streptavidin conjugated to alkaline phosphatase  (Thermo Fisher)


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    Name:
    Lab Vision Streptavidin Alkaline Phosphatase Ready To Use
    Description:
    Incubate slides for 10 minutes with Thermo Scientific Lab Vision Streptavidin Alkaline Phospatase Ready to Use reagent for results that will remain stable for 18 months Reagent is intended for use in a labeled streptavidin biotin immunoenzymatic antigen detection system
    Catalog Number:
    ts-125-ap
    Price:
    None
    Applications:
    Anatomical Pathology|Clinical
    Category:
    Lab Reagents and Chemicals
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    Structured Review

    Thermo Fisher streptavidin conjugated to alkaline phosphatase
    Demonstration of an E. cuniculi spore protein that binds Vero host cells. A total E. cuniculi spore protein lysate was generated, biotin labeled, TCA precipitated, and resuspended in DMEM growth medium, which was placed onto Vero host cell monolayers grown in 12-well culture plates. After incubation, the monolayers were washed of unbound protein, and a Western blot of host cell protein lysate was detected with <t>streptavidin-conjugated</t> alkaline phosphatase. The control lanes include biotin-labeled TCA-precipitated (TCA ppt) E. cuniculi spore protein and host cell protein without the addition of biotinylated spore protein. A single 40-kDa E. cuniculi spore protein was detected (arrow).
    Incubate slides for 10 minutes with Thermo Scientific Lab Vision Streptavidin Alkaline Phospatase Ready to Use reagent for results that will remain stable for 18 months Reagent is intended for use in a labeled streptavidin biotin immunoenzymatic antigen detection system
    https://www.bioz.com/result/streptavidin conjugated to alkaline phosphatase/product/Thermo Fisher
    Average 94 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated to alkaline phosphatase - by Bioz Stars, 2020-09
    94/100 stars

    Images

    1) Product Images from "EnP1, a Microsporidian Spore Wall Protein That Enables Spores To Adhere to and Infect Host Cells In Vitro ▿"

    Article Title: EnP1, a Microsporidian Spore Wall Protein That Enables Spores To Adhere to and Infect Host Cells In Vitro ▿

    Journal: Eukaryotic Cell

    doi: 10.1128/EC.00113-07

    Demonstration of an E. cuniculi spore protein that binds Vero host cells. A total E. cuniculi spore protein lysate was generated, biotin labeled, TCA precipitated, and resuspended in DMEM growth medium, which was placed onto Vero host cell monolayers grown in 12-well culture plates. After incubation, the monolayers were washed of unbound protein, and a Western blot of host cell protein lysate was detected with streptavidin-conjugated alkaline phosphatase. The control lanes include biotin-labeled TCA-precipitated (TCA ppt) E. cuniculi spore protein and host cell protein without the addition of biotinylated spore protein. A single 40-kDa E. cuniculi spore protein was detected (arrow).
    Figure Legend Snippet: Demonstration of an E. cuniculi spore protein that binds Vero host cells. A total E. cuniculi spore protein lysate was generated, biotin labeled, TCA precipitated, and resuspended in DMEM growth medium, which was placed onto Vero host cell monolayers grown in 12-well culture plates. After incubation, the monolayers were washed of unbound protein, and a Western blot of host cell protein lysate was detected with streptavidin-conjugated alkaline phosphatase. The control lanes include biotin-labeled TCA-precipitated (TCA ppt) E. cuniculi spore protein and host cell protein without the addition of biotinylated spore protein. A single 40-kDa E. cuniculi spore protein was detected (arrow).

