biotinylated  (Vector Laboratories)


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    Name:
    Biotinylated Protein A S aureus
    Description:
    Biotinylated Protein A B 2001 isolated from a special strain of S aureus is a 41 kDa protein which binds to the Fc portion of most immunoglobulins This interaction is neither species specific nor isotype specific as Protein A has been shown to bind IgG from a variety of species Protein A can also interact with IgA IgM and subclasses of IgG from different species Biotinylated Protein A is useful to detect or localize immunoglobulins on cell surfaces or in tissue sections Used with the appropriate avidin or streptavidin conjugates immunoglobulins can be studied with brightfield fluorescence or electron microscopy Biotinylated Protein A can also be used to detect positive clones in monoclonal antibody production by an avidin or streptavidin enzyme conjugate Biotinylated Protein A is used in many systems as a substitute for a biotinylated second antibody However in some applications Biotinylated Protein A may bind to endogenous immunoglobulin in the tissue producing background In addition Biotinylated Protein A may not bind to the species or class of primary antibody being employed For routine immunohistochemical staining we recommend using biotinylated anti immunoglobulins
    Catalog Number:
    b-2001
    Price:
    None
    Size:
    1 mg
    Category:
    Proteins
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    Structured Review

    Vector Laboratories biotinylated
    Biotinylated Protein A S aureus
    Biotinylated Protein A B 2001 isolated from a special strain of S aureus is a 41 kDa protein which binds to the Fc portion of most immunoglobulins This interaction is neither species specific nor isotype specific as Protein A has been shown to bind IgG from a variety of species Protein A can also interact with IgA IgM and subclasses of IgG from different species Biotinylated Protein A is useful to detect or localize immunoglobulins on cell surfaces or in tissue sections Used with the appropriate avidin or streptavidin conjugates immunoglobulins can be studied with brightfield fluorescence or electron microscopy Biotinylated Protein A can also be used to detect positive clones in monoclonal antibody production by an avidin or streptavidin enzyme conjugate Biotinylated Protein A is used in many systems as a substitute for a biotinylated second antibody However in some applications Biotinylated Protein A may bind to endogenous immunoglobulin in the tissue producing background In addition Biotinylated Protein A may not bind to the species or class of primary antibody being employed For routine immunohistochemical staining we recommend using biotinylated anti immunoglobulins
    https://www.bioz.com/result/biotinylated/product/Vector Laboratories
    Average 99 stars, based on 58 article reviews
    Price from $9.99 to $1999.99
    biotinylated - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Autoimmunity due to molecular mimicry as a cause of neurological disease"

    Article Title: Autoimmunity due to molecular mimicry as a cause of neurological disease

    Journal: Nature medicine

    doi: 10.1038/nm0502-509

    Specificity of HAM/TSP IgG for CNS neurons and isolation of the neuronal antigen. a , Immunohistochemistry of human tissues. Biotinylated HAM/TSP IgG stained CNS neurons (cortex, brown reaction product) (scale bar, 100 µm). There was no staining of glia (arrowhead), dorsal root ganglion or systemic organs. A tax mAb mimicked HAM/TSP IgG staining indicated by the red stain. Neurofilament (gray) confirmed localization of tax mAb to neurons. b , Western blots of proteins derived from CNS neurons. HAM/TSP IgG showed an intense signal at 33 kD (lane 1). There was no reactivity using IgG isolated from HTLV-1 seronegative (lane 2) or HTLV-1 seropositive, neurologically asymptomatic individuals (lane 3). The tax mAb recognized the 33-kD neuronal antigen (lane 4). c , Purification and western blots of the neuronal protein following high salt extraction and centrifugation. Molecular weight markers (lane 1), precipitate (lane 2) and supernatant (lane 3). HAM/TSP IgG reacted with the supernatant (lane 3), but not the precipitate (lane 2). d , 2-D gel electrophoresis and western blot of the neuronal protein purified from the supernatant. Coomassie stain of gel (left). Western blot of the neuronal extract (right), HAM/TSP IgG reacted at 33–38 kD, pI = 9.3 (arrow).
    Figure Legend Snippet: Specificity of HAM/TSP IgG for CNS neurons and isolation of the neuronal antigen. a , Immunohistochemistry of human tissues. Biotinylated HAM/TSP IgG stained CNS neurons (cortex, brown reaction product) (scale bar, 100 µm). There was no staining of glia (arrowhead), dorsal root ganglion or systemic organs. A tax mAb mimicked HAM/TSP IgG staining indicated by the red stain. Neurofilament (gray) confirmed localization of tax mAb to neurons. b , Western blots of proteins derived from CNS neurons. HAM/TSP IgG showed an intense signal at 33 kD (lane 1). There was no reactivity using IgG isolated from HTLV-1 seronegative (lane 2) or HTLV-1 seropositive, neurologically asymptomatic individuals (lane 3). The tax mAb recognized the 33-kD neuronal antigen (lane 4). c , Purification and western blots of the neuronal protein following high salt extraction and centrifugation. Molecular weight markers (lane 1), precipitate (lane 2) and supernatant (lane 3). HAM/TSP IgG reacted with the supernatant (lane 3), but not the precipitate (lane 2). d , 2-D gel electrophoresis and western blot of the neuronal protein purified from the supernatant. Coomassie stain of gel (left). Western blot of the neuronal extract (right), HAM/TSP IgG reacted at 33–38 kD, pI = 9.3 (arrow).

