ocp  (Millipore)


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    Name:
    Sample mill
    Description:
    SS blades for small sample grinding SS shearing blades rotate within SS chamber Transparent lid with Pulse On safety switch operates only with lid in place Use should be restricted to nonflammable noncorrosive solids Approx capacity 50 g
    Catalog Number:
    z278181
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    Millipore ocp
    Sample mill
    SS blades for small sample grinding SS shearing blades rotate within SS chamber Transparent lid with Pulse On safety switch operates only with lid in place Use should be restricted to nonflammable noncorrosive solids Approx capacity 50 g
    https://www.bioz.com/result/ocp/product/Millipore
    Average 99 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    ocp - by Bioz Stars, 2020-07
    99/100 stars

    Images

    1) Product Images from "Xanthine oxidoreductase regulates macrophage IL1β secretion upon NLRP3 inflammasome activation"

    Article Title: Xanthine oxidoreductase regulates macrophage IL1β secretion upon NLRP3 inflammasome activation

    Journal: Nature Communications

    doi: 10.1038/ncomms7555

    Crystal-induced IL1β secretion is mediated by ROS. In vitro BMDM (Pam3Cys primed) were pretreated with XOR inhibitors: febuxostat, 200 μM and allopurinol, 500 μg ml −1 and stimulated with OCP or MSU at 250 μg ml −1 , Alum-500 μg ml −1 and HZ-200 μg ml −1 . ( a ) Superoxide was measured with dihydroethidium (DHE), results expressed as fold increase in relative fluorescence units (RFUs) at T =120 min over T =0. ( b ) ROS measured by luminol, data obtained by relative luminescence units (RLUs) at T =60 min. Data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by the t -test for all panels.
    Figure Legend Snippet: Crystal-induced IL1β secretion is mediated by ROS. In vitro BMDM (Pam3Cys primed) were pretreated with XOR inhibitors: febuxostat, 200 μM and allopurinol, 500 μg ml −1 and stimulated with OCP or MSU at 250 μg ml −1 , Alum-500 μg ml −1 and HZ-200 μg ml −1 . ( a ) Superoxide was measured with dihydroethidium (DHE), results expressed as fold increase in relative fluorescence units (RFUs) at T =120 min over T =0. ( b ) ROS measured by luminol, data obtained by relative luminescence units (RLUs) at T =60 min. Data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by the t -test for all panels.

    Techniques Used: In Vitro, Fluorescence

    Urate generated by XOR is not the mediator of inflammasome responses in crystal-stimulated macrophages. ( a , b ) In vitro C57BL/6 or intUOX-Tg-derived BMDM (Pam3Cys primed), pretreated with uricase—10 μg ml −1 and XOR inhibitor febuxostat—200 μM, were stimulated with OCP or MSU at 250 μg ml −1 , Alum-500 μg ml −1 , HZ-200 μg ml −1 or soluble urate at 600 μM. Experiments were performed at 6 h; data are representative of at least two experiments. ( c ) Mice were pretreated with uricase—20 μg per mouse. OCP or PBS injected. After 6 h, peritoneal washes were obtained, viable cells counted, and urate and IL1β measured in cell-free washes (two pooled experiments). Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance. ND, not detectable; NS, not significant.
    Figure Legend Snippet: Urate generated by XOR is not the mediator of inflammasome responses in crystal-stimulated macrophages. ( a , b ) In vitro C57BL/6 or intUOX-Tg-derived BMDM (Pam3Cys primed), pretreated with uricase—10 μg ml −1 and XOR inhibitor febuxostat—200 μM, were stimulated with OCP or MSU at 250 μg ml −1 , Alum-500 μg ml −1 , HZ-200 μg ml −1 or soluble urate at 600 μM. Experiments were performed at 6 h; data are representative of at least two experiments. ( c ) Mice were pretreated with uricase—20 μg per mouse. OCP or PBS injected. After 6 h, peritoneal washes were obtained, viable cells counted, and urate and IL1β measured in cell-free washes (two pooled experiments). Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance. ND, not detectable; NS, not significant.

