streptavidin conjugated alkaline phosphatase  (Vector Laboratories)


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    Name:
    Streptavidin
    Description:
    Vector s Streptavidin is isolated from Streptomyces avidinii by a specific affinity system which results in a homogeneous ultrapure streptavidin with very low nonspecific binding characteristics Unconjugated streptavidin is recommended for use in solid phase assays and immunohistochemical applications when the technique of sequential addition of reagents sandwich technique is employed This reagent has also been effectively employed in subtractive hybridization procedures
    Catalog Number:
    sa-5000
    Price:
    None
    Size:
    1 mg
    Category:
    Protein chemifluorescent detection reagents or kits or substrates
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    Structured Review

    Vector Laboratories streptavidin conjugated alkaline phosphatase
    Streptavidin
    Vector s Streptavidin is isolated from Streptomyces avidinii by a specific affinity system which results in a homogeneous ultrapure streptavidin with very low nonspecific binding characteristics Unconjugated streptavidin is recommended for use in solid phase assays and immunohistochemical applications when the technique of sequential addition of reagents sandwich technique is employed This reagent has also been effectively employed in subtractive hybridization procedures
    https://www.bioz.com/result/streptavidin conjugated alkaline phosphatase/product/Vector Laboratories
    Average 98 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated alkaline phosphatase - by Bioz Stars, 2020-09
    98/100 stars

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    Related Articles

    Immunostaining:

    Article Title: Phosphatidylethanolamine dynamics are required for osteoclast fusion
    Article Snippet: .. Immunostaining was performed with a FITC-conjugated anti-streptavidin antibody (Vector Laboratories). .. F-actin was stained using Alexa Fluor 594-conjugated phalloidin (Molecular Probes).

    Enzyme-linked Immunosorbent Assay:

    Article Title: A novel LRP1-binding peptide L57 that crosses the blood brain barrier
    Article Snippet: .. 2.2 Evaluation of phage- or synthetic peptide-binding to recombinant proteins by plate ELISA The wells of a Nunc Maxisorp microplate (460−518) were coated with an anti-human Fc goat polyclonal antibody (10 μg/mL) (Jackson ImmunoResearch, West Grove, PA, USA) at 4 °C overnight and then blocked with 0.5% BSA in PBS at room temperature for 2 h. Fc-fused proteins (1 μg/mL) were captured by the antibody, and phage solution (1.0 × 1011 pfu/mL) or biotinylated peptide solution was added to the wells and incubated at room temperature for 1 h. After three times washing with PBST, bound phages or peptides were detected using horseradish peroxidase (HRP)-conjugated anti-T7 antibody (5000-fold dilution in PBS with 0.5% BSA) (Merck Millipore) and HRP-conjugated streptavidin (1000-fold dilution in PBS with 0.5% BSA) (Vector Laboratories Inc., Burlingame, CA, USA), respectively. .. The amount of HRP in each well was measured colorimetrically with the chromogenic reagent tetramethylbenzidine (Wako, Osaka, Japan).

    Incubation:

    Article Title: A novel LRP1-binding peptide L57 that crosses the blood brain barrier
    Article Snippet: .. 2.2 Evaluation of phage- or synthetic peptide-binding to recombinant proteins by plate ELISA The wells of a Nunc Maxisorp microplate (460−518) were coated with an anti-human Fc goat polyclonal antibody (10 μg/mL) (Jackson ImmunoResearch, West Grove, PA, USA) at 4 °C overnight and then blocked with 0.5% BSA in PBS at room temperature for 2 h. Fc-fused proteins (1 μg/mL) were captured by the antibody, and phage solution (1.0 × 1011 pfu/mL) or biotinylated peptide solution was added to the wells and incubated at room temperature for 1 h. After three times washing with PBST, bound phages or peptides were detected using horseradish peroxidase (HRP)-conjugated anti-T7 antibody (5000-fold dilution in PBS with 0.5% BSA) (Merck Millipore) and HRP-conjugated streptavidin (1000-fold dilution in PBS with 0.5% BSA) (Vector Laboratories Inc., Burlingame, CA, USA), respectively. .. The amount of HRP in each well was measured colorimetrically with the chromogenic reagent tetramethylbenzidine (Wako, Osaka, Japan).

    Article Title:
    Article Snippet: .. Cells were washed three times and incubated with DyLight 594–conjugated streptavidin (15 μ g/ml; Vectorlabs, Peterborough, UK) for 30 minutes at RT in the dark. .. After three final washes, cells were imaged using an 880 laser-scanning confocal microscope (Zeiss, Cambridge, UK).