    Techniques Used: Isolation, Immunohistochemistry, Staining, Western Blot, Derivative Assay, Purification, Centrifugation, Molecular Weight, Nucleic Acid Electrophoresis

    2) Product Images from "The effect of an ionic detergent on the natively unfolded ?-dystroglycan ectodomain and on its interaction with ?-dystroglycan"

    Article Title: The effect of an ionic detergent on the natively unfolded ?-dystroglycan ectodomain and on its interaction with ?-dystroglycan

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1110/ps.04762504

    Solid-phase biotinylated-ligand binding assay. Biotinylated β-DG(654–750) binding to Trx-α-DG(485–600) with increasing amounts of SDS: (open circles) 0 mM; (solid circles) 0.05 mM; (squares) 0.1 mM. Data refer to a representative experiment.
    Figure Legend Snippet: Solid-phase biotinylated-ligand binding assay. Biotinylated β-DG(654–750) binding to Trx-α-DG(485–600) with increasing amounts of SDS: (open circles) 0 mM; (solid circles) 0.05 mM; (squares) 0.1 mM. Data refer to a representative experiment.

    Techniques Used: Ligand Binding Assay, Binding Assay

    Related Articles

    Incubation:

    Article Title: Trafficking to the Plasma Membrane of the Seven-Transmembrane Protein Encoded by Human Herpesvirus 6 U51 Gene Involves a Cell-Specific Function Present in T Lymphocytes
    Article Snippet: .. The biotinylated proteins were detected by incubation with avidin-biotin-conjugated peroxidase (Vector Laboratories) for 30 min and diaminobenzidine as substrate. ..

    other:

    Article Title: Plasminogen activator inhibitors regulate cell adhesion through a uPAR-dependent mechanism
    Article Snippet: Biotinylated proteins were detected as above.

    Autoradiography:

    Article Title: Association with FcR? Is Essential for Activation Signal through NKR-P1 (CD161) in Natural Killer (NK) Cells and NK1.1+ T Cells
    Article Snippet: .. The biotinylated proteins were detected using streptavidin-peroxidase (VECSTAIN Elite ABC kit; Vector Laboratories Incorporated, Burlingame, CA), the ECL system ( Amersham International , Buckinghamshire, England), and autoradiography. .. After termination of chemiluminescence, the membrane was blotted with anti-FcRγ Ab followed by peroxidase-labeled anti–rabbit Ab ( Amersham ) and detected by the ECL system.

    Avidin-Biotin Assay:

    Article Title: Trafficking to the Plasma Membrane of the Seven-Transmembrane Protein Encoded by Human Herpesvirus 6 U51 Gene Involves a Cell-Specific Function Present in T Lymphocytes
    Article Snippet: .. The biotinylated proteins were detected by incubation with avidin-biotin-conjugated peroxidase (Vector Laboratories) for 30 min and diaminobenzidine as substrate. ..

    Blocking Assay:

    Article Title: Targeted Disruption of Core 1 ?1,3-galactosyltransferase (C1galt1) Induces Apical Endocytic Trafficking in Human Corneal Keratinocytes
    Article Snippet: .. Biotinylated protein was detected on the membranes after blocking with Tris-buffered saline Tween (TBS-T) using a biotin-streptavidin-peroxidase kit (Vectastain® ABC Kit; Vector Laboratories, Burlingame, CA). .. Band intensities were quantified by densitometry using ImageJ software (National Institutes of Health, Bethesda, MD; http://rsb.info.nih.gov/nih-image ).

