of the hMCRs in HEK293 cells. Cells were incubated with [ 125 I]-NDP- α -MSH and caveolae inhibitors, filipin (▼) and nystatin (▼) compared with control (|) at 37 °C for the indicated times. Acid-resistant and acid-sensitive binding were determined. Percentage internalization (acid-resistant binding) was expressed by measuring total binding at each time-point.

    Journal: Chemical biology & drug design

    Article Title: Cell Signaling and Trafficking of Human Melanocortin Receptors in Real Time Using Two-photon Fluorescence and Confocal Laser Microscopy: Differentiation of Agonists and Antagonists

    doi: 10.1111/j.1747-0285.2006.00432.x

    Figure Lengend Snippet: Internalization of the hMCRs in HEK293 cells. Cells were incubated with [ 125 I]-NDP- α -MSH and caveolae inhibitors, filipin (▼) and nystatin (▼) compared with control (|) at 37 °C for the indicated times. Acid-resistant and acid-sensitive binding were determined. Percentage internalization (acid-resistant binding) was expressed by measuring total binding at each time-point.

    Article Snippet: H-89 and Filipin were from Calbiochem (San Diego, CA, USA).

    Techniques: Incubation, Binding Assay