    Microscopy:

    Article Title: Effects of Cellular Methylation on Transgene Expression and Site-Specific Integration of Adeno-Associated Virus
    Article Snippet: .. Excess streptavidin was washed off with PBST and slides were mounted in Vectashield® mounting medium from Vector Laboratories, visualized and imaged in a Zeiss LSM 710 Laser Confocal Scanning Microscope (Carl Zeiss Microscopy GmbH, Jena, Germany) using 0.42 μm resolution and Zen2008 4.7.2 software (Carl Zeiss). ..

    Recombinant:

    Article Title: A novel LRP1-binding peptide L57 that crosses the blood brain barrier
    Article Snippet: .. 2.2 Evaluation of phage- or synthetic peptide-binding to recombinant proteins by plate ELISA The wells of a Nunc Maxisorp microplate (460−518) were coated with an anti-human Fc goat polyclonal antibody (10 μg/mL) (Jackson ImmunoResearch, West Grove, PA, USA) at 4 °C overnight and then blocked with 0.5% BSA in PBS at room temperature for 2 h. Fc-fused proteins (1 μg/mL) were captured by the antibody, and phage solution (1.0 × 1011 pfu/mL) or biotinylated peptide solution was added to the wells and incubated at room temperature for 1 h. After three times washing with PBST, bound phages or peptides were detected using horseradish peroxidase (HRP)-conjugated anti-T7 antibody (5000-fold dilution in PBS with 0.5% BSA) (Merck Millipore) and HRP-conjugated streptavidin (1000-fold dilution in PBS with 0.5% BSA) (Vector Laboratories Inc., Burlingame, CA, USA), respectively. .. The amount of HRP in each well was measured colorimetrically with the chromogenic reagent tetramethylbenzidine (Wako, Osaka, Japan).

    SDS Page:

    Article Title: Identification of a Novel Recycling Sequence in the C-tail of FPR2/ALX Receptor
    Article Snippet: .. Samples were resolved by SDS-PAGE and visualized with streptavidin overlay (VECTASTAIN ABC immunoperoxidase reagent, Vector Laboratories). .. Apoptosis Assay HEK293 cells stably expressing N-terminal FLAG-tagged FPR2/ALX or N333-stop were grown to 50% confluency in 6-well plates and either untreated or treated with W peptide for 5 h. Etoposide was used as a positive control.

    Software:

    Article Title: Effects of Cellular Methylation on Transgene Expression and Site-Specific Integration of Adeno-Associated Virus
    Article Snippet: .. Excess streptavidin was washed off with PBST and slides were mounted in Vectashield® mounting medium from Vector Laboratories, visualized and imaged in a Zeiss LSM 710 Laser Confocal Scanning Microscope (Carl Zeiss Microscopy GmbH, Jena, Germany) using 0.42 μm resolution and Zen2008 4.7.2 software (Carl Zeiss). ..

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  • 99
    Vector Laboratories streptavidin conjugated to alkaline phosphatase
    Competition ELISAs between biotinylated MAbs and immune rabbit sera. The x axis represents the concentration of biotinylated human MAb (μg/ml). The y axis represents the binding of biotinylated MAb detected with <t>streptavidin-alkaline</t> phosphatase
    Streptavidin Conjugated To Alkaline Phosphatase, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated to alkaline phosphatase/product/Vector Laboratories
    Average 99 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated to alkaline phosphatase - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    99
    Vector Laboratories alkaline phosphatase conjugated avidin d
    Lectin staining of glycoproteins derived from wild-type MDCK and CHO and mutant MDCK-RCA r and CHO-Lec8 cells. Mutant cells were stably transfected with respective expression plasmids and UGT splice variants were expressed either singly or in combination. Proteins were extracted as described in Materials and Methods , separated by SDS-PAGE and transferred onto nitrocellulose membranes. Phenotypic correction was determined using GSL II (lectin from Griffonia simplicifolia ) or VVL (lectin from Vicia villosa ) lectin. Reactivity of glycoproteins derived from protein cell extracts with GSL II, lectin specific for terminal N -acetylglucosamine present in both N - and O -glycans or with VVL, lectin specific for N -acetylgalactosamine attached to O -glycans was visualized using alkaline phosphatase-conjugated <t>avidin</t> D and NBT/BCIP. Control cells transfected with empty vector gave similar results as mutant cells. Representative data out of three sets with a similar pattern are shown
    Alkaline Phosphatase Conjugated Avidin D, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alkaline phosphatase conjugated avidin d/product/Vector Laboratories
    Average 99 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    alkaline phosphatase conjugated avidin d - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    Competition ELISAs between biotinylated MAbs and immune rabbit sera. The x axis represents the concentration of biotinylated human MAb (μg/ml). The y axis represents the binding of biotinylated MAb detected with streptavidin-alkaline phosphatase

    Journal: Journal of Virology

    Article Title: Comparing Antigenicity and Immunogenicity of Engineered gp120

    doi: 10.1128/JVI.79.19.12148-12163.2005

    Figure Lengend Snippet: Competition ELISAs between biotinylated MAbs and immune rabbit sera. The x axis represents the concentration of biotinylated human MAb (μg/ml). The y axis represents the binding of biotinylated MAb detected with streptavidin-alkaline phosphatase

    Article Snippet: Plates were washed, and streptavidin conjugated to alkaline phosphatase (Vector Laboratory), diluted 1:300, was added, and the plates were incubated for 1 h at RT.