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  • 92
    Vector Laboratories biotinylated 3g9 antibody
    Comparison of untreated KAT-4 and Capan-2 carcinoma models. a Hematoxylin and Eosin and Sirius red staining in KAT-4 and Capan-2 carcinomas (bars = 100 μm). Trichrome staining (bars = 20 μm) and immunofluorescence staining with <t>biotinylated</t> <t>3G9</t> antibody (green) shows that the expression of integrin α V β 6 is located at the cell membrane in both KAT-4 and Capan-2 carcinomas (cell nuclei stained with DAPI, blue; bars = 50 μm). b Collagen content in untreated KAT-4 ( n = 4) and Capan-2 ( n = 5) carcinomas, represented by hydroxyproline mg/g wet weight. c Average growth of untreated KAT-4 ( n = 8) and Capan-2 tumors ( n = 7), represented in mm 3 measured externally (length x width x height)
    Biotinylated 3g9 Antibody, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated 3g9 antibody/product/Vector Laboratories
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
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    91
    Vector Laboratories biotinylated isolectin b4
    Myocardial interstitial collagen expression and capillary density in control and diabetic rats. Interstitial collagen accumulation (C) assessed via picrosirius red staining in control (A) and diabetic (B) rats (20× objective). Capillary density (F) assessed via <t>isolectin</t> B4 staining in control (D) and diabetic (E) rats (40× objective). There was no significant difference between groups. Control, n = 6 and diabetic, n = 8. Values expressed as mean ± SEM.
    Biotinylated Isolectin B4, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 91/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated isolectin b4/product/Vector Laboratories
    Average 91 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
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    88
    Vector Laboratories biotinylated mab binding
    Potent vaccine sera target epitopes that overlap the CD4 binding site. Selected vaccine sera (1:10 dilution) were competed against various <t>biotinylated</t> monoclonal bnAbs for binding to SOS E168K trimer VLPs by ELISA. E168K+N189A mutant trimer VLPs were used for assays involving biotinylated V2 quaternary mAbs to ensure a full epitope knock in [ 56 ]. Three previously mapped HIV-1-infected plasmas were included for reference purposes [ 54 ]. These are (epitopes in parentheses) 1702 (some MPER and unmapped nAb), 1686 (predominantly CD4bs nAb) and BB34 (predominantly MPER nAb). Numbers are expressed as the residual % binding titer of biotinylated mAb in the presence of competitor compared to its titer in the presence of a control rabbit prebleed or HIV-1 seronegative human plasma (from donor 210). Each assay was performed at least in duplicate. Standard errors are shown in S8 Fig .
    Biotinylated Mab Binding, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated mab binding/product/Vector Laboratories
    Average 88 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
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    86
    Vector Laboratories carbohydrate specific biotinylated lectins
    Accessibility and characterization of the glycosylated region of lubricin. A , the enriched synovial lubricin samples, before and after trypsin digestion, were separated on a 3–8% Tris acetate gel, blotted onto PVDF membrane, and then probed with lubricin-specific antibody (mouse anti-lubricin) and carbohydrate-specific <t>biotinylated</t> <t>lectins</t> PNA, specific for core 1 (Galβ1–3GalNAc) O -glycan, and WGA, specific for sialic acid and terminal GlcNAc. B , SDS-PAGE (3–8% Tris acetate gel) of the acidic glycoprotein fractions of the SF before (−) and after (+) partial de-glycosylation stained with Coomassie Brilliant Blue. C , SF lubricin was in-solution digested, and non-modified peptides were identified via mass spectrometry for protein coverage determination (black). The low protein coverage (in particular the mucin domain) suggests that the mucin domain is extensively glycosylated. Some of the core 1 structures were removed by partial de-glycosylation, and the previously glycosylated peptides were identified for protein coverage (gray). The results suggest that lubricin contains an extended STP-rich region relative to the mucin domain previously defined by UniProt.
    Carbohydrate Specific Biotinylated Lectins, supplied by Vector Laboratories, 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/carbohydrate specific biotinylated lectins/product/Vector Laboratories
    Average 86 stars, based on 1 article reviews
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    Image Search Results


