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calf intestinal phosphatase  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology calf intestinal phosphatase
    Calf Intestinal Phosphatase, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 13833 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lambda+protein+phosphatase+buffer/Protein+A%2FG+PLUS-Agarose/pmc08494485-74-7-15
    Average 96 stars, based on 13833 article reviews
    calf intestinal phosphatase - by Bioz Stars, 2026-09
    96/100 stars

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    Incubation:

    Article Title: Voltage-dependent anion channel 1 oligomerization regulates PANoptosis in retinal ischemia–reperfusion injury
    Article Snippet: Pierce immunoprecipitation lysis buffer (Beyotime, Cat# P0013) was used to lyse the R28 cells. .. Antibodies (rabbit anti-ASC/TMS1, 1 μg/mL, Bioworld Technology, Cat# BS80036, RRID: AB_3251477) were added to the lysates with protein A + G agarose (Santa Cruz Biotechnology, Inc., Dallas, TX, USA), and the mixture was incubated at 4°C overnight. .. Next, the mixture was centrifuged, and the precipitate was washed three times with dilution/wash buffer and resuspended in 1× sodium dodecyl sulfate polyacrylamide gel electrophoresis loading buffer (CWBio, Cat# CW0027S).

    Article Title: SIRT7 facilitates ferroptosis resistance of melanocytes via activating the SMAD3-ATF3-GPX4 signaling pathway in vitiligo
    Article Snippet: .. For immunoprecipitation, 5–10 μL of SMAD3 antibody (9523S, Cell Signaling Technology, MA, USA), SIRT7 antibody (12994-1-AP, Proteintech, Wuhan, China) or control IgG (30000–0-AP, Proteintech) was mixed with the protein supernatant and incubated at 4°C for 2 h. Then, 25 μL of protein A/G PLUS-Agarose (sc-2003, Santa Cruz Biotechnology, Beijing, China) was mixed with protein lysates. ..

    Western Blot:

    Article Title: BCL2-overexpression in donor lymphocytes reduces the risk of graft-versus-host disease.
    Article Snippet: .. 75 Co-immunoprecipitation and Western blotting: for Co-IP 25 μl of protein A/G (Protein 76 A/G PLUS-Agarose, sc-2003, Santa Cruz) was mixed with the anti-BCL2 antibody (15071S, Cell 77 Signalling) for 2 h at 4o C in rotation. ..

    Co-Immunoprecipitation Assay:

    Article Title: BCL2-overexpression in donor lymphocytes reduces the risk of graft-versus-host disease.
    Article Snippet: .. 75 Co-immunoprecipitation and Western blotting: for Co-IP 25 μl of protein A/G (Protein 76 A/G PLUS-Agarose, sc-2003, Santa Cruz) was mixed with the anti-BCL2 antibody (15071S, Cell 77 Signalling) for 2 h at 4o C in rotation. ..

    other:

    Article Title: YY1 nitration participates in DbCM cardiomyocyte lipotoxicity by inhibiting ANXA3 -induced microlipophagy
    Article Snippet: Then added 50 μl Protein A/G PLUS-Agarose (Santa Cruz Biotechnology, sc-2003) to co-incubated for 6 h. Centrifuge at 2500g for 5 min, taking the sediment.

    Article Title: YY1 nitration participates in DbCM cardiomyocyte lipotoxicity by inhibiting ANXA3 -induced microlipophagy
    Article Snippet: Then the protein lysis buffer was gently mixed with 20 μl Protein A/G PLUS-Agarose (Santa Cruz Biotechnology, sc-2003) at 4 °C for 2 h. Centrifuge at 2500g for 5 min at 4 °C, taking the supernatant, and add 2.5 μg anti-Flag antibody (Medical and Biological Laboratories co., M185-3L) with gentle mixing for 8 h at 4 °C.

