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  • 99
    Thermo Fisher streptavidin agarose beads
    Streptavidin Agarose Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin agarose beads/product/Thermo Fisher
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    86
    Millipore streptavidin agarose beads
    The amino acid residues of TRPM5 corresponding to those forming the Ca 2+ -binding site of TRPM4 were also necessary for the normal Ca 2+ -sensitivity of rTRPM5. ( A ) Numbers of corresponding amino acids of rTRPM5 are labeled in the illustration of the Ca 2+ -binding site of hTRPM4. ( B ) CRCs for the effect of Ca 2+ on the current densities mediated by WT rTRPM5 (black circles), D802A (red squares), N805D (dark red triangles), Q782A (green diamonds), D808E (dark yellow circles), E779D (dark yellow horizontal bars), E779Q (purple open diamonds), N805A (light green asterisks), D808N (brown crosses) and the empty vector (gray circles) ( n = 3 or 4 each). ( C ) A result of surface biotinylation assay. The proteins of rTRPM5 expressed in the plasma membrane were biotinylated and precipitated with <t>streptavidin</t> beads (Surface). Non-precipitated fractions contain intracellular proteins (Intracellular). ( D ) Signal ratios of the surface rTRPM5 to the intracellular rTRPM5 as an indication of the surface expression levels of rTRPM5. The mutants showed similar surface expression levels to WT rTRPM5 ( n = 3).
    Streptavidin Agarose Beads, supplied by Millipore, 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/streptavidin agarose beads/product/Millipore
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    Price from $9.99 to $1999.99
    streptavidin agarose beads - by Bioz Stars, 2021-07
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    86
    GE Healthcare streptavidin sepharose beads
    Nutrient starvation upregulates nSMase2. PC12 cells were starved with HBSS for the indicated times. a Induction of autophagy by nutrient starvation in PC12 cells. Degradation of p62 and LC3 turnover were detected by immunoblotting for assessing autophagic flux. For LC3 turnover assays, cells were starved with HBSS with or without 50 μM CQ for the indicated times. b Activation of nSMase2 by starvation. Specific activity of nSMase2 was analyzed using [ 14 C]-labeled sphingomyelin. c Increase in nSMase2 expression by starvation. Protein expression levels of nSMase2 in starved cells were determined by immunoblotting and were normalized to β-actin levels. d No changes in nSMase2 mRNA levels were induced by starvation. The mRNA levels of nSMase2 were measured by quantitative real-time PCR and were normalized to Hprt1 . e Starvation-induced phosphorylation of nSMase2 at a serine residue. PC12 cells were starved with HBSS for the indicated time, and cell lysates were incubated with biotin-conjugated sphingomyelin (the nSMase2 substrate) followed by pull-down with <t>streptavidin-sepharose</t> beads. The pellets were analyzed using immunoblots to detect serine phosphorylation of nSMase2. The data are presented as the mean ± SEM of three independent experiments. Significant differences, * p
    Streptavidin Sepharose Beads, supplied by GE Healthcare, 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/streptavidin sepharose beads/product/GE Healthcare
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin sepharose beads - by Bioz Stars, 2021-07
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    99
    Thermo Fisher streptavidin coated magnetic beads
    Isolation and enumeration of CTCs from non-small cell lung cancer (NSCLC) patients: ( A ) the detailed GenoCTC workflow using clinical samples is summarized as follows: (1) Whole blood is drawn from cancer patients. (2) The biotinylated anti-EPCAM antibody is conjugated with 1 μm <t>streptavidin-coated</t> magnetic nanobeads. (3) Anti-EPCAM antibody-coated beads and whole blood are incubated together, and the nanobeads will specifically bind onto EPCAM-positive cells. (4) EPCAM-positive cells are isolated using GenoCTC with a disposable GenoChip. (5) Molecular analysis is conducted in various ways using isolated EPCAM-positive cells. ( B ) Representative fluorescent images of isolated EPCAM-positive cells from three NSCLC patients are shown. Cells were immunostained with DAPI for nuclear staining (blue), an anti-cytokeratin 18 (CK18) antibody for CTCs (Alexa flour 488; Green), and an anti-CD45 antibody for leukocytes (Alexa 594; red). ( C ) EPCAM-positive cells isolated from the whole blood of 10 NSCLC patients were enumerated, and the number of cells observed varied between patients. EPCAM-positive cell counts ranged from 2 to 112 in 3.5 mL of whole blood, and the average count of the cells was 20.75, showing 95% confidence. The orange shaded area show the serial assessment of CTCs from those patients. The grey arrows indicate the clinical changes in the disease status determined by a physician. SD: stable disease, PR: partial response, PD: progressive disease. The orange arrows indicate the increase or decrease in CTC counts during the serial assessment.
    Streptavidin Coated Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin coated magnetic beads/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin coated magnetic beads - by Bioz Stars, 2021-07
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    Image Search Results


