sheep spinophilin antibody  (Thermo Fisher)


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    Name:
    Exosome Immunoprecipitation Reagent Protein A
    Description:
    Exosome Immunoprecipitation Reagent Protein A enables fast and gentle magnetic isolation of exosomal proteins causing minimal physical stress to the target protein and allowing comparison of multiple samples on the same gel • Maintain intact exosome protein complexes• Reduce background significantly low non specific binding• Fast protocol time only 30 minutes• Maximal comparison ultra sensitivity allows many samples on the same gel Dynabeads coupled to Protein A are widely used for immunoprecipitation IP chromatin immunoprecipitation ChIP and protein isolation The magnetic properties of Dynabeads makes them a superior alternative to sepharose or agarose slurry for immunoprecipitation since magnetic separation technology is faster and gentler than other methods causing minimal physical stress to the target proteins This permits the isolation and concentration of labile composites that might otherwise dissociate or be damaged by proteases during long incubation times Native protein conformation and intact large protein complexes will be preserved Exosome Immunoprecipitation Protein A makes use of Dynabeads Protein A for antibody binding and subsequent immunoprecipitation of exosomal proteins Antibody is added to the Dynabeads suspension where binding occurs via the Fc region of the antibody The mixture is then placed near a magnet causing the beads migrate to the side of the tube allowing easy removal of the supernatant The bead bound antibody can now be used for immunoprecipitation of exosomal proteins Immunoprecipitation allows a 10 to 50 times concentration of exosomal proteins prior to protein analysis such as Western blotting The amount of Ig captured by Exosome Immunoprecipitation Protein A is dependent on the concentration of Ig in the starting sample The binding capacity is approximately 240 ug human Ig per mL beads For isolation of Ig via protein G we recommend the Exosome Immunoprecipitation Protein G
    Catalog Number:
    10610D
    Price:
    None
    Category:
    Beads Microspheres
    Applications:
    Cancer Research|Cell Analysis|Clinical|Exosomes|Immunoprecipitation|Oncology & Genetic Disease Research|Protein Assays and Analysis|Protein Biology|Protein Microarrays|Protein Purification & Isolation|Protein from Exosomes|Protein Isolation from Exosomes
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    Structured Review

    Thermo Fisher sheep spinophilin antibody
    Generation and characterization of Cre-expressing, HA-tagged human <t>spinophilin</t> mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.
    Exosome Immunoprecipitation Reagent Protein A enables fast and gentle magnetic isolation of exosomal proteins causing minimal physical stress to the target protein and allowing comparison of multiple samples on the same gel • Maintain intact exosome protein complexes• Reduce background significantly low non specific binding• Fast protocol time only 30 minutes• Maximal comparison ultra sensitivity allows many samples on the same gel Dynabeads coupled to Protein A are widely used for immunoprecipitation IP chromatin immunoprecipitation ChIP and protein isolation The magnetic properties of Dynabeads makes them a superior alternative to sepharose or agarose slurry for immunoprecipitation since magnetic separation technology is faster and gentler than other methods causing minimal physical stress to the target proteins This permits the isolation and concentration of labile composites that might otherwise dissociate or be damaged by proteases during long incubation times Native protein conformation and intact large protein complexes will be preserved Exosome Immunoprecipitation Protein A makes use of Dynabeads Protein A for antibody binding and subsequent immunoprecipitation of exosomal proteins Antibody is added to the Dynabeads suspension where binding occurs via the Fc region of the antibody The mixture is then placed near a magnet causing the beads migrate to the side of the tube allowing easy removal of the supernatant The bead bound antibody can now be used for immunoprecipitation of exosomal proteins Immunoprecipitation allows a 10 to 50 times concentration of exosomal proteins prior to protein analysis such as Western blotting The amount of Ig captured by Exosome Immunoprecipitation Protein A is dependent on the concentration of Ig in the starting sample The binding capacity is approximately 240 ug human Ig per mL beads For isolation of Ig via protein G we recommend the Exosome Immunoprecipitation Protein G
    https://www.bioz.com/result/sheep spinophilin antibody/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sheep spinophilin antibody - by Bioz Stars, 2021-07
    97/100 stars

    Images

    1) Product Images from "Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization"

    Article Title: Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization

    Journal: Proteomes

    doi: 10.3390/proteomes6040053

    Generation and characterization of Cre-expressing, HA-tagged human spinophilin mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.
    Figure Legend Snippet: Generation and characterization of Cre-expressing, HA-tagged human spinophilin mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.