    Immunoprecipitation:

    Article Title: SIRT7 facilitates ferroptosis resistance of melanocytes via activating the SMAD3-ATF3-GPX4 signaling pathway in vitiligo
    Article Snippet: .. For immunoprecipitation, 5–10 μL of SMAD3 antibody (9523S, Cell Signaling Technology, MA, USA), SIRT7 antibody (12994-1-AP, Proteintech, Wuhan, China) or control IgG (30000–0-AP, Proteintech) was mixed with the protein supernatant and incubated at 4°C for 2 h. Then, 25 μL of protein A/G PLUS-Agarose (sc-2003, Santa Cruz Biotechnology, Beijing, China) was mixed with protein lysates. ..

    Control:

    Article Title: SIRT7 facilitates ferroptosis resistance of melanocytes via activating the SMAD3-ATF3-GPX4 signaling pathway in vitiligo
    Article Snippet: .. For immunoprecipitation, 5–10 μL of SMAD3 antibody (9523S, Cell Signaling Technology, MA, USA), SIRT7 antibody (12994-1-AP, Proteintech, Wuhan, China) or control IgG (30000–0-AP, Proteintech) was mixed with the protein supernatant and incubated at 4°C for 2 h. Then, 25 μL of protein A/G PLUS-Agarose (sc-2003, Santa Cruz Biotechnology, Beijing, China) was mixed with protein lysates. ..



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    (A) Western blot analysis of cleared bacterial lysates of GST-PFKFB2 and mutants. Top: Total protein staining of cleared bacterial lysates over-expressing GST-PFKFB2 and mutants. Bottom: Western blots against GST and phosphorylated-PFKFB2 (Ser483) for GST-PFKFB2 and mutants. “Double mut” indicates protein containing both K174G and H259A. (B) Western blot analysis of GST-PFKFB2 expression, purification, and in vitro phosphorylation. Flow thru indicates proteins unbound to GSH beads. Column are proteins bound to the GSH beads. Column + Thrombin are proteins remaining bound to GSH beads after thrombin cleavage. Purified PFK2 lanes are proteins eluted from the GSH beads with thrombin cleavage. Purified PFK2 + ATP are proteins incubated with ATP alone. Purified PFK2 + ATP + PKA are proteins phosphorylated by PKA. (C) Western blot analysis of GST-PFKFB2 and mutant proteins showing they are phosphorylated (Ser483) upon extraction from bacteria ( left lanes ), lose phosphorylation after purification ( middle lanes ), but are re-phosphorylated upon treatment with PKA and ATP ( right lanes ). (D) Representative western blot against phosphorylated-PFKFB2 (Ser483) of bacterial samples (WT PFKFB2) treated/not treated with <t>λ-phosphatase</t> for indicated times before lysis. Equal amounts of purified PFKFB2 were treated and loaded into each lane. Quantitation of bacterial samples treated with λ-phosphatase. Data are shown as mean±SD. The original, unedited blots are included in .
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    (A) Western blot analysis of cleared bacterial lysates of GST-PFKFB2 and mutants. Top: Total protein staining of cleared bacterial lysates over-expressing GST-PFKFB2 and mutants. Bottom: Western blots against GST and phosphorylated-PFKFB2 (Ser483) for GST-PFKFB2 and mutants. “Double mut” indicates protein containing both K174G and H259A. (B) Western blot analysis of GST-PFKFB2 expression, purification, and in vitro phosphorylation. Flow thru indicates proteins unbound to GSH beads. Column are proteins bound to the GSH beads. Column + Thrombin are proteins remaining bound to GSH beads after thrombin cleavage. Purified PFK2 lanes are proteins eluted from the GSH beads with thrombin cleavage. Purified PFK2 + ATP are proteins incubated with ATP alone. Purified PFK2 + ATP + PKA are proteins phosphorylated by PKA. (C) Western blot analysis of GST-PFKFB2 and mutant proteins showing they are phosphorylated (Ser483) upon extraction from bacteria ( left lanes ), lose phosphorylation after purification ( middle lanes ), but are re-phosphorylated upon treatment with PKA and ATP ( right lanes ). (D) Representative western blot against phosphorylated-PFKFB2 (Ser483) of bacterial samples (WT PFKFB2) treated/not treated with <t>λ-phosphatase</t> for indicated times before lysis. Equal amounts of purified PFKFB2 were treated and loaded into each lane. Quantitation of bacterial samples treated with λ-phosphatase. Data are shown as mean±SD. The original, unedited blots are included in .
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    Image Search Results