    Techniques Used: Generated, In Vitro, Derivative Assay, Mouse Assay, Injection

    Crystal-mediated XOR activation induces the PI3K–AKT–mTOR pathway and mitochondrial ROS production. In vitro BMDM (Pam3Cys primed), and THP1 cells (PMA primed) were pretreated with 200 μM febuxostat, 10 μM Ly294002, 10 μM Wortmannin, 10 μM AKTx, or Rapamycin (Rapa), and stimulated with OCP or MSU at 250 μg ml −1 , or 500 μg ml −1 Alum. ( a , b ) IL1β protein secretion measured in BMDM. ( c ) Relative expression levels determined by ELISA of phosphorylated (p-) AKT (ser473) over total AKT levels in BMDM at 1 h. ( d ) THP1 cell extracts analysed for phosphorylated AKT (p-AKT) at ser473, and α-tubulin by western blot. Relative protein levels determined by band intensity quantification, and given as p-AKT over α-tubulin, normalized with unstimulated cells being 1. ( e ) Mitochondrial ROS detected by MitoSOX, results given as RFU at T =60 min over T =0. ( f ) Mitochondrial potential of BMDM was measured using the ratio of monomeric (Em 525 ) to multimeric JC-10 (Em 590 ). Experiments were performed at 6 h; data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance for all panels
    Figure Legend Snippet: Crystal-mediated XOR activation induces the PI3K–AKT–mTOR pathway and mitochondrial ROS production. In vitro BMDM (Pam3Cys primed), and THP1 cells (PMA primed) were pretreated with 200 μM febuxostat, 10 μM Ly294002, 10 μM Wortmannin, 10 μM AKTx, or Rapamycin (Rapa), and stimulated with OCP or MSU at 250 μg ml −1 , or 500 μg ml −1 Alum. ( a , b ) IL1β protein secretion measured in BMDM. ( c ) Relative expression levels determined by ELISA of phosphorylated (p-) AKT (ser473) over total AKT levels in BMDM at 1 h. ( d ) THP1 cell extracts analysed for phosphorylated AKT (p-AKT) at ser473, and α-tubulin by western blot. Relative protein levels determined by band intensity quantification, and given as p-AKT over α-tubulin, normalized with unstimulated cells being 1. ( e ) Mitochondrial ROS detected by MitoSOX, results given as RFU at T =60 min over T =0. ( f ) Mitochondrial potential of BMDM was measured using the ratio of monomeric (Em 525 ) to multimeric JC-10 (Em 590 ). Experiments were performed at 6 h; data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance for all panels

    Techniques Used: Activation Assay, In Vitro, Expressing, Enzyme-linked Immunosorbent Assay, Western Blot

    XOR was not modulated at RNA and protein levels. In vitro C57BL/6 BMDM (Pam3Cys (P3C) or LPSup primed), and THP1 (PMA primed) were stimulated with OCP and MSU at 250 μg ml −1 , 500 μg ml −1 Alum and 200 μg ml −1 HZ. ( a ) The % XO and XDH activity was measured in BMDM cell lysates using the pterin assay; ( b ) RNA transcript level of XOR by qRT–PCR in P3C-primed BMDM. Expression levels were quantified using the 2 ΔΔCT method, with Tbp as a reference gene. ( c ) Total XOR protein levels in P3C-primed BMDM measured by ELISA. ( d ) THP1 cells stimulated with OCP crystals and the CE, and supernatants blotted against anti-human XOR antibody or α-tubulin.
    Figure Legend Snippet: XOR was not modulated at RNA and protein levels. In vitro C57BL/6 BMDM (Pam3Cys (P3C) or LPSup primed), and THP1 (PMA primed) were stimulated with OCP and MSU at 250 μg ml −1 , 500 μg ml −1 Alum and 200 μg ml −1 HZ. ( a ) The % XO and XDH activity was measured in BMDM cell lysates using the pterin assay; ( b ) RNA transcript level of XOR by qRT–PCR in P3C-primed BMDM. Expression levels were quantified using the 2 ΔΔCT method, with Tbp as a reference gene. ( c ) Total XOR protein levels in P3C-primed BMDM measured by ELISA. ( d ) THP1 cells stimulated with OCP crystals and the CE, and supernatants blotted against anti-human XOR antibody or α-tubulin.