    Techniques Used: Expressing, Mouse Assay, Construct, Sequencing, Clone Assay, Plasmid Preparation, Modification, Transgenic Assay, Transfection, Immunoprecipitation, Western Blot

    Validation of spinophilin interactions. WT or spinophilin KO striatal (STR) or olfactory tubercle (OT) lysates were immunoprecipitated with a spinophilin antibody. Lysates or immunoprecipitates were immunoblotted for spinophilin and three interacting proteins that were detected in the HA immunoprecipitates that had a decreased (SAP102) or increased (Clathrin heavy chain and SRCIN1) interaction with spinophilin in amphetamine-treated animals. Spinophilin and all associated proteins were detected in the spinophilin immunoprecipitates from WT animals, but were absent in immunoprecipitates isolated from KO animals.
    Figure Legend Snippet: Validation of spinophilin interactions. WT or spinophilin KO striatal (STR) or olfactory tubercle (OT) lysates were immunoprecipitated with a spinophilin antibody. Lysates or immunoprecipitates were immunoblotted for spinophilin and three interacting proteins that were detected in the HA immunoprecipitates that had a decreased (SAP102) or increased (Clathrin heavy chain and SRCIN1) interaction with spinophilin in amphetamine-treated animals. Spinophilin and all associated proteins were detected in the spinophilin immunoprecipitates from WT animals, but were absent in immunoprecipitates isolated from KO animals.

    Techniques Used: Immunoprecipitation, Isolation

    Greater abundance of spinophilin interacting proteins in amphetamine-treated animals occurs across both sexes and cell types. ( A ) Principal component analysis of individual samples normalized to spinophilin abundance within each sample and filtered for eight or more PSMs. ( B ) A volcano plot showing a majority of the proteins have increased abundance in HA immunoprecipitates isolated from amphetamine treated animals when normalized to the amphetamine-dependent increase in spinophilin abundance. ( C ) A plot of the abundance of spinophilin interacting proteins isolated from male, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. Left panel shows mean ± standard deviation, the right panel just shows the mean of the two values. ( D ) A plot of the abundance of spinophilin interacting proteins isolated from female, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. ( E ) A plot of the abundance of spinophilin interacting proteins isolated from female, A2A-Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples.
    Figure Legend Snippet: Greater abundance of spinophilin interacting proteins in amphetamine-treated animals occurs across both sexes and cell types. ( A ) Principal component analysis of individual samples normalized to spinophilin abundance within each sample and filtered for eight or more PSMs. ( B ) A volcano plot showing a majority of the proteins have increased abundance in HA immunoprecipitates isolated from amphetamine treated animals when normalized to the amphetamine-dependent increase in spinophilin abundance. ( C ) A plot of the abundance of spinophilin interacting proteins isolated from male, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. Left panel shows mean ± standard deviation, the right panel just shows the mean of the two values. ( D ) A plot of the abundance of spinophilin interacting proteins isolated from female, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. ( E ) A plot of the abundance of spinophilin interacting proteins isolated from female, A2A-Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples.