    Comparison of untreated KAT-4 and Capan-2 carcinoma models. a Hematoxylin and Eosin and Sirius red staining in KAT-4 and Capan-2 carcinomas (bars = 100 μm). Trichrome staining (bars = 20 μm) and immunofluorescence staining with biotinylated 3G9 antibody (green) shows that the expression of integrin α V β 6 is located at the cell membrane in both KAT-4 and Capan-2 carcinomas (cell nuclei stained with DAPI, blue; bars = 50 μm). b Collagen content in untreated KAT-4 ( n = 4) and Capan-2 ( n = 5) carcinomas, represented by hydroxyproline mg/g wet weight. c Average growth of untreated KAT-4 ( n = 8) and Capan-2 tumors ( n = 7), represented in mm 3 measured externally (length x width x height)

    Journal: Cell Communication and Signaling : CCS

    Article Title: Inhibition of integrin αVβ6 changes fibril thickness of stromal collagen in experimental carcinomas

    doi: 10.1186/s12964-018-0249-7

    Figure Lengend Snippet: Comparison of untreated KAT-4 and Capan-2 carcinoma models. a Hematoxylin and Eosin and Sirius red staining in KAT-4 and Capan-2 carcinomas (bars = 100 μm). Trichrome staining (bars = 20 μm) and immunofluorescence staining with biotinylated 3G9 antibody (green) shows that the expression of integrin α V β 6 is located at the cell membrane in both KAT-4 and Capan-2 carcinomas (cell nuclei stained with DAPI, blue; bars = 50 μm). b Collagen content in untreated KAT-4 ( n = 4) and Capan-2 ( n = 5) carcinomas, represented by hydroxyproline mg/g wet weight. c Average growth of untreated KAT-4 ( n = 8) and Capan-2 tumors ( n = 7), represented in mm 3 measured externally (length x width x height)

    Article Snippet: Sections were blocked in 5% swine serum (Sigma) and 2% BSA (Sigma), incubated with biotinylated 3G9 antibody and then with Fluorescein Avidin D (Vector Labs).

    Techniques: Staining, Immunofluorescence, Expressing

    Myocardial interstitial collagen expression and capillary density in control and diabetic rats. Interstitial collagen accumulation (C) assessed via picrosirius red staining in control (A) and diabetic (B) rats (20× objective). Capillary density (F) assessed via isolectin B4 staining in control (D) and diabetic (E) rats (40× objective). There was no significant difference between groups. Control, n = 6 and diabetic, n = 8. Values expressed as mean ± SEM.

    Journal: Cardiovascular Diabetology

    Article Title: Acute Rho-kinase inhibition improves coronary dysfunction in vivo, in the early diabetic microcirculation

    doi: 10.1186/1475-2840-12-111

    Figure Lengend Snippet: Myocardial interstitial collagen expression and capillary density in control and diabetic rats. Interstitial collagen accumulation (C) assessed via picrosirius red staining in control (A) and diabetic (B) rats (20× objective). Capillary density (F) assessed via isolectin B4 staining in control (D) and diabetic (E) rats (40× objective). There was no significant difference between groups. Control, n = 6 and diabetic, n = 8. Values expressed as mean ± SEM.

    Article Snippet: Sections were then incubated with biotinylated isolectin B4 at 4°C over-night, followed by avidin-biotin horseradish peroxidase (Vector Laboratories, Inc, Burlingame, CA, USA) and diaminobenzidine (Vector Laboratories, Inc, Burlingame, CA, USA), as described previously [ ].

    Techniques: Expressing, Staining

    Potent vaccine sera target epitopes that overlap the CD4 binding site. Selected vaccine sera (1:10 dilution) were competed against various biotinylated monoclonal bnAbs for binding to SOS E168K trimer VLPs by ELISA. E168K+N189A mutant trimer VLPs were used for assays involving biotinylated V2 quaternary mAbs to ensure a full epitope knock in [ 56 ]. Three previously mapped HIV-1-infected plasmas were included for reference purposes [ 54 ]. These are (epitopes in parentheses) 1702 (some MPER and unmapped nAb), 1686 (predominantly CD4bs nAb) and BB34 (predominantly MPER nAb). Numbers are expressed as the residual % binding titer of biotinylated mAb in the presence of competitor compared to its titer in the presence of a control rabbit prebleed or HIV-1 seronegative human plasma (from donor 210). Each assay was performed at least in duplicate. Standard errors are shown in S8 Fig .