    Techniques Used: In Vitro, Activity Assay, Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay

    XOR is involved in caspase1-dependent secretion of IL1β in macrophages stimulated with microcrystals. In vitro C57BL/6 BMDM (Pam3Cys (P3C) or LPSup primed), and THP1 (PMA primed) were stimulated with OCP and MSU at 250 μg ml −1 , Alum-500 μg ml −1 and HZ-200 μg ml −1 . IL1β protein was measured by ELISA in supernatants; intracellular XO and UA measured on protein extracts by activity tests. ( a ) Upper panel: P3C primed, OCP-stimulated BMDM. Lower panel: In vivo OCP-induced peritonitis. Levels of IL1β, XO and UA measured in peritoneal washes of individual mice. ( b ) XO activity measured in LPSup primed, crystal-stimulated BMDM at 2 h. ( c ) IL1β measured in XOR siRNA, or control NegSiRNA-transfected BMDM that were P3C primed. ( d ) BMDM were pretreated with XOR inhibitors (Allopurinol 250 g ml −1 , Febuxostat 200 μM) and Apocynin (2.5 mM), extracellular IL1β protein levels quantified and expressed as percentage of stimulation of inhibitor-treated versus non-treated cells. ( e ) Protein sizes of proCaspase1 and proIL1β in cell extracts (CEs), and active IL1β in the supernatants (spts) by western blot, secreted IL1β and caspase1 by ELISA. ( f ) In vivo , mice were pretreated with Allopurinol—500 μg per mouse 30 min prior to OCP-1 mg per mouse or PBS control intraperitoneal injection. After 6 h, peritoneal washes were obtained (two pooled experiments). Viable cells were counted and urate, and IL1β measured. Unless stated, experiments were performed at 6 h and data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance ( b , d – f ) or the t -test ( a , c ). NP, not performed; NS, not significant.
    Figure Legend Snippet: XOR is involved in caspase1-dependent secretion of IL1β in macrophages stimulated with microcrystals. In vitro C57BL/6 BMDM (Pam3Cys (P3C) or LPSup primed), and THP1 (PMA primed) were stimulated with OCP and MSU at 250 μg ml −1 , Alum-500 μg ml −1 and HZ-200 μg ml −1 . IL1β protein was measured by ELISA in supernatants; intracellular XO and UA measured on protein extracts by activity tests. ( a ) Upper panel: P3C primed, OCP-stimulated BMDM. Lower panel: In vivo OCP-induced peritonitis. Levels of IL1β, XO and UA measured in peritoneal washes of individual mice. ( b ) XO activity measured in LPSup primed, crystal-stimulated BMDM at 2 h. ( c ) IL1β measured in XOR siRNA, or control NegSiRNA-transfected BMDM that were P3C primed. ( d ) BMDM were pretreated with XOR inhibitors (Allopurinol 250 g ml −1 , Febuxostat 200 μM) and Apocynin (2.5 mM), extracellular IL1β protein levels quantified and expressed as percentage of stimulation of inhibitor-treated versus non-treated cells. ( e ) Protein sizes of proCaspase1 and proIL1β in cell extracts (CEs), and active IL1β in the supernatants (spts) by western blot, secreted IL1β and caspase1 by ELISA. ( f ) In vivo , mice were pretreated with Allopurinol—500 μg per mouse 30 min prior to OCP-1 mg per mouse or PBS control intraperitoneal injection. After 6 h, peritoneal washes were obtained (two pooled experiments). Viable cells were counted and urate, and IL1β measured. Unless stated, experiments were performed at 6 h and data are representative of at least two experiments. Results are expressed as mean±s.e.m. Significance was determined at * P ≤0.05, ** P ≤0.01, *** P ≤0.005 and **** P ≤0.0001 by analysis of variance ( b , d – f ) or the t -test ( a , c ). NP, not performed; NS, not significant.