    Techniques Used: Isolation, Expressing, Standard Deviation

    Quantitation of spinophilin complexes isolated from dMSNs and iMSNs using tandem mass tag (TMT) analysis. ( A ) Striatal lysates isolated from male or female mice expressing HA spinophilin under the control of D1 or A2A promoters and treated with saline or amphetamine were immunoprecipitated with an HA antibody, digested with trypsin, labelled with eight different TMT tags, mixed and analyzed by mass spectrometry (MS/MS). ( B ) A higher intensity of TMT reporter abundance matching spinophilin was observed in amphetamine-treated compared to saline treated animals ( t -test; * p
    Figure Legend Snippet: Quantitation of spinophilin complexes isolated from dMSNs and iMSNs using tandem mass tag (TMT) analysis. ( A ) Striatal lysates isolated from male or female mice expressing HA spinophilin under the control of D1 or A2A promoters and treated with saline or amphetamine were immunoprecipitated with an HA antibody, digested with trypsin, labelled with eight different TMT tags, mixed and analyzed by mass spectrometry (MS/MS). ( B ) A higher intensity of TMT reporter abundance matching spinophilin was observed in amphetamine-treated compared to saline treated animals ( t -test; * p

    Techniques Used: Quantitation Assay, Isolation, Mouse Assay, Expressing, Immunoprecipitation, Mass Spectrometry

    Related Articles

    Immunoprecipitation:

    Article Title: YAP controls retinal stem cell DNA replication timing and genomic stability
    Article Snippet: Co-immunoprecipitation assay and Western blot Western blot were conducted using standard procedures on Xenopus embryo/tadpole protein extracts. .. Immunoprecipitation assays on HEK293T protein extracts were performed with the Dynabeads Protein A Immunoprecipitation Kit (Invitrogen) according to the manufacturer's protocol. .. BiFC analysis For BiFC experiments, plasmids (50 ng each) were transiently transfected in HEK293T cells using lipofectamine 2000 reagent (Invitrogen).

    Article Title: Modulation of Clock Gene Expression by the Transcriptional Coregulator Receptor Interacting Protein 140 (RIP140)
    Article Snippet: The period length (τ) was calculated using the sine fit (damped) function from the LumiCycle analysis software package (Actimetrics), and the phase (φ) was calculated using the second peak after release from serum shock as a reference. .. Immunoprecipitation Proteins were crosslinked using 2 mM DSP (Pierce, Waltham, MA) according to the manufacturer’s instructions for 30 minutes. .. Cells were lysed in SDS lysis buffer (2% SDS, 30 mM NaCl, 10 mM HEPES, pH 7.4, 20 mM NaF, 1 mM NaPPi, 1 mM PMSF, and 1X Complete Protease Inhibitor Cocktail [Roche]).

    Article Title: Nitric oxide prevents H2O2-induced apoptosis in SK-N-MC human neuroblastoma cells
    Article Snippet: .. Immunoprecipitation Immunoprecipitation was performed using an indirect technique involving magnetic Dynabead separation (Dynal ASA, Oslo, Norway) at 4°C. ..

    Article Title: Identification of ROCK1 kinase as a critical regulator of Beclin1 mediated autophagy during metabolic stress
    Article Snippet: For cDNA and siRNA transfection, Lipofectamine 2000 (Invitrogen) and X-tremeGENE (Roche), respectively, was used according to manufacturers’ protocols. .. Immunoblot and immunoprecipitation For endogenous ROCK1 and Beclin1 immunoprecipitation, Crosslink IP kit (Thermo Pierce) was used according to manufacturer’s recommendation with a few changes. .. In short, ROCK1 or Beclin1 antibody was crosslinked to Protein A/G agarose (Santa Cruz) using 450 µM DSS.

    Article Title: The human cytomegalovirus UL116 glycoprotein is a chaperone to control gH-based complexes levels on virions
    Article Snippet: HEK-293T transfections were carried out with Lipofectamine 2000 (Thermo Fischer) according to the manufacturer’s protocol. .. The HEK-293T transfected cells were trypsinized 48h post-transfection and treated for immunoprecipitation assays. gH_myc, UL116 and UL148-6XHIS were expressed following cloning of the codon optimized sequence in pcDNA3.1(−) plasmid. .. Binding assay to HFF-1 and ARPE-19 cells For the binding of gH/UL116, Trimer and Pentamer to cells, trypsinized HFF-1 or ARPE-19 were divided in identical aliquot of 3 × 105 cells.

