Review



phorbol 12 myristate 13 acetate pma  (Sino Biological)


Bioz Verified Symbol Sino Biological is a verified supplier
Bioz Manufacturer Symbol Sino Biological manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 94
      Buy from Supplier

    Structured Review

    Sino Biological phorbol 12 myristate 13 acetate pma
    Phorbol 12 Myristate 13 Acetate Pma, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p61/Phorbol-12-myristate-13+acetate/pm41639044-211-13-32
    Average 94 stars, based on 12 article reviews
    phorbol 12 myristate 13 acetate pma - by Bioz Stars, 2026-09
    94/100 stars

    Images

    Related Articles

    Recombinant:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Fluorescence:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Isolation:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Double Knockout:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Mutagenesis:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Plasmid Preparation:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.

    Software:

    Article Title: Epinephrine inhibits PI3Kα via the Hippo kinases
    Article Snippet: PKCA , SignalChem , P61–18G.



    Similar Products

    phorbol 12 myristate 13 acetate pma  (Sino Biological)
    94
    Sino Biological phorbol 12 myristate 13 acetate pma
    Phorbol 12 Myristate 13 Acetate Pma, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p61/Phorbol-12-myristate-13+acetate/pm41639044-211-13-32
    Average 94 stars, based on 1 article reviews
    phorbol 12 myristate 13 acetate pma - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    phorbol 12 myristate 13 acetate  (Sino Biological)
    94
    Sino Biological phorbol 12 myristate 13 acetate
    Phorbol 12 Myristate 13 Acetate, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p61/Phorbol-12-myristate-13+acetate/pmc12910970-56-8-30
    Average 94 stars, based on 1 article reviews
    phorbol 12 myristate 13 acetate - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    poly glu tyr peptide  (Sino Biological)
    93
    Sino Biological poly glu tyr peptide
    Poly Glu Tyr Peptide, supplied by Sino Biological, 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/product/p61/Poly+(4%3A1+Glu%2C+Tyr)+Peptide/10__3390_slash_ijms27010329-225-0-8
    Average 93 stars, based on 1 article reviews
    poly glu tyr peptide - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier
    pkcα  (Sino Biological)
    93
    Sino Biological pkcα
    A) 20 ng <t>GST-PKCα</t> WT , GST-PKCα D463H , GST-PKCα D463N was subject to in vitro kinase assay against MARCKS peptide substrate for 5 min in the presence or absence of activators DG/PS and Ca 2+ . B) Myc-PKCα WT or Myc-PKCα D463H were isolated by immunoprecipitation from HEK293T cells. Proteins were subject to kinase assay for 30 min across a peptide array of PKCα substrates, incubated <t>with</t> <t>purified</t> PKC, PKC activators DG/PS, Calcium and PMA, and ATP [γ-32P]. Array was imaged by autoradiography. C) Autoradiography intensities of peptide spots from D) normalized to scrambled peptide negative controls, n=3. D) Quantification of normalized autoradiography intensities from D), n=3, bar represents mean intensity across all replicates. (**** p < 0.0001, two-tailed Mann-Whitney test) E) Domain Structure of PKCα. PKCα is a member of the conventional PKC family, with 2 tandem DG-binding C1 domains (orange), and a Ca 2+ -binding C2 domain (yellow). Catalysis is performed by a kinase domain (blue) and regulated by an AGC C-tail and an N-terminal pseudosubstrate (red), which sits in the active site in the absence of agonist. Phosphorylation occurs at the activation loop (pink), turn motif (orange) and hydrophobic motif (green). F) COS7 cells were transfected for 48 h with HA-empty, or HA-PKCα constructs indicated, before lysis and probing for processing phosphosites by western blot. G) Quantification of HA-PKCα upper band intensity, relative to total HA-PKCα. Bars represent mean +/- SEM from n=3 experiments (**** p < 0.0001, 1-way ANOVA and Tukey multiple comparisons test).
    Pkcα, supplied by Sino Biological, 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/product/p61/PKC+alpha%2C+Active/bio_rxiv__2025__05__30__657104-297-2-3
    Average 93 stars, based on 1 article reviews
    pkcα - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier
    pma  (Sino Biological)
    94
    Sino Biological pma
    A) 20 ng <t>GST-PKCα</t> WT , GST-PKCα D463H , GST-PKCα D463N was subject to in vitro kinase assay against MARCKS peptide substrate for 5 min in the presence or absence of activators DG/PS and Ca 2+ . B) Myc-PKCα WT or Myc-PKCα D463H were isolated by immunoprecipitation from HEK293T cells. Proteins were subject to kinase assay for 30 min across a peptide array of PKCα substrates, incubated <t>with</t> <t>purified</t> PKC, PKC activators DG/PS, Calcium and PMA, and ATP [γ-32P]. Array was imaged by autoradiography. C) Autoradiography intensities of peptide spots from D) normalized to scrambled peptide negative controls, n=3. D) Quantification of normalized autoradiography intensities from D), n=3, bar represents mean intensity across all replicates. (**** p < 0.0001, two-tailed Mann-Whitney test) E) Domain Structure of PKCα. PKCα is a member of the conventional PKC family, with 2 tandem DG-binding C1 domains (orange), and a Ca 2+ -binding C2 domain (yellow). Catalysis is performed by a kinase domain (blue) and regulated by an AGC C-tail and an N-terminal pseudosubstrate (red), which sits in the active site in the absence of agonist. Phosphorylation occurs at the activation loop (pink), turn motif (orange) and hydrophobic motif (green). F) COS7 cells were transfected for 48 h with HA-empty, or HA-PKCα constructs indicated, before lysis and probing for processing phosphosites by western blot. G) Quantification of HA-PKCα upper band intensity, relative to total HA-PKCα. Bars represent mean +/- SEM from n=3 experiments (**** p < 0.0001, 1-way ANOVA and Tukey multiple comparisons test).
    Pma, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p61/Phorbol-12-myristate-13+acetate/pm40281576-97-6-8
    Average 94 stars, based on 1 article reviews
    pma - by Bioz Stars, 2026-09
    94/100 stars
    		  Buy from Supplier
    btk substrate  (Sino Biological)
    93
    Sino Biological btk substrate
    A) 20 ng <t>GST-PKCα</t> WT , GST-PKCα D463H , GST-PKCα D463N was subject to in vitro kinase assay against MARCKS peptide substrate for 5 min in the presence or absence of activators DG/PS and Ca 2+ . B) Myc-PKCα WT or Myc-PKCα D463H were isolated by immunoprecipitation from HEK293T cells. Proteins were subject to kinase assay for 30 min across a peptide array of PKCα substrates, incubated <t>with</t> <t>purified</t> PKC, PKC activators DG/PS, Calcium and PMA, and ATP [γ-32P]. Array was imaged by autoradiography. C) Autoradiography intensities of peptide spots from D) normalized to scrambled peptide negative controls, n=3. D) Quantification of normalized autoradiography intensities from D), n=3, bar represents mean intensity across all replicates. (**** p < 0.0001, two-tailed Mann-Whitney test) E) Domain Structure of PKCα. PKCα is a member of the conventional PKC family, with 2 tandem DG-binding C1 domains (orange), and a Ca 2+ -binding C2 domain (yellow). Catalysis is performed by a kinase domain (blue