    Techniques Used: In Vitro, Enzyme-linked Immunosorbent Assay, Activity Assay, In Vivo, Mouse Assay, Transfection, Western Blot, Injection

    2) Product Images from "Solid state NMR - An indispensable tool in organic-inorganic biocomposite characterization; refining the structure of octacalcium phosphate composites with the linear metabolic di-acids succinate and adipate"

    Article Title: Solid state NMR - An indispensable tool in organic-inorganic biocomposite characterization; refining the structure of octacalcium phosphate composites with the linear metabolic di-acids succinate and adipate

    Journal: Solid State Nuclear Magnetic Resonance

    doi: 10.1016/j.ssnmr.2018.08.004

    13 C— 13 C proton-driven spin diffusion correlation (PDSD, 5 ms mixing time) experiments on uniformly 13 C labelled OCP-SUC (left) and OCP-ADI (right). Correlations proving a single non-centrosymmetric ADI within the OCP-ADI structure are highlighted in red. Corresponding 1D 13 C spectra are superimposed. Signal broadening relative to unlabelled composites is ascribed to residual 13 C— 13 C dipolar interactions, and unresolved 13 C— 13 C scalar coupling. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: 13 C— 13 C proton-driven spin diffusion correlation (PDSD, 5 ms mixing time) experiments on uniformly 13 C labelled OCP-SUC (left) and OCP-ADI (right). Correlations proving a single non-centrosymmetric ADI within the OCP-ADI structure are highlighted in red. Corresponding 1D 13 C spectra are superimposed. Signal broadening relative to unlabelled composites is ascribed to residual 13 C— 13 C dipolar interactions, and unresolved 13 C— 13 C scalar coupling. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Diffusion-based Assay, Mass Spectrometry

    Diagrams on the right depict structures of OCP-SUC (top) and OCP-ADI (bottom) consistent with two identical non-centrosymmetric di-acids per unit cell, modified from those implied by Model I of Markovic et al. [ 18 ], (left) which implies the existence of two identical and centrosymmetric di-acids.
    Figure Legend Snippet: Diagrams on the right depict structures of OCP-SUC (top) and OCP-ADI (bottom) consistent with two identical non-centrosymmetric di-acids per unit cell, modified from those implied by Model I of Markovic et al. [ 18 ], (left) which implies the existence of two identical and centrosymmetric di-acids.

    Techniques Used: Modification

    Typical 13 C{ 31 P} REDOR data (top) for OCP-SUC (left) and OCP-ADI (right), and resultant dephasing curves (bottom), showing the non-equivalence of the carboxylate carbons, and of the methylene carbons, with respect to neighbourhood phosphorus atoms Error bars in the dephasing curves represent spectral signal-to-noise measurements at each respective dephasing time.
    Figure Legend Snippet: Typical 13 C{ 31 P} REDOR data (top) for OCP-SUC (left) and OCP-ADI (right), and resultant dephasing curves (bottom), showing the non-equivalence of the carboxylate carbons, and of the methylene carbons, with respect to neighbourhood phosphorus atoms Error bars in the dephasing curves represent spectral signal-to-noise measurements at each respective dephasing time.

    Techniques Used:

    Comparison between 13 C, and 31 P, NMR spectra of different batches of OCP-SUC and OCP-ADI, and pure OCP. Minor 13 C signals in some batches, of variable occurrence, are marked by asterisks.
    Figure Legend Snippet: Comparison between 13 C, and 31 P, NMR spectra of different batches of OCP-SUC and OCP-ADI, and pure OCP. Minor 13 C signals in some batches, of variable occurrence, are marked by asterisks.