    Article Title: The Herpes Simplex Virus Type 1 UL20 Protein and the Amino Terminus of Glycoprotein K (gK) Physically Interact with gB ▿
    Article Snippet: The cells collected from one T75 flask were washed with phosphate-buffered saline (PBS) and lysed for 30 min on ice with 1 ml of NP-40 lysis buffer (Invitrogen) supplemented with phenylmethylsulfonyl fluoride (PMSF) (Sigma-Aldrich) and a cocktail of protease inhibitors (Roche Diagnostics, Indianapolis, IN). .. Immunoprecipitation reactions were performed by using Dynabeads protein G (Invitrogen) according to the manufacturer's instructions. .. Briefly, 50 μl of Dynabeads was incubated for 10 min at room temperature with either 2 μl of anti-V5 antibody (Invitrogen) or 1 μl of anti-FLAG antibody (Sigma-Aldrich) for each reaction.

    Article Title: P2A-Fluorophore Tagging of BRAF Tightly Links Expression to Fluorescence In Vivo
    Article Snippet: .. Immunoprecipitation Protein preparation: Snap-frozen brains and lungs were homogenized on ice in a glass tissue homogenizer containing immunoprecipitation lysis buffer (1% NP-40, 10% glycerol, 20 mM Tris pH 8, 137 mM Sodium Chloride, 1 mM Magnesium Chloride, 0.5 mM EDTA, 10 mM Sodium Pyrophosphate) supplemented with Halt Protease and Phosphatase Inhibitor Cocktail (Life Technologies, 78446). .. After homogenization, samples were lysed on ice for one hour and centrifuged at 14,000 rpm and 4°C for 10 minutes to pellet tissue debris.

    Article Title: CD28 Promotes Plasma Cell Survival, Sustained Antibody Responses, and BLIMP-1 Upregulation through Its Distal PYAP Proline Motif
    Article Snippet: For the immunoprecipitations, 1 × 107 J558/conditions were activated with control hamster Ig (10 μg/ml) or anti-CD28 mAb (PV1.1, 2 μl/100 μl) for 15 min, then lysed in radioimmunoprecipitation assay buffer. .. A total of 1–10 μg primary immunoprecipitation Ab (CD28 or phosphotyrosine) was incubated with the protein lysate for 2–4 h, and immunocomplexes were captured by rProtein G agarose (Invitrogen) and analyzed by Western blot for the p85 subunit of PI3K or for Vav1, as detailed above. .. BM chimeras were generated as previously described ( ); briefly, the chimeras were generated by retro-orbitally injecting 106 BM cells, depleted of T cells (Miltenyi Biotec), at a 40:60 ratio of μMT and WT, μMT and CD28−/− , μMT and CD28-AYAA, or μMT and CD28-Y170F BM into lethally irradiated WT mice.

    Transfection:

    Article Title: The human cytomegalovirus UL116 glycoprotein is a chaperone to control gH-based complexes levels on virions
    Article Snippet: HEK-293T transfections were carried out with Lipofectamine 2000 (Thermo Fischer) according to the manufacturer’s protocol. .. The HEK-293T transfected cells were trypsinized 48h post-transfection and treated for immunoprecipitation assays. gH_myc, UL116 and UL148-6XHIS were expressed following cloning of the codon optimized sequence in pcDNA3.1(−) plasmid. .. Binding assay to HFF-1 and ARPE-19 cells For the binding of gH/UL116, Trimer and Pentamer to cells, trypsinized HFF-1 or ARPE-19 were divided in identical aliquot of 3 × 105 cells.

    Clone Assay:

    Article Title: The human cytomegalovirus UL116 glycoprotein is a chaperone to control gH-based complexes levels on virions
    Article Snippet: HEK-293T transfections were carried out with Lipofectamine 2000 (Thermo Fischer) according to the manufacturer’s protocol. .. The HEK-293T transfected cells were trypsinized 48h post-transfection and treated for immunoprecipitation assays. gH_myc, UL116 and UL148-6XHIS were expressed following cloning of the codon optimized sequence in pcDNA3.1(−) plasmid. .. Binding assay to HFF-1 and ARPE-19 cells For the binding of gH/UL116, Trimer and Pentamer to cells, trypsinized HFF-1 or ARPE-19 were divided in identical aliquot of 3 × 105 cells.