    Techniques: Concentration Assay, Binding Assay

    Reduced enhancement of Ca 2+ flux in YF16 +/− B cells after co-cross-linking of the BCR and FcγRIIB as compared to FcγRIIB deficient B cells. Intracellular Ca 2+ levels were evaluated in purified B cells from mice of the indicated genotypes as described in Materials and Methods. After establishing basal Ca 2+ levels, either 10 μg/ml of anti-IgM F(ab') 2 biotin (A) or 10 μg/ml of this reagent and 2.4G2 biotin Abs were added (B), Ca 2+ levels were continuously monitored, and cross-linking of receptors was achieved by then adding streptavidin to 200 ng/ml followed by continued monitoring. The results are representative of two independent experiments.

    Journal: Immunity, Inflammation and Disease

    Article Title: Testing the role of the FcγRIIB immunoreceptor tyrosine-based inhibitory motif in regulation of the B cell immune response

    doi: 10.1002/iid3.64

    Figure Lengend Snippet: Reduced enhancement of Ca 2+ flux in YF16 +/− B cells after co-cross-linking of the BCR and FcγRIIB as compared to FcγRIIB deficient B cells. Intracellular Ca 2+ levels were evaluated in purified B cells from mice of the indicated genotypes as described in Materials and Methods. After establishing basal Ca 2+ levels, either 10 μg/ml of anti-IgM F(ab') 2 biotin (A) or 10 μg/ml of this reagent and 2.4G2 biotin Abs were added (B), Ca 2+ levels were continuously monitored, and cross-linking of receptors was achieved by then adding streptavidin to 200 ng/ml followed by continued monitoring. The results are representative of two independent experiments.

    Article Snippet: Bound antibodies were detected using biotinylated anti-mouse IgM and IgG Abs (Jackson Immunoresearch Laboratories, West, Grove, PA) followed by streptavidin conjugated to alkaline phosphatase (Vector Laboratories, Burlingame, CA).

    Techniques: Purification, Mouse Assay

    Effects of WT N-Myc-ASPH Over-expression on ASPH and Notch Pathway Protein Immunoreactivity: PNET2 cells transfected with recombinant plasmids carrying full-length cDNAs encoding (A, D, G, J) WT-ASPH, (B, E, H, K) GFP, or (C, F, I, L) Humbug (truncated form of ASPH) were harvested after 48 hours to generate cytospin preparations for immunofluorescence assays. Formalin-fixed, permeabilized cells were incubated with (A-C) A85G6-ASPH, (D-F) FB50-ASPH/Humbug, (G-I) Notch-1, or (J-L) Jagged-1 monoclonal antibodies. Immunoreactivity was detected with biotinylated secondary antibody and Streptavidin-conjugated Dylight 547 (green) or Dylight 647 (red). Cells were counterstained with 4′,6-diamidino-2-phenylindole (DAPI; blue). Panels depict merged confocal microscopy images. (600× original magnification, 2× digitalzoom).

    Journal: Cell biology : research & therapy

    Article Title: Phosphorylation Modulates Aspartyl-(Asparaginyl)-β Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells

    doi: 10.4172/2324-9293.1000133

    Figure Lengend Snippet: Effects of WT N-Myc-ASPH Over-expression on ASPH and Notch Pathway Protein Immunoreactivity: PNET2 cells transfected with recombinant plasmids carrying full-length cDNAs encoding (A, D, G, J) WT-ASPH, (B, E, H, K) GFP, or (C, F, I, L) Humbug (truncated form of ASPH) were harvested after 48 hours to generate cytospin preparations for immunofluorescence assays. Formalin-fixed, permeabilized cells were incubated with (A-C) A85G6-ASPH, (D-F) FB50-ASPH/Humbug, (G-I) Notch-1, or (J-L) Jagged-1 monoclonal antibodies. Immunoreactivity was detected with biotinylated secondary antibody and Streptavidin-conjugated Dylight 547 (green) or Dylight 647 (red). Cells were counterstained with 4′,6-diamidino-2-phenylindole (DAPI; blue). Panels depict merged confocal microscopy images. (600× original magnification, 2× digitalzoom).