    Techniques Used: Nuclear Magnetic Resonance

    3) Product Images from "Molecular Mechanism of Photoactivation and Structural Location of the Cyanobacterial Orange Carotenoid Protein"

    Article Title: Molecular Mechanism of Photoactivation and Structural Location of the Cyanobacterial Orange Carotenoid Protein

    Journal: Biochemistry

    doi: 10.1021/bi401539w

    The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted
    Figure Legend Snippet: The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted

    Techniques Used: Binding Assay

    Related Articles

    Electron Microscopy:

    Article Title: Dirofilaria immitis Microfilariae and Third-Stage Larvae Induce Canine NETosis Resulting in Different Types of Neutrophil Extracellular Traps
    Article Snippet: .. Scanning Electron Microscopy (SEM) Canine PMN (n = 3.5 × 105 ) were cocultured with vital D. immitis L3 (10 larvae/sample) or microfilariae (20 larvae/sample) on poly-l -lysine (Sigma-Aldrich) pre-coated coverslips (60 min, 37°C). .. After incubation, the samples were fixed in 2.5% glutaraldehyde [60 min, room temperature (RT), Merck], post-fixed in 1% osmium tetroxide (Merck), washed in distilled water, dehydrated, critical point dried by CO2 treatment, and spayed with gold.

    Whole Genome Amplification:

    Article Title: Genome wide identification of promoter binding sites for H4K12ac in human sperm and its relevance for early embryonic development
    Article Snippet: .. The required amount of DNA for microarray analysis (4 µg per sample) was generated using WGA Re-amplification Kit (Sigma-Aldrich, Steinheim, Germany). ..

    Buffer Exchange:

    Article Title: An accurate TMT-based approach to quantify and model lysine susceptibility to conjugation via N-hydroxysuccinimide esters in a monoclonal antibody
    Article Snippet: .. For the deglycosylation experiment, 400 μg of NIST mAb was diluted to 5 mg/mL through the addition of 45 μL of PBS (control glycosylated sample) or PNGaseF (Sigma, deglycosylated sample) and incubated at 37 °C for 5 h, prior to the initial buffer exchange step. .. To remove sample heterogeneity due to glycans and C-terminal lysine residues prior to intact mass analysis, a 20 μg aliquot of each TMT-labeled sample was treated with 4 μL PNGaseF overnight at 37 °C followed by a 2 h incubation with 4 μL of Carboxypeptidase B (Sigma, 0.05 mg/mL).

    Incubation:

    Article Title: An accurate TMT-based approach to quantify and model lysine susceptibility to conjugation via N-hydroxysuccinimide esters in a monoclonal antibody
    Article Snippet: .. For the deglycosylation experiment, 400 μg of NIST mAb was diluted to 5 mg/mL through the addition of 45 μL of PBS (control glycosylated sample) or PNGaseF (Sigma, deglycosylated sample) and incubated at 37 °C for 5 h, prior to the initial buffer exchange step. .. To remove sample heterogeneity due to glycans and C-terminal lysine residues prior to intact mass analysis, a 20 μg aliquot of each TMT-labeled sample was treated with 4 μL PNGaseF overnight at 37 °C followed by a 2 h incubation with 4 μL of Carboxypeptidase B (Sigma, 0.05 mg/mL).

    Purification:

    Article Title: Molecular Determinants of Scaffold-induced Linear Ubiquitinylation of B Cell Lymphoma/Leukemia 10 (Bcl10) during T Cell Receptor and Oncogenic Caspase Recruitment Domain-containing Protein 11 (CARD11) Signaling *
    Article Snippet: .. Purified mouse CD4+ T cells (7 × 107 /sample) or Jurkat T cells (1 × 108 /sample) were stimulated with or without 50 ng/ml PMA (Sigma) and 1 μ m iono (Sigma) for 30 min at 37 °C. ..

    Microarray:

    Article Title: Genome wide identification of promoter binding sites for H4K12ac in human sperm and its relevance for early embryonic development
    Article Snippet: .. The required amount of DNA for microarray analysis (4 µg per sample) was generated using WGA Re-amplification Kit (Sigma-Aldrich, Steinheim, Germany). ..

    Generated:

    Article Title: Genome wide identification of promoter binding sites for H4K12ac in human sperm and its relevance for early embryonic development
    Article Snippet: .. The required amount of DNA for microarray analysis (4 µg per sample) was generated using WGA Re-amplification Kit (Sigma-Aldrich, Steinheim, Germany). ..