    Sequencing:

    Article Title: The human cytomegalovirus UL116 glycoprotein is a chaperone to control gH-based complexes levels on virions
    Article Snippet: HEK-293T transfections were carried out with Lipofectamine 2000 (Thermo Fischer) according to the manufacturer’s protocol. .. The HEK-293T transfected cells were trypsinized 48h post-transfection and treated for immunoprecipitation assays. gH_myc, UL116 and UL148-6XHIS were expressed following cloning of the codon optimized sequence in pcDNA3.1(−) plasmid. .. Binding assay to HFF-1 and ARPE-19 cells For the binding of gH/UL116, Trimer and Pentamer to cells, trypsinized HFF-1 or ARPE-19 were divided in identical aliquot of 3 × 105 cells.

    Plasmid Preparation:

    Article Title: The human cytomegalovirus UL116 glycoprotein is a chaperone to control gH-based complexes levels on virions
    Article Snippet: HEK-293T transfections were carried out with Lipofectamine 2000 (Thermo Fischer) according to the manufacturer’s protocol. .. The HEK-293T transfected cells were trypsinized 48h post-transfection and treated for immunoprecipitation assays. gH_myc, UL116 and UL148-6XHIS were expressed following cloning of the codon optimized sequence in pcDNA3.1(−) plasmid. .. Binding assay to HFF-1 and ARPE-19 cells For the binding of gH/UL116, Trimer and Pentamer to cells, trypsinized HFF-1 or ARPE-19 were divided in identical aliquot of 3 × 105 cells.

    Lysis:

    Article Title: P2A-Fluorophore Tagging of BRAF Tightly Links Expression to Fluorescence In Vivo
    Article Snippet: .. Immunoprecipitation Protein preparation: Snap-frozen brains and lungs were homogenized on ice in a glass tissue homogenizer containing immunoprecipitation lysis buffer (1% NP-40, 10% glycerol, 20 mM Tris pH 8, 137 mM Sodium Chloride, 1 mM Magnesium Chloride, 0.5 mM EDTA, 10 mM Sodium Pyrophosphate) supplemented with Halt Protease and Phosphatase Inhibitor Cocktail (Life Technologies, 78446). .. After homogenization, samples were lysed on ice for one hour and centrifuged at 14,000 rpm and 4°C for 10 minutes to pellet tissue debris.

    Incubation:

    Article Title: CD28 Promotes Plasma Cell Survival, Sustained Antibody Responses, and BLIMP-1 Upregulation through Its Distal PYAP Proline Motif
    Article Snippet: For the immunoprecipitations, 1 × 107 J558/conditions were activated with control hamster Ig (10 μg/ml) or anti-CD28 mAb (PV1.1, 2 μl/100 μl) for 15 min, then lysed in radioimmunoprecipitation assay buffer. .. A total of 1–10 μg primary immunoprecipitation Ab (CD28 or phosphotyrosine) was incubated with the protein lysate for 2–4 h, and immunocomplexes were captured by rProtein G agarose (Invitrogen) and analyzed by Western blot for the p85 subunit of PI3K or for Vav1, as detailed above. .. BM chimeras were generated as previously described ( ); briefly, the chimeras were generated by retro-orbitally injecting 106 BM cells, depleted of T cells (Miltenyi Biotec), at a 40:60 ratio of μMT and WT, μMT and CD28−/− , μMT and CD28-AYAA, or μMT and CD28-Y170F BM into lethally irradiated WT mice.