    Journal: PLoS Pathogens

    Article Title: Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site

    doi: 10.1371/journal.ppat.1004932

    Figure Lengend Snippet: Potent vaccine sera target epitopes that overlap the CD4 binding site. Selected vaccine sera (1:10 dilution) were competed against various biotinylated monoclonal bnAbs for binding to SOS E168K trimer VLPs by ELISA. E168K+N189A mutant trimer VLPs were used for assays involving biotinylated V2 quaternary mAbs to ensure a full epitope knock in [ 56 ]. Three previously mapped HIV-1-infected plasmas were included for reference purposes [ 54 ]. These are (epitopes in parentheses) 1702 (some MPER and unmapped nAb), 1686 (predominantly CD4bs nAb) and BB34 (predominantly MPER nAb). Numbers are expressed as the residual % binding titer of biotinylated mAb in the presence of competitor compared to its titer in the presence of a control rabbit prebleed or HIV-1 seronegative human plasma (from donor 210). Each assay was performed at least in duplicate. Standard errors are shown in S8 Fig .

    Article Snippet: Biotinylated mAb binding was detected using streptavidin-alkaline phosphatase (Vector, Burlingame, CA), and developed as above.

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Mutagenesis, Knock-In, Infection

    Accessibility and characterization of the glycosylated region of lubricin. A , the enriched synovial lubricin samples, before and after trypsin digestion, were separated on a 3–8% Tris acetate gel, blotted onto PVDF membrane, and then probed with lubricin-specific antibody (mouse anti-lubricin) and carbohydrate-specific biotinylated lectins PNA, specific for core 1 (Galβ1–3GalNAc) O -glycan, and WGA, specific for sialic acid and terminal GlcNAc. B , SDS-PAGE (3–8% Tris acetate gel) of the acidic glycoprotein fractions of the SF before (−) and after (+) partial de-glycosylation stained with Coomassie Brilliant Blue. C , SF lubricin was in-solution digested, and non-modified peptides were identified via mass spectrometry for protein coverage determination (black). The low protein coverage (in particular the mucin domain) suggests that the mucin domain is extensively glycosylated. Some of the core 1 structures were removed by partial de-glycosylation, and the previously glycosylated peptides were identified for protein coverage (gray). The results suggest that lubricin contains an extended STP-rich region relative to the mucin domain previously defined by UniProt.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: The O-glycomap of Lubricin, a Novel Mucin Responsible for Joint Lubrication, Identified by Site-specific Glycopeptide Analysis *

    doi: 10.1074/mcp.M114.040865

    Figure Lengend Snippet: Accessibility and characterization of the glycosylated region of lubricin. A , the enriched synovial lubricin samples, before and after trypsin digestion, were separated on a 3–8% Tris acetate gel, blotted onto PVDF membrane, and then probed with lubricin-specific antibody (mouse anti-lubricin) and carbohydrate-specific biotinylated lectins PNA, specific for core 1 (Galβ1–3GalNAc) O -glycan, and WGA, specific for sialic acid and terminal GlcNAc. B , SDS-PAGE (3–8% Tris acetate gel) of the acidic glycoprotein fractions of the SF before (−) and after (+) partial de-glycosylation stained with Coomassie Brilliant Blue. C , SF lubricin was in-solution digested, and non-modified peptides were identified via mass spectrometry for protein coverage determination (black). The low protein coverage (in particular the mucin domain) suggests that the mucin domain is extensively glycosylated. Some of the core 1 structures were removed by partial de-glycosylation, and the previously glycosylated peptides were identified for protein coverage (gray). The results suggest that lubricin contains an extended STP-rich region relative to the mucin domain previously defined by UniProt.

    Article Snippet: The separated proteins were transferred to PVDF membrane using a semi-dry blotter (Bio-Rad) and probed with lubricin-specific antibody (mouse anti-lubricin mAb13, Pfizer Research, Cambridge, MA) and carbohydrate-specific biotinylated lectins including peanut agglutinin (PNA) (Vector Laboratories, Burlingame, CA) and wheat germ agglutinin (WGA) (Vector Laboratories) as previously described ( ).

    Techniques: Whole Genome Amplification, SDS Page, Staining, Modification, Mass Spectrometry