    Western Blot:

    Article Title: Ku86 exists as both a full-length and a protease-sensitive natural variant in multiple myeloma cells
    Article Snippet: .. Western immunoblotting Cell lysates (20.0 μg of protein/sample) were first resolved on a 12.5% SDS-PAGE gel, transferred onto polyvinylidene difluoride (PVDF) membranes (Millipore Corporation, Billerica, MA) and then blocked using Tris buffered saline Tween-20 (TBST) buffer containing 5% non-fat milk. .. Membranes were next hybridized overnight in the cold room using various murine monoclonal antibodies (mAb) – i.e. S10B1 anti-Ku86 N-terminus (amino acid (aa) residues 8–221; NeoMarkers, Fremont, CA); anti-heavy chain of the human major histocompatibility complex (MHC) mAb (clone 22.63.4, Accurate Chemical and Scientific Co., Westbuty, NY; a kind gift from P. Macary, from the National University of Singapore); and anti-actin (Santa Cruz Biotechnology, Santa Cruz, CA) mAbs; washed three times in ice cold TBS-T; and then incubated with horseradish peroxidase (hrp) conjugated anti-mouse IgG mAb (1:2,000; Santa Cruz) for 1 hr.

    SDS Page:

    Article Title: Ku86 exists as both a full-length and a protease-sensitive natural variant in multiple myeloma cells
    Article Snippet: .. Western immunoblotting Cell lysates (20.0 μg of protein/sample) were first resolved on a 12.5% SDS-PAGE gel, transferred onto polyvinylidene difluoride (PVDF) membranes (Millipore Corporation, Billerica, MA) and then blocked using Tris buffered saline Tween-20 (TBST) buffer containing 5% non-fat milk. .. Membranes were next hybridized overnight in the cold room using various murine monoclonal antibodies (mAb) – i.e. S10B1 anti-Ku86 N-terminus (amino acid (aa) residues 8–221; NeoMarkers, Fremont, CA); anti-heavy chain of the human major histocompatibility complex (MHC) mAb (clone 22.63.4, Accurate Chemical and Scientific Co., Westbuty, NY; a kind gift from P. Macary, from the National University of Singapore); and anti-actin (Santa Cruz Biotechnology, Santa Cruz, CA) mAbs; washed three times in ice cold TBS-T; and then incubated with horseradish peroxidase (hrp) conjugated anti-mouse IgG mAb (1:2,000; Santa Cruz) for 1 hr.

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  • 90
    Millipore ocps
    Illustration of the basic components of an <t>ELISA</t> for detection of <t>OCPs</t> and PCBs in environmental samples or extracts. Sample antigen (analyte) competes with antigen for binding sites on coating protein; after a wash step, detection is performed by adding substrate and chromophore
    Ocps, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ocps/product/Millipore
    Average 90 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    ocps - by Bioz Stars, 2020-07
    90/100 stars
      Buy from Supplier

    85
    Millipore pbs ocp complexes
    The structural location of the <t>OCP</t> in <t>PBS.</t> (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted
    Pbs Ocp Complexes, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs ocp complexes/product/Millipore
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pbs ocp complexes - by Bioz Stars, 2020-07
    85/100 stars
      Buy from Supplier

    85
    Millipore wt ocps
    Tumor necrosis factor <t>(TNF)</t> increases expression of vascular endothelial growth factor-C (VEGF-C) by osteoclast precursors <t>(OCPs).</t> Wild-type (WT) spleen cells were cultured with macrophage colony-stimulating factor (M-CSF) for 3 days to enrich for OCPs. OCPs were cultured in 10% serum with M-CSF and treated with phosphate-buffered saline (PBS) or TNF (10 ng/mL). (a) Expression of VEGF-C and β-actin mRNA was measured by real-time reverse transcription-polymerase chain reaction (RT-PCR) at various times (left panel), and protein levels were measured by Western blot analysis (right panels). (b) Expression of VEGF-A , - B , - C , - D , and placental growth factor ( PLGF ) mRNA was examined in samples treated for 24 hours. The fold increases in TNF-treated over PBS-treated cells at a given time were calculated. Values are the means of triplicate loadings plus standard deviation. The effect of different doses of TNF (c) or a combination with interleukin 1 (IL-1) (TNF and IL-1 10 ng/mL) (d) on VEGF-C expression at 24 hours was examined by RT-PCR. Experiments were repeated twice with similar results.
    Wt Ocps, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/wt ocps/product/Millipore
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    wt ocps - by Bioz Stars, 2020-07
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    Image Search Results