    Western Blot:

    Article Title: CD28 Promotes Plasma Cell Survival, Sustained Antibody Responses, and BLIMP-1 Upregulation through Its Distal PYAP Proline Motif
    Article Snippet: For the immunoprecipitations, 1 × 107 J558/conditions were activated with control hamster Ig (10 μg/ml) or anti-CD28 mAb (PV1.1, 2 μl/100 μl) for 15 min, then lysed in radioimmunoprecipitation assay buffer. .. A total of 1–10 μg primary immunoprecipitation Ab (CD28 or phosphotyrosine) was incubated with the protein lysate for 2–4 h, and immunocomplexes were captured by rProtein G agarose (Invitrogen) and analyzed by Western blot for the p85 subunit of PI3K or for Vav1, as detailed above. .. BM chimeras were generated as previously described ( ); briefly, the chimeras were generated by retro-orbitally injecting 106 BM cells, depleted of T cells (Miltenyi Biotec), at a 40:60 ratio of μMT and WT, μMT and CD28−/− , μMT and CD28-AYAA, or μMT and CD28-Y170F BM into lethally irradiated WT mice.

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    Thermo Fisher sheep spinophilin antibody
    Generation and characterization of Cre-expressing, HA-tagged human <t>spinophilin</t> mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.
    Sheep Spinophilin Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep spinophilin antibody/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sheep spinophilin antibody - by Bioz Stars, 2021-07
    97/100 stars
      Buy from Supplier

    Image Search Results


    Generation and characterization of Cre-expressing, HA-tagged human spinophilin mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.

    Journal: Proteomes

    Article Title: Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization

    doi: 10.3390/proteomes6040053

    Figure Lengend Snippet: Generation and characterization of Cre-expressing, HA-tagged human spinophilin mice. ( A ) A construct containing DNA encoding HA-tagged human spinophilin with a P2A sequence and mNeptune3 fluorescent protein was cloned into the pBIGT vector that contains a floxed-stop sequence. ( B ) The construct encoding the floxed-stop sequence and the HA-spinophilin-P2A-mNeptune 3 sequence was subcloned into the ROSA targeting vector pROSA_26.PA. ( C ) The modified ROSA vector was used for generation of the targeted transgenic mice. ( D ) Striatal cells were transfected without or with HA-tagged human spinophilin. Lysates were immunoprecipitated with either an HA or spinophilin antibody and immunoblotted with an HA antibody or a spinophilin antibody. HA-spinophilin was selectively detected when it was overexpressed. ( E ) Mice express HA-tagged spinophilin upon crossing with Cre recombinase expressed in the direct pathway (D1) or indirect pathway (A2A) medium spiny neurons. ( F ) Spinophilin and protein phosphatase 1 immunoblots of inputs and HA-immunoprecipitates from HA spinophilin mice crossed with D1 or A2A Cre-recombinase-expressing mice. ( G ) Mice expressing HA-spinophilin had non-significant increases in total spinophilin expression.

    Article Snippet: Striatal cell lysates were immunoprecipitated with 1.6 µg of a sheep spinophilin antibody (ThermoFisher Scientific).

    Techniques: Expressing, Mouse Assay, Construct, Sequencing, Clone Assay, Plasmid Preparation, Modification, Transgenic Assay, Transfection, Immunoprecipitation, Western Blot

    Validation of spinophilin interactions. WT or spinophilin KO striatal (STR) or olfactory tubercle (OT) lysates were immunoprecipitated with a spinophilin antibody. Lysates or immunoprecipitates were immunoblotted for spinophilin and three interacting proteins that were detected in the HA immunoprecipitates that had a decreased (SAP102) or increased (Clathrin heavy chain and SRCIN1) interaction with spinophilin in amphetamine-treated animals. Spinophilin and all associated proteins were detected in the spinophilin immunoprecipitates from WT animals, but were absent in immunoprecipitates isolated from KO animals.

    Journal: Proteomes

    Article Title: Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization

    doi: 10.3390/proteomes6040053

    Figure Lengend Snippet: Validation of spinophilin interactions. WT or spinophilin KO striatal (STR) or olfactory tubercle (OT) lysates were immunoprecipitated with a spinophilin antibody. Lysates or immunoprecipitates were immunoblotted for spinophilin and three interacting proteins that were detected in the HA immunoprecipitates that had a decreased (SAP102) or increased (Clathrin heavy chain and SRCIN1) interaction with spinophilin in amphetamine-treated animals. Spinophilin and all associated proteins were detected in the spinophilin immunoprecipitates from WT animals, but were absent in immunoprecipitates isolated from KO animals.