    Techniques Used: Generated, Labeling, Incubation, Western Blot

    2) Product Images from "Host Protein Interactions with the 3? End of Bovine Coronavirus RNA and the Requirement of the Poly(A) Tail for Coronavirus Defective Genome Replication"

    Article Title: Host Protein Interactions with the 3? End of Bovine Coronavirus RNA and the Requirement of the Poly(A) Tail for Coronavirus Defective Genome Replication

    Journal: Journal of Virology

    doi:

    In vitro binding of PABP to coronavirus 3′ UTR RNAs. In vitro-translated luciferase or PABP was incubated with 1 μg of biotinylated BCV3′UTR RNAs containing poly(A) tails of 1, 5, 10, or 68 A residues (A) or MHV3′UTR RNAs containing poly(A) tails of 0, 5, 10, or > 50 A residues (B). Immobilized streptavidin was added to recover biotinylated RNA complexes, and samples were washed to remove any unbound RNA or protein. Samples were analyzed by SDS-PAGE (8% polyacrylamide). M (lanes 1 and 12) denotes marker and corresponds to the input amount of radiolabeled luciferase (lane 1) or PABP (lane 12) in each reaction. Lanes 2 and 7 represent the level of background protein binding in the absence of biotinylated RNA for luciferase (lane 2) and PABP (lane 7). (A) Lanes 3 to 6, luciferase recovered from interaction with BCV3′UTR RNAs; lanes 8 to 11, PABP recovered from interaction with BCV3′UTR RNAs. (B) Lanes 3 to 6, luciferase recovered from interaction with MHV3′UTR RNAs; lanes 8 to 11, PABP recovered from interaction with MHV3′UTR RNAs.
    Figure Legend Snippet: In vitro binding of PABP to coronavirus 3′ UTR RNAs. In vitro-translated luciferase or PABP was incubated with 1 μg of biotinylated BCV3′UTR RNAs containing poly(A) tails of 1, 5, 10, or 68 A residues (A) or MHV3′UTR RNAs containing poly(A) tails of 0, 5, 10, or > 50 A residues (B). Immobilized streptavidin was added to recover biotinylated RNA complexes, and samples were washed to remove any unbound RNA or protein. Samples were analyzed by SDS-PAGE (8% polyacrylamide). M (lanes 1 and 12) denotes marker and corresponds to the input amount of radiolabeled luciferase (lane 1) or PABP (lane 12) in each reaction. Lanes 2 and 7 represent the level of background protein binding in the absence of biotinylated RNA for luciferase (lane 2) and PABP (lane 7). (A) Lanes 3 to 6, luciferase recovered from interaction with BCV3′UTR RNAs; lanes 8 to 11, PABP recovered from interaction with BCV3′UTR RNAs. (B) Lanes 3 to 6, luciferase recovered from interaction with MHV3′UTR RNAs; lanes 8 to 11, PABP recovered from interaction with MHV3′UTR RNAs.

    Techniques Used: In Vitro, Binding Assay, Luciferase, Incubation, SDS Page, Marker, Protein Binding

    Related Articles

    Incubation:

    Article Title: Altering the Cellular Location of an Antigen Expressed by a DNA-Based Vaccine Modulates the Immune Response
    Article Snippet: .. After incubation of 60 min, plates were washed extensively, and streptavidin-alkaline phosphatase (Gibco, Life Technologies, Burlington, Ontario, Canada), diluted to 1/2,000 in PBST-g, was added to each plate. .. Following a 60-min incubation, plates were washed six times in PBST.

    Article Title: Pax2 expression occurs in renal medullary epithelial cells in vivo and in cell culture, is osmoregulated, and promotes osmotic tolerance
    Article Snippet: .. For double labeling, the Pax2-stained sections were incubated overnight at 4°C with rabbit anti-aquaporin 1 water channel (AQP1) antibody (1:400 dilution) or aquaporin 2 water channel (AQP2) (1:600 dilution) (both from M. Knepper, National Institutes of Health), followed by biotinylated secondary antibody (anti-rabbit IgG), as above, and alkaline phosphatase-conjugated streptavidin (Zymed). ..