    Illustration of the basic components of an ELISA for detection of OCPs and PCBs in environmental samples or extracts. Sample antigen (analyte) competes with antigen for binding sites on coating protein; after a wash step, detection is performed by adding substrate and chromophore

    Journal: Analytical and Bioanalytical Chemistry

    Article Title: Analytical methods for PCBs and organochlorine pesticides in environmental monitoring and surveillance: a critical appraisal

    doi: 10.1007/s00216-006-0765-y

    Figure Lengend Snippet: Illustration of the basic components of an ELISA for detection of OCPs and PCBs in environmental samples or extracts. Sample antigen (analyte) competes with antigen for binding sites on coating protein; after a wash step, detection is performed by adding substrate and chromophore

    Article Snippet: Commercial ELISA kits for detection of PCBs and most OCPs are available from Millipore Corp. (Billerica, MA, USA) and Strategic Diagnostics (Newark, DE, USA).

    Techniques: Enzyme-linked Immunosorbent Assay, Environmental Sampling, Binding Assay

    The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted

    Journal: Biochemistry

    Article Title: Molecular Mechanism of Photoactivation and Structural Location of the Cyanobacterial Orange Carotenoid Protein

    doi: 10.1021/bi401539w

    Figure Lengend Snippet: The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted

    Article Snippet: To separate the resulting PBS-OCP complexes from the unbound OCP after illumination, the sample was loaded onto a 100 kDa filter (Millipore Amicon Centrifugal Filters, Billerica, MA) and centrifuged at 4,000×g at 23 °C for 20 min. Fresh 0.8 M phosphate buffer was applied three times to dilute the retentate.

    Techniques: Binding Assay

    The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted

    Journal: Biochemistry

    Article Title: Molecular Mechanism of Photoactivation and Structural Location of the Cyanobacterial Orange Carotenoid Protein

    doi: 10.1021/bi401539w

    Figure Lengend Snippet: The structural location of the OCP in PBS. (A) The OCP (cyan) binds to the basal cylinder containing both APC 660 trimers and APC 680 . ApcA (light blue), ApcB (wheat), ApcE (raserry). 3D structure of ApcE phycocyanobilin binding domain (raspberry) was predicted

    Article Snippet: To separate the resulting PBS-OCP complexes from the unbound OCP after illumination, the sample was loaded onto a 100 kDa filter (Millipore Amicon Centrifugal Filters, Billerica, MA) and centrifuged at 4,000×g at 23 °C for 20 min. Fresh 0.8 M phosphate buffer was applied three times to dilute the retentate.

    Techniques: Binding Assay

    Tumor necrosis factor (TNF) increases expression of vascular endothelial growth factor-C (VEGF-C) by osteoclast precursors (OCPs). Wild-type (WT) spleen cells were cultured with macrophage colony-stimulating factor (M-CSF) for 3 days to enrich for OCPs. OCPs were cultured in 10% serum with M-CSF and treated with phosphate-buffered saline (PBS) or TNF (10 ng/mL). (a) Expression of VEGF-C and β-actin mRNA was measured by real-time reverse transcription-polymerase chain reaction (RT-PCR) at various times (left panel), and protein levels were measured by Western blot analysis (right panels). (b) Expression of VEGF-A , - B , - C , - D , and placental growth factor ( PLGF ) mRNA was examined in samples treated for 24 hours. The fold increases in TNF-treated over PBS-treated cells at a given time were calculated. Values are the means of triplicate loadings plus standard deviation. The effect of different doses of TNF (c) or a combination with interleukin 1 (IL-1) (TNF and IL-1 10 ng/mL) (d) on VEGF-C expression at 24 hours was examined by RT-PCR. Experiments were repeated twice with similar results.