    Article Snippet: Striatal cell lysates were immunoprecipitated with 1.6 µg of a sheep spinophilin antibody (ThermoFisher Scientific).

    Techniques: Immunoprecipitation, Isolation

    Greater abundance of spinophilin interacting proteins in amphetamine-treated animals occurs across both sexes and cell types. ( A ) Principal component analysis of individual samples normalized to spinophilin abundance within each sample and filtered for eight or more PSMs. ( B ) A volcano plot showing a majority of the proteins have increased abundance in HA immunoprecipitates isolated from amphetamine treated animals when normalized to the amphetamine-dependent increase in spinophilin abundance. ( C ) A plot of the abundance of spinophilin interacting proteins isolated from male, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. Left panel shows mean ± standard deviation, the right panel just shows the mean of the two values. ( D ) A plot of the abundance of spinophilin interacting proteins isolated from female, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. ( E ) A plot of the abundance of spinophilin interacting proteins isolated from female, A2A-Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples.

    Journal: Proteomes

    Article Title: Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization

    doi: 10.3390/proteomes6040053

    Figure Lengend Snippet: Greater abundance of spinophilin interacting proteins in amphetamine-treated animals occurs across both sexes and cell types. ( A ) Principal component analysis of individual samples normalized to spinophilin abundance within each sample and filtered for eight or more PSMs. ( B ) A volcano plot showing a majority of the proteins have increased abundance in HA immunoprecipitates isolated from amphetamine treated animals when normalized to the amphetamine-dependent increase in spinophilin abundance. ( C ) A plot of the abundance of spinophilin interacting proteins isolated from male, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. Left panel shows mean ± standard deviation, the right panel just shows the mean of the two values. ( D ) A plot of the abundance of spinophilin interacting proteins isolated from female, D1 Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples. ( E ) A plot of the abundance of spinophilin interacting proteins isolated from female, A2A-Cre expressing animals and normalized for spinophilin expression ( Table S2 ) and quantified from treated (Y-axis) or control (X-axis) samples.

    Article Snippet: Striatal cell lysates were immunoprecipitated with 1.6 µg of a sheep spinophilin antibody (ThermoFisher Scientific).

    Techniques: Isolation, Expressing, Standard Deviation

    Quantitation of spinophilin complexes isolated from dMSNs and iMSNs using tandem mass tag (TMT) analysis. ( A ) Striatal lysates isolated from male or female mice expressing HA spinophilin under the control of D1 or A2A promoters and treated with saline or amphetamine were immunoprecipitated with an HA antibody, digested with trypsin, labelled with eight different TMT tags, mixed and analyzed by mass spectrometry (MS/MS). ( B ) A higher intensity of TMT reporter abundance matching spinophilin was observed in amphetamine-treated compared to saline treated animals ( t -test; * p

    Journal: Proteomes

    Article Title: Proteomic Analysis of the Spinophilin Interactome in Rodent Striatum Following Psychostimulant Sensitization

    doi: 10.3390/proteomes6040053

    Figure Lengend Snippet: Quantitation of spinophilin complexes isolated from dMSNs and iMSNs using tandem mass tag (TMT) analysis. ( A ) Striatal lysates isolated from male or female mice expressing HA spinophilin under the control of D1 or A2A promoters and treated with saline or amphetamine were immunoprecipitated with an HA antibody, digested with trypsin, labelled with eight different TMT tags, mixed and analyzed by mass spectrometry (MS/MS). ( B ) A higher intensity of TMT reporter abundance matching spinophilin was observed in amphetamine-treated compared to saline treated animals ( t -test; * p

    Article Snippet: Striatal cell lysates were immunoprecipitated with 1.6 µg of a sheep spinophilin antibody (ThermoFisher Scientific).

    Techniques: Quantitation Assay, Isolation, Mouse Assay, Expressing, Immunoprecipitation, Mass Spectrometry