    Article Snippet: Alkaline Phosphatase Conjugated to Streptavidin was purchased from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Over Expression, Transfection, Recombinant, Immunofluorescence, Incubation, Confocal Microscopy

    Effects of S/T→A mutations on ASPH protein expression and subcellular localization: PNET2 cells were transiently transfected with wildtype (WT) or a pointmutated (M#:S/T→A) N-Myc-ASPH cDNA. Myc-empty vector (EV) served as a negative control. The M19-H675Q mutant, disrupting ASPH’s catalytic activity, served as a positive control. Representative results obtained by immunofluorescence staining and confocal imaging of cells transfected with (A) WT, (B) M7-S24A, (C) M18-T748A, (D) M19-H675Q, or (E) EV and stained by immunofluorescence with anti-Myc. Immunoreactivity was detected with biotinylated secondary antibody and Streptavidin-conjugated Dylight 547 (red). Cells were counterstained with DAPI (blue). (Merged images: 600× magnification, 2× digital zoom).

    Journal: Cell biology : research & therapy

    Article Title: Phosphorylation Modulates Aspartyl-(Asparaginyl)-β Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells

    doi: 10.4172/2324-9293.1000133

    Figure Lengend Snippet: Effects of S/T→A mutations on ASPH protein expression and subcellular localization: PNET2 cells were transiently transfected with wildtype (WT) or a pointmutated (M#:S/T→A) N-Myc-ASPH cDNA. Myc-empty vector (EV) served as a negative control. The M19-H675Q mutant, disrupting ASPH’s catalytic activity, served as a positive control. Representative results obtained by immunofluorescence staining and confocal imaging of cells transfected with (A) WT, (B) M7-S24A, (C) M18-T748A, (D) M19-H675Q, or (E) EV and stained by immunofluorescence with anti-Myc. Immunoreactivity was detected with biotinylated secondary antibody and Streptavidin-conjugated Dylight 547 (red). Cells were counterstained with DAPI (blue). (Merged images: 600× magnification, 2× digital zoom).

    Article Snippet: Alkaline Phosphatase Conjugated to Streptavidin was purchased from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Expressing, Transfection, Plasmid Preparation, Negative Control, Mutagenesis, Activity Assay, Positive Control, Immunofluorescence, Staining, Imaging

    Lectin staining of glycoproteins derived from wild-type MDCK and CHO and mutant MDCK-RCA r and CHO-Lec8 cells. Mutant cells were stably transfected with respective expression plasmids and UGT splice variants were expressed either singly or in combination. Proteins were extracted as described in Materials and Methods , separated by SDS-PAGE and transferred onto nitrocellulose membranes. Phenotypic correction was determined using GSL II (lectin from Griffonia simplicifolia ) or VVL (lectin from Vicia villosa ) lectin. Reactivity of glycoproteins derived from protein cell extracts with GSL II, lectin specific for terminal N -acetylglucosamine present in both N - and O -glycans or with VVL, lectin specific for N -acetylgalactosamine attached to O -glycans was visualized using alkaline phosphatase-conjugated avidin D and NBT/BCIP. Control cells transfected with empty vector gave similar results as mutant cells. Representative data out of three sets with a similar pattern are shown

    Journal: Glycoconjugate Journal

    Article Title: Comparative analysis of involvement of UGT1 and UGT2 splice variants of UDP-galactose transporter in glycosylation of macromolecules in MDCK and CHO cell lines

    doi: 10.1007/s10719-011-9348-z

    Figure Lengend Snippet: Lectin staining of glycoproteins derived from wild-type MDCK and CHO and mutant MDCK-RCA r and CHO-Lec8 cells. Mutant cells were stably transfected with respective expression plasmids and UGT splice variants were expressed either singly or in combination. Proteins were extracted as described in Materials and Methods , separated by SDS-PAGE and transferred onto nitrocellulose membranes. Phenotypic correction was determined using GSL II (lectin from Griffonia simplicifolia ) or VVL (lectin from Vicia villosa ) lectin. Reactivity of glycoproteins derived from protein cell extracts with GSL II, lectin specific for terminal N -acetylglucosamine present in both N - and O -glycans or with VVL, lectin specific for N -acetylgalactosamine attached to O -glycans was visualized using alkaline phosphatase-conjugated avidin D and NBT/BCIP. Control cells transfected with empty vector gave similar results as mutant cells. Representative data out of three sets with a similar pattern are shown

    Article Snippet: Lectins bound to specific glycans were subsequently detected using alkaline phosphatase-conjugated avidin D (Vector Laboratories) and visualized with NBT/BCIP solution (Roche) according to the manufacturer’s instructions.

    Techniques: Staining, Derivative Assay, Mutagenesis, Stable Transfection, Transfection, Expressing, SDS Page, Avidin-Biotin Assay, Plasmid Preparation