    (A) Western blot analysis of cleared bacterial lysates of GST-PFKFB2 and mutants. Top: Total protein staining of cleared bacterial lysates over-expressing GST-PFKFB2 and mutants. Bottom: Western blots against GST and phosphorylated-PFKFB2 (Ser483) for GST-PFKFB2 and mutants. “Double mut” indicates protein containing both K174G and H259A. (B) Western blot analysis of GST-PFKFB2 expression, purification, and in vitro phosphorylation. Flow thru indicates proteins unbound to GSH beads. Column are proteins bound to the GSH beads. Column + Thrombin are proteins remaining bound to GSH beads after thrombin cleavage. Purified PFK2 lanes are proteins eluted from the GSH beads with thrombin cleavage. Purified PFK2 + ATP are proteins incubated with ATP alone. Purified PFK2 + ATP + PKA are proteins phosphorylated by PKA. (C) Western blot analysis of GST-PFKFB2 and mutant proteins showing they are phosphorylated (Ser483) upon extraction from bacteria ( left lanes ), lose phosphorylation after purification ( middle lanes ), but are re-phosphorylated upon treatment with PKA and ATP ( right lanes ). (D) Representative western blot against phosphorylated-PFKFB2 (Ser483) of bacterial samples (WT PFKFB2) treated/not treated with λ-phosphatase for indicated times before lysis. Equal amounts of purified PFKFB2 were treated and loaded into each lane. Quantitation of bacterial samples treated with λ-phosphatase. Data are shown as mean±SD. The original, unedited blots are included in .

    Journal: PLOS One

    Article Title: Mechanistic studies of PFKFB2 reveal a novel inhibitor of its kinase activity

    doi: 10.1371/journal.pone.0317167

    Figure Lengend Snippet: (A) Western blot analysis of cleared bacterial lysates of GST-PFKFB2 and mutants. Top: Total protein staining of cleared bacterial lysates over-expressing GST-PFKFB2 and mutants. Bottom: Western blots against GST and phosphorylated-PFKFB2 (Ser483) for GST-PFKFB2 and mutants. “Double mut” indicates protein containing both K174G and H259A. (B) Western blot analysis of GST-PFKFB2 expression, purification, and in vitro phosphorylation. Flow thru indicates proteins unbound to GSH beads. Column are proteins bound to the GSH beads. Column + Thrombin are proteins remaining bound to GSH beads after thrombin cleavage. Purified PFK2 lanes are proteins eluted from the GSH beads with thrombin cleavage. Purified PFK2 + ATP are proteins incubated with ATP alone. Purified PFK2 + ATP + PKA are proteins phosphorylated by PKA. (C) Western blot analysis of GST-PFKFB2 and mutant proteins showing they are phosphorylated (Ser483) upon extraction from bacteria ( left lanes ), lose phosphorylation after purification ( middle lanes ), but are re-phosphorylated upon treatment with PKA and ATP ( right lanes ). (D) Representative western blot against phosphorylated-PFKFB2 (Ser483) of bacterial samples (WT PFKFB2) treated/not treated with λ-phosphatase for indicated times before lysis. Equal amounts of purified PFKFB2 were treated and loaded into each lane. Quantitation of bacterial samples treated with λ-phosphatase. Data are shown as mean±SD. The original, unedited blots are included in .

    Article Snippet: Assay conditions were 100 µL sonicated sample, 10 µL MnCl 2 (10 mM NEB), 10 µL phosphatase buffer (10x PMP buffer, NEB) with or without 2 µL Lambda protein phosphatase (NEB, 400000 U/mL).

    Techniques: Western Blot, Staining, Expressing, Purification, In Vitro, Phospho-proteomics, Incubation, Mutagenesis, Extraction, Bacteria, Lysis, Quantitation Assay