    Article Title: The resveratrol analogue, 2,3?,4,5?-tetramethoxystilbene, does not inhibit CYP gene expression, enzyme activity and benzo[a]pyrene-DNA adduct formation in MCF-7 cells exposed to benzo[a]pyrene
    Article Snippet: .. After adding samples and standards to wells, plates were incubated at 37°C for 90 min followed by washing with PBST and incubation with biotinylated anti-rabbit antibody (1:2500; Jackson ImmunoResearch Laboratories, West Grove, PA, USA) in PBST containing casein (0.25%) at room temperature for 60 min. After washing, plates were incubated with streptavidin alkaline phosphatase (1:5000; Avidix-AP; Applied Biosystems) in PBST containing casein (0.25%) at room temperature for 60 min. Plates were subsequently washed eight times with PBST, once with distilled water and three times with Tris buffer (20 mM Tris and 1 mM MgCl2 , pH 9.5) before addition of CDP Star with Emerald II solution (Applied Biosystems). .. After overnight incubation at 4°C, plates were brought to room temperature and luminescence was read using a Tropix 717 Microplate Luminometer (Applied Biosystems).

    Labeling:

    Article Title: Pax2 expression occurs in renal medullary epithelial cells in vivo and in cell culture, is osmoregulated, and promotes osmotic tolerance
    Article Snippet: .. For double labeling, the Pax2-stained sections were incubated overnight at 4°C with rabbit anti-aquaporin 1 water channel (AQP1) antibody (1:400 dilution) or aquaporin 2 water channel (AQP2) (1:600 dilution) (both from M. Knepper, National Institutes of Health), followed by biotinylated secondary antibody (anti-rabbit IgG), as above, and alkaline phosphatase-conjugated streptavidin (Zymed). ..

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    Thermo Fisher streptavidin conjugated to alkaline phosphatase
    Streptavidin Conjugated To Alkaline Phosphatase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated to alkaline phosphatase/product/Thermo Fisher
    Average 99 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated to alkaline phosphatase - by Bioz Stars, 2020-09
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    93
    Thermo Fisher streptavidin conjugated alkaline phosphatase sav alp
    Schematic illustration of tdEV sensing using a sandwich immunoassay and redox cycling on nIDEs resulting in a two-level selectivity and a two-level amplification. tdEVs are captured using C-AE tethered to electrodes (first level of selectivity). The binding of R-AE to the tdEVs completes the antibody–antigen-antibody sandwich (second-level selectivity), after which the enzyme <t>ALP</t> is introduced using a <t>biotin–SAV</t> interaction. ALP provides an enzymatic amplification of pAPP to pAP by substrate cleavage (first-level amplification), which is followed by an electrochemical signal amplification via the oxidation of pAP to pQI and subsequent redox cycling thereof between the nIDE electrodes (second-level amplification).
    Streptavidin Conjugated Alkaline Phosphatase Sav Alp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated alkaline phosphatase sav alp/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated alkaline phosphatase sav alp - by Bioz Stars, 2020-09
    93/100 stars
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    84
    prozyme alkaline phosphatase conjugated streptavidin sa ap
    Detection of PD-1 and PD-L1 expression on canine cell lines. (A) PD-1 expression on CLGL-90 cells was detected with JC053 hybridoma culture supernatant. Biotinylated anti-mouse IgA and FITC-conjugated <t>streptavidin</t> was used. Mouse IgA isotype control was used as negative control. Light gray is for isotype control and dark gray is for JC053. (B) Four purified anti-PD-L1s were compared in their capacity to bind activated DH82 cells. DH82 cells were cultivated either with or without 10ng/ml IFN-γ and JC071, JC173, JC194, and JC205 binding to PD-L1 was assessed. Histograms show unstimulated DH82 without anti-PD-L1 (light gray), unstimulated DH82 with anti-PD-L1 (medium gray), and IFN-γ stimulated DH82 with anti-PD-L1 (dark gray), respectively. FITC conjugated Anti-Mouse IgG was used with all samples including no anti-PD-L1 sample, as secondary antibody. PD-1 or PD-L1 positive population was selected following FSC, SSC gating, single cell gating, and live cell gating.
    Alkaline Phosphatase Conjugated Streptavidin Sa Ap, supplied by prozyme, 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/alkaline phosphatase conjugated streptavidin sa ap/product/prozyme
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    alkaline phosphatase conjugated streptavidin sa ap - by Bioz Stars, 2020-09
    84/100 stars
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    Image Search Results