    The amino acid residues of TRPM5 corresponding to those forming the Ca 2+ -binding site of TRPM4 were also necessary for the normal Ca 2+ -sensitivity of rTRPM5. ( A ) Numbers of corresponding amino acids of rTRPM5 are labeled in the illustration of the Ca 2+ -binding site of hTRPM4. ( B ) CRCs for the effect of Ca 2+ on the current densities mediated by WT rTRPM5 (black circles), D802A (red squares), N805D (dark red triangles), Q782A (green diamonds), D808E (dark yellow circles), E779D (dark yellow horizontal bars), E779Q (purple open diamonds), N805A (light green asterisks), D808N (brown crosses) and the empty vector (gray circles) ( n = 3 or 4 each). ( C ) A result of surface biotinylation assay. The proteins of rTRPM5 expressed in the plasma membrane were biotinylated and precipitated with streptavidin beads (Surface). Non-precipitated fractions contain intracellular proteins (Intracellular). ( D ) Signal ratios of the surface rTRPM5 to the intracellular rTRPM5 as an indication of the surface expression levels of rTRPM5. The mutants showed similar surface expression levels to WT rTRPM5 ( n = 3).

    Journal: International Journal of Molecular Sciences

    Article Title: TRPM4 and TRPM5 Channels Share Crucial Amino Acid Residues for Ca2+ Sensitivity but Not Significance of PI(4,5)P2

    doi: 10.3390/ijms20082012

    Figure Lengend Snippet: The amino acid residues of TRPM5 corresponding to those forming the Ca 2+ -binding site of TRPM4 were also necessary for the normal Ca 2+ -sensitivity of rTRPM5. ( A ) Numbers of corresponding amino acids of rTRPM5 are labeled in the illustration of the Ca 2+ -binding site of hTRPM4. ( B ) CRCs for the effect of Ca 2+ on the current densities mediated by WT rTRPM5 (black circles), D802A (red squares), N805D (dark red triangles), Q782A (green diamonds), D808E (dark yellow circles), E779D (dark yellow horizontal bars), E779Q (purple open diamonds), N805A (light green asterisks), D808N (brown crosses) and the empty vector (gray circles) ( n = 3 or 4 each). ( C ) A result of surface biotinylation assay. The proteins of rTRPM5 expressed in the plasma membrane were biotinylated and precipitated with streptavidin beads (Surface). Non-precipitated fractions contain intracellular proteins (Intracellular). ( D ) Signal ratios of the surface rTRPM5 to the intracellular rTRPM5 as an indication of the surface expression levels of rTRPM5. The mutants showed similar surface expression levels to WT rTRPM5 ( n = 3).

    Article Snippet: Streptavidin-agarose beads (Sigma-Aldrich) were added to the protein extracts.

    Techniques: Binding Assay, Labeling, Plasmid Preparation, Surface Biotinylation Assay, Expressing

    The mutations of the negatively-charged amino acid residues near and in the TRP domain reduced the Ca 2+ -sensitivity of rTRPM5. ( A ) Positions of the acidic amino acid residues (Asp 987 (D987) and Glu 1000 (E1000)) which were mutated. (Upper) The predicted membrane topology of rTRPM5 and the position of TRP domain in the C-terminal tail. (Lower) An alignment of amino acid sequences around the TRP domain of rat TRPM (rTRPM) channels. The aspartate and the glutamate of rTRPM5 are conserved in rTRPM4 (GenBank #NP_001129701.1), rTRPM2 (NP_001011559.1) and rTRPM8 (NP_599198.2) but not in rTRPM1 (NP_001032823.1), rTRPM3 (NP_001178491.1), rTRPM6 (XP_006223728.1) nor rTRPM7 (NP_446157.2). ( B ) CRCs for the effect of Ca 2+ on the rTRPM5 current densities at +100 mV. EC 50 for Ca 2+ of WT rTRPM5 and D987N mutant were 3.25 and 196 µM, respectively. EC 50 for Ca 2+ of E1000Q was unable to be estimated but it seems to be at least more than 100 µM. ( C ) A result of a biotinylation assay in order to evaluate the surface expression level of rTRPM5. The proteins of rTRPM5 and EGFP were detected by Western blotting. The biotinylated rTRPM5 (biotin+, Surface) is indicative of rTRPM5 which was expressed in the plasma membrane. Expression levels of EGFP in the intracellular fractions indicate the transfection efficiencies, and no signal of EGFP in the surface fractions indicates that intracellular proteins were not biotinylated. In order to monitor nonspecific binding, lysates of cells which were not treated with biotin were also subjected to precipitations with the streptavidin-agarose beads (biotin−). ( D ) Signal ratios of the surface rTRPM5 to the intracellular rTRPM5 as an indication of the surface expression levels of rTRPM5. The expression levels of WT rTRPM5 and mutants did not differ significantly ( n = 3).

    Journal: International Journal of Molecular Sciences

    Article Title: TRPM4 and TRPM5 Channels Share Crucial Amino Acid Residues for Ca2+ Sensitivity but Not Significance of PI(4,5)P2

    doi: 10.3390/ijms20082012

    Figure Lengend Snippet: The mutations of the negatively-charged amino acid residues near and in the TRP domain reduced the Ca 2+ -sensitivity of rTRPM5. ( A ) Positions of the acidic amino acid residues (Asp 987 (D987) and Glu 1000 (E1000)) which were mutated. (Upper) The predicted membrane topology of rTRPM5 and the position of TRP domain in the C-terminal tail. (Lower) An alignment of amino acid sequences around the TRP domain of rat TRPM (rTRPM) channels. The aspartate and the glutamate of rTRPM5 are conserved in rTRPM4 (GenBank #NP_001129701.1), rTRPM2 (NP_001011559.1) and rTRPM8 (NP_599198.2) but not in rTRPM1 (NP_001032823.1), rTRPM3 (NP_001178491.1), rTRPM6 (XP_006223728.1) nor rTRPM7 (NP_446157.2). ( B ) CRCs for the effect of Ca 2+ on the rTRPM5 current densities at +100 mV. EC 50 for Ca 2+ of WT rTRPM5 and D987N mutant were 3.25 and 196 µM, respectively. EC 50 for Ca 2+ of E1000Q was unable to be estimated but it seems to be at least more than 100 µM. ( C ) A result of a biotinylation assay in order to evaluate the surface expression level of rTRPM5. The proteins of rTRPM5 and EGFP were detected by Western blotting. The biotinylated rTRPM5 (biotin+, Surface) is indicative of rTRPM5 which was expressed in the plasma membrane. Expression levels of EGFP in the intracellular fractions indicate the transfection efficiencies, and no signal of EGFP in the surface fractions indicates that intracellular proteins were not biotinylated. In order to monitor nonspecific binding, lysates of cells which were not treated with biotin were also subjected to precipitations with the streptavidin-agarose beads (biotin−). ( D ) Signal ratios of the surface rTRPM5 to the intracellular rTRPM5 as an indication of the surface expression levels of rTRPM5. The expression levels of WT rTRPM5 and mutants did not differ significantly ( n = 3).

    Article Snippet: Streptavidin-agarose beads (Sigma-Aldrich) were added to the protein extracts.

    Techniques: Mutagenesis, Cell Surface Biotinylation Assay, Expressing, Western Blot, Transfection, Binding Assay

    Nutrient starvation upregulates nSMase2. PC12 cells were starved with HBSS for the indicated times. a Induction of autophagy by nutrient starvation in PC12 cells. Degradation of p62 and LC3 turnover were detected by immunoblotting for assessing autophagic flux. For LC3 turnover assays, cells were starved with HBSS with or without 50 μM CQ for the indicated times. b Activation of nSMase2 by starvation. Specific activity of nSMase2 was analyzed using [ 14 C]-labeled sphingomyelin. c Increase in nSMase2 expression by starvation. Protein expression levels of nSMase2 in starved cells were determined by immunoblotting and were normalized to β-actin levels. d No changes in nSMase2 mRNA levels were induced by starvation. The mRNA levels of nSMase2 were measured by quantitative real-time PCR and were normalized to Hprt1 . e Starvation-induced phosphorylation of nSMase2 at a serine residue. PC12 cells were starved with HBSS for the indicated time, and cell lysates were incubated with biotin-conjugated sphingomyelin (the nSMase2 substrate) followed by pull-down with streptavidin-sepharose beads. The pellets were analyzed using immunoblots to detect serine phosphorylation of nSMase2. The data are presented as the mean ± SEM of three independent experiments. Significant differences, * p

    Journal: Cell Death & Disease

    Article Title: Activation of neutral sphingomyelinase 2 by starvation induces cell-protective autophagy via an increase in Golgi-localized ceramide

    doi: 10.1038/s41419-018-0709-4

    Figure Lengend Snippet: Nutrient starvation upregulates nSMase2. PC12 cells were starved with HBSS for the indicated times. a Induction of autophagy by nutrient starvation in PC12 cells. Degradation of p62 and LC3 turnover were detected by immunoblotting for assessing autophagic flux. For LC3 turnover assays, cells were starved with HBSS with or without 50 μM CQ for the indicated times. b Activation of nSMase2 by starvation. Specific activity of nSMase2 was analyzed using [ 14 C]-labeled sphingomyelin. c Increase in nSMase2 expression by starvation. Protein expression levels of nSMase2 in starved cells were determined by immunoblotting and were normalized to β-actin levels. d No changes in nSMase2 mRNA levels were induced by starvation. The mRNA levels of nSMase2 were measured by quantitative real-time PCR and were normalized to Hprt1 . e Starvation-induced phosphorylation of nSMase2 at a serine residue. PC12 cells were starved with HBSS for the indicated time, and cell lysates were incubated with biotin-conjugated sphingomyelin (the nSMase2 substrate) followed by pull-down with streptavidin-sepharose beads. The pellets were analyzed using immunoblots to detect serine phosphorylation of nSMase2. The data are presented as the mean ± SEM of three independent experiments. Significant differences, * p

    Article Snippet: Sequentially, streptavidin-Sepharose beads (GE Healthcare, Buckinghamshire, UK, #71-5004-40 AE) was added to the samples and incubated on a rocker overnight at 4 °C.

    Techniques: Activation Assay, Activity Assay, Labeling, Expressing, Real-time Polymerase Chain Reaction, Incubation, Western Blot

    Isolation and enumeration of CTCs from non-small cell lung cancer (NSCLC) patients: ( A ) the detailed GenoCTC workflow using clinical samples is summarized as follows: (1) Whole blood is drawn from cancer patients. (2) The biotinylated anti-EPCAM antibody is conjugated with 1 μm streptavidin-coated magnetic nanobeads. (3) Anti-EPCAM antibody-coated beads and whole blood are incubated together, and the nanobeads will specifically bind onto EPCAM-positive cells. (4) EPCAM-positive cells are isolated using GenoCTC with a disposable GenoChip. (5) Molecular analysis is conducted in various ways using isolated EPCAM-positive cells. ( B ) Representative fluorescent images of isolated EPCAM-positive cells from three NSCLC patients are shown. Cells were immunostained with DAPI for nuclear staining (blue), an anti-cytokeratin 18 (CK18) antibody for CTCs (Alexa flour 488; Green), and an anti-CD45 antibody for leukocytes (Alexa 594; red). ( C ) EPCAM-positive cells isolated from the whole blood of 10 NSCLC patients were enumerated, and the number of cells observed varied between patients. EPCAM-positive cell counts ranged from 2 to 112 in 3.5 mL of whole blood, and the average count of the cells was 20.75, showing 95% confidence. The orange shaded area show the serial assessment of CTCs from those patients. The grey arrows indicate the clinical changes in the disease status determined by a physician. SD: stable disease, PR: partial response, PD: progressive disease. The orange arrows indicate the increase or decrease in CTC counts during the serial assessment.

    Journal: Micromachines

    Article Title: An Immune–Magnetophoretic Device for the Selective and Precise Enrichment of Circulating Tumor Cells from Whole Blood

    doi: 10.3390/mi11060560

    Figure Lengend Snippet: Isolation and enumeration of CTCs from non-small cell lung cancer (NSCLC) patients: ( A ) the detailed GenoCTC workflow using clinical samples is summarized as follows: (1) Whole blood is drawn from cancer patients. (2) The biotinylated anti-EPCAM antibody is conjugated with 1 μm streptavidin-coated magnetic nanobeads. (3) Anti-EPCAM antibody-coated beads and whole blood are incubated together, and the nanobeads will specifically bind onto EPCAM-positive cells. (4) EPCAM-positive cells are isolated using GenoCTC with a disposable GenoChip. (5) Molecular analysis is conducted in various ways using isolated EPCAM-positive cells. ( B ) Representative fluorescent images of isolated EPCAM-positive cells from three NSCLC patients are shown. Cells were immunostained with DAPI for nuclear staining (blue), an anti-cytokeratin 18 (CK18) antibody for CTCs (Alexa flour 488; Green), and an anti-CD45 antibody for leukocytes (Alexa 594; red). ( C ) EPCAM-positive cells isolated from the whole blood of 10 NSCLC patients were enumerated, and the number of cells observed varied between patients. EPCAM-positive cell counts ranged from 2 to 112 in 3.5 mL of whole blood, and the average count of the cells was 20.75, showing 95% confidence. The orange shaded area show the serial assessment of CTCs from those patients. The grey arrows indicate the clinical changes in the disease status determined by a physician. SD: stable disease, PR: partial response, PD: progressive disease. The orange arrows indicate the increase or decrease in CTC counts during the serial assessment.

    Article Snippet: Preparation of Antibody-Coated Magnetic Microbeads Magnetic microbead-conjugated antibodies for CTC isolation were prepared in phosphate-buffered saline (PBS; Gibco, Thermo Fisher Scientific, Inc., Waltham, MA, USA) by incubation of biotinylated anti-human EPCAM (eBioscience, Thermo Fisher Scientific, Inc.), biotinylated anti-human vimentin (R & D systems, Biotechne., Minneapolis, MN, USA), or biotinylated anti-human MET (eBioscience, Thermo Fisher Scientific, Inc.) with streptavidin-coated magnetic beads (Size 1 µm) (Dynabead, Invitrogen, Carlsbad, CA, USA) for 1 h at room temperature.

    Techniques: Isolation, Incubation, Staining