    Journal: Arthritis Research & Therapy

    Article Title: Increased lymphangiogenesis in joints of mice with inflammatory arthritis

    doi: 10.1186/ar2326

    Figure Lengend Snippet: Tumor necrosis factor (TNF) increases expression of vascular endothelial growth factor-C (VEGF-C) by osteoclast precursors (OCPs). Wild-type (WT) spleen cells were cultured with macrophage colony-stimulating factor (M-CSF) for 3 days to enrich for OCPs. OCPs were cultured in 10% serum with M-CSF and treated with phosphate-buffered saline (PBS) or TNF (10 ng/mL). (a) Expression of VEGF-C and β-actin mRNA was measured by real-time reverse transcription-polymerase chain reaction (RT-PCR) at various times (left panel), and protein levels were measured by Western blot analysis (right panels). (b) Expression of VEGF-A , - B , - C , - D , and placental growth factor ( PLGF ) mRNA was examined in samples treated for 24 hours. The fold increases in TNF-treated over PBS-treated cells at a given time were calculated. Values are the means of triplicate loadings plus standard deviation. The effect of different doses of TNF (c) or a combination with interleukin 1 (IL-1) (TNF and IL-1 10 ng/mL) (d) on VEGF-C expression at 24 hours was examined by RT-PCR. Experiments were repeated twice with similar results.

    Article Snippet: To further confirm the involvement of NF-κB in TNF-induced VEGF-C expression, we treated WT OCPs with an NF-κB inhibitor (Calbiochem, now part of EMD Biosciences, Inc., San Diego, CA, USA) and found that it inhibited TNF-induced VEGF-C expression in a dose-dependent manner (Figure ).

    Techniques: Expressing, Cell Culture, Reverse Transcription Polymerase Chain Reaction, Western Blot, Standard Deviation

    Differential expression of vascular endothelial growth factor ( VEGF ) and platelet-derived growth factor ( PDGF ) family genes in CD11b + /Gr-1 -/lo osteoclast precursors (OCPs) from tumor necrosis factor-transgenic (TNF-Tg) and wild-type (WT) mice. CD11b + /Gr-1 -/lo cells from peripheral blood and bone marrow from TNF-Tg (7 mice per array) and WT (23 mice per array) mice were pooled and purified by flow sorting. The RNA samples were subjected to microarray analysis using the GeneChip mouse genome 430A 2.0 array from Affymetrix. The array data on angiogenic gene expression were analyzed using GeneTraffic software. The expression ratio was calculated by dividing the mean value of the intensity of RNA signals from two separate arrays of TNF-Tg OCPs by that from WT cells.

    Journal: Arthritis Research & Therapy

    Article Title: Increased lymphangiogenesis in joints of mice with inflammatory arthritis

    doi: 10.1186/ar2326

    Figure Lengend Snippet: Differential expression of vascular endothelial growth factor ( VEGF ) and platelet-derived growth factor ( PDGF ) family genes in CD11b + /Gr-1 -/lo osteoclast precursors (OCPs) from tumor necrosis factor-transgenic (TNF-Tg) and wild-type (WT) mice. CD11b + /Gr-1 -/lo cells from peripheral blood and bone marrow from TNF-Tg (7 mice per array) and WT (23 mice per array) mice were pooled and purified by flow sorting. The RNA samples were subjected to microarray analysis using the GeneChip mouse genome 430A 2.0 array from Affymetrix. The array data on angiogenic gene expression were analyzed using GeneTraffic software. The expression ratio was calculated by dividing the mean value of the intensity of RNA signals from two separate arrays of TNF-Tg OCPs by that from WT cells.

    Article Snippet: To further confirm the involvement of NF-κB in TNF-induced VEGF-C expression, we treated WT OCPs with an NF-κB inhibitor (Calbiochem, now part of EMD Biosciences, Inc., San Diego, CA, USA) and found that it inhibited TNF-induced VEGF-C expression in a dose-dependent manner (Figure ).

    Techniques: Expressing, Derivative Assay, Transgenic Assay, Mouse Assay, Purification, Flow Cytometry, Microarray, Software