    Schematic illustration of tdEV sensing using a sandwich immunoassay and redox cycling on nIDEs resulting in a two-level selectivity and a two-level amplification. tdEVs are captured using C-AE tethered to electrodes (first level of selectivity). The binding of R-AE to the tdEVs completes the antibody–antigen-antibody sandwich (second-level selectivity), after which the enzyme ALP is introduced using a biotin–SAV interaction. ALP provides an enzymatic amplification of pAPP to pAP by substrate cleavage (first-level amplification), which is followed by an electrochemical signal amplification via the oxidation of pAP to pQI and subsequent redox cycling thereof between the nIDE electrodes (second-level amplification).

    Journal: Nano Letters

    Article Title: Electrochemical Detection of Tumor-Derived Extracellular Vesicles on Nanointerdigitated Electrodes

    doi: 10.1021/acs.nanolett.9b02741

    Figure Lengend Snippet: Schematic illustration of tdEV sensing using a sandwich immunoassay and redox cycling on nIDEs resulting in a two-level selectivity and a two-level amplification. tdEVs are captured using C-AE tethered to electrodes (first level of selectivity). The binding of R-AE to the tdEVs completes the antibody–antigen-antibody sandwich (second-level selectivity), after which the enzyme ALP is introduced using a biotin–SAV interaction. ALP provides an enzymatic amplification of pAPP to pAP by substrate cleavage (first-level amplification), which is followed by an electrochemical signal amplification via the oxidation of pAP to pQI and subsequent redox cycling thereof between the nIDE electrodes (second-level amplification).

    Article Snippet: Streptavidin-conjugated alkaline phosphatase (SAV-ALP) was purchased from Thermo Fisher (Eindhoven, The Netherlands).

    Techniques: Amplification, Binding Assay

    Detection of PD-1 and PD-L1 expression on canine cell lines. (A) PD-1 expression on CLGL-90 cells was detected with JC053 hybridoma culture supernatant. Biotinylated anti-mouse IgA and FITC-conjugated streptavidin was used. Mouse IgA isotype control was used as negative control. Light gray is for isotype control and dark gray is for JC053. (B) Four purified anti-PD-L1s were compared in their capacity to bind activated DH82 cells. DH82 cells were cultivated either with or without 10ng/ml IFN-γ and JC071, JC173, JC194, and JC205 binding to PD-L1 was assessed. Histograms show unstimulated DH82 without anti-PD-L1 (light gray), unstimulated DH82 with anti-PD-L1 (medium gray), and IFN-γ stimulated DH82 with anti-PD-L1 (dark gray), respectively. FITC conjugated Anti-Mouse IgG was used with all samples including no anti-PD-L1 sample, as secondary antibody. PD-1 or PD-L1 positive population was selected following FSC, SSC gating, single cell gating, and live cell gating.

    Journal: PLoS ONE

    Article Title: Development of canine PD-1/PD-L1 specific monoclonal antibodies and amplification of canine T cell function

    doi: 10.1371/journal.pone.0235518

    Figure Lengend Snippet: Detection of PD-1 and PD-L1 expression on canine cell lines. (A) PD-1 expression on CLGL-90 cells was detected with JC053 hybridoma culture supernatant. Biotinylated anti-mouse IgA and FITC-conjugated streptavidin was used. Mouse IgA isotype control was used as negative control. Light gray is for isotype control and dark gray is for JC053. (B) Four purified anti-PD-L1s were compared in their capacity to bind activated DH82 cells. DH82 cells were cultivated either with or without 10ng/ml IFN-γ and JC071, JC173, JC194, and JC205 binding to PD-L1 was assessed. Histograms show unstimulated DH82 without anti-PD-L1 (light gray), unstimulated DH82 with anti-PD-L1 (medium gray), and IFN-γ stimulated DH82 with anti-PD-L1 (dark gray), respectively. FITC conjugated Anti-Mouse IgG was used with all samples including no anti-PD-L1 sample, as secondary antibody. PD-1 or PD-L1 positive population was selected following FSC, SSC gating, single cell gating, and live cell gating.

    Article Snippet: The transferred membrane was blocked with 5% skim milk, incubated with alkaline phosphatase conjugated streptavidin (SA-AP), and developed using NBT/BCIP (Thermo Fisher Scientific) as a substrate.

    Techniques: Expressing, Negative Control, Purification, Binding Assay

    Evaluation of blocking activity by anti-canine PD-1 and PD-L1 antibodies. Antibodies were screened for their opposite ligand blocking capability. Hybridoma supernatants were added to ELISA plates coated with unbiotinylated PD-1Ig (A) or PD-L1Ig (B). After washing, biotinylated PD-L1Ig (A) or PD-1Ig (B) was used to detect blocking capacity of anti-PD-1 (A) and anti-PD-L1 (B) using HRP conjugated streptavidin to detect unblocked protein. All samples were assayed in duplicates. Each value is presented as mean ± standard deviation. In (A), JC053 value was significantly different from the rest of anti-PD-1 hybridomas with P value of 0.0002. In (B), JC071, JC173, JC194, and JC205 values were significantly different from PBS and medium values with P values less than 0.0001.

    Journal: PLoS ONE

    Article Title: Development of canine PD-1/PD-L1 specific monoclonal antibodies and amplification of canine T cell function

    doi: 10.1371/journal.pone.0235518

    Figure Lengend Snippet: Evaluation of blocking activity by anti-canine PD-1 and PD-L1 antibodies. Antibodies were screened for their opposite ligand blocking capability. Hybridoma supernatants were added to ELISA plates coated with unbiotinylated PD-1Ig (A) or PD-L1Ig (B). After washing, biotinylated PD-L1Ig (A) or PD-1Ig (B) was used to detect blocking capacity of anti-PD-1 (A) and anti-PD-L1 (B) using HRP conjugated streptavidin to detect unblocked protein. All samples were assayed in duplicates. Each value is presented as mean ± standard deviation. In (A), JC053 value was significantly different from the rest of anti-PD-1 hybridomas with P value of 0.0002. In (B), JC071, JC173, JC194, and JC205 values were significantly different from PBS and medium values with P values less than 0.0001.

    Article Snippet: The transferred membrane was blocked with 5% skim milk, incubated with alkaline phosphatase conjugated streptavidin (SA-AP), and developed using NBT/BCIP (Thermo Fisher Scientific) as a substrate.

    Techniques: Blocking Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Expression of recombinant PD-1Ig and PD-L1Ig in D . melanogaster S2 cells. Expression of monomers was tested by Western blot. Biotinylated PD-1Ig and PD-L1Ig were expressed and secreted from D . melanogaster S2 cells. S2 cell culture supernatant expressing PD-1Ig (lane 2) or PD-L1Ig (lane 3) was analyzed against vector only control (lane 1) on Western blot in reducing condition. Alkaline phosphatase conjugated streptavidin was used to detect proteins.

    Journal: PLoS ONE

    Article Title: Development of canine PD-1/PD-L1 specific monoclonal antibodies and amplification of canine T cell function

    doi: 10.1371/journal.pone.0235518

    Figure Lengend Snippet: Expression of recombinant PD-1Ig and PD-L1Ig in D . melanogaster S2 cells. Expression of monomers was tested by Western blot. Biotinylated PD-1Ig and PD-L1Ig were expressed and secreted from D . melanogaster S2 cells. S2 cell culture supernatant expressing PD-1Ig (lane 2) or PD-L1Ig (lane 3) was analyzed against vector only control (lane 1) on Western blot in reducing condition. Alkaline phosphatase conjugated streptavidin was used to detect proteins.

    Article Snippet: The transferred membrane was blocked with 5% skim milk, incubated with alkaline phosphatase conjugated streptavidin (SA-AP), and developed using NBT/BCIP (Thermo Fisher Scientific) as a substrate.

    Techniques: Expressing, Recombinant, Western Blot, Cell Culture, Plasmid Preparation

    Detection of PD-1 and PD-L1 expression on CHO cells expressing canine markers. Antibody specificity toward PD-1 and PD-L1 by anti-PD-1 (JC053) and anti-PD-L1s (JC071, JC173, JC194, and JC205) was tested on CHO cells by flow cytometry. (A) Anti-PD-1 and anti-PD-L1 bind to CHO-PD1 and CHO-PDL1, respectively, while they do not bind to untransfected CHO-K1. PD-1 positive population were selected following FSC, SSC gating, single cell gating, and live cell gating. PD-L1 positive population was selected following FSC, SSC gating, and single cell gating. (B) JC053, an anti-PD-1 antibody, was compared to a mouse IgA isotype control for staining CHO-PD1. Biotinylated anti-mouse IgA and APC conjugated streptavidin was used following primary antibody staining. A population of CHO-PD1 cells was selected on FSC and SSC gating. Single cells were selected and dead cells were excluded. Then, PD-1 positive cells are shown on histograms. Anti-PD-L1s were conjugated with PE and used to stain CHO-PDL1 cells. Appropriate isotype controls were included and anti-mouse IgG1 and anti-mouse IgG2a were used in combination with PE conjugated streptavidin. PE positive population is shown on histograms following FSC/SSC gating, single cell selection, and exclusion of dead cells.

    Journal: PLoS ONE

    Article Title: Development of canine PD-1/PD-L1 specific monoclonal antibodies and amplification of canine T cell function

    doi: 10.1371/journal.pone.0235518

    Figure Lengend Snippet: Detection of PD-1 and PD-L1 expression on CHO cells expressing canine markers. Antibody specificity toward PD-1 and PD-L1 by anti-PD-1 (JC053) and anti-PD-L1s (JC071, JC173, JC194, and JC205) was tested on CHO cells by flow cytometry. (A) Anti-PD-1 and anti-PD-L1 bind to CHO-PD1 and CHO-PDL1, respectively, while they do not bind to untransfected CHO-K1. PD-1 positive population were selected following FSC, SSC gating, single cell gating, and live cell gating. PD-L1 positive population was selected following FSC, SSC gating, and single cell gating. (B) JC053, an anti-PD-1 antibody, was compared to a mouse IgA isotype control for staining CHO-PD1. Biotinylated anti-mouse IgA and APC conjugated streptavidin was used following primary antibody staining. A population of CHO-PD1 cells was selected on FSC and SSC gating. Single cells were selected and dead cells were excluded. Then, PD-1 positive cells are shown on histograms. Anti-PD-L1s were conjugated with PE and used to stain CHO-PDL1 cells. Appropriate isotype controls were included and anti-mouse IgG1 and anti-mouse IgG2a were used in combination with PE conjugated streptavidin. PE positive population is shown on histograms following FSC/SSC gating, single cell selection, and exclusion of dead cells.

    Article Snippet: The transferred membrane was blocked with 5% skim milk, incubated with alkaline phosphatase conjugated streptavidin (SA-AP), and developed using NBT/BCIP (Thermo Fisher Scientific) as a substrate.

    Techniques: Expressing, Flow Cytometry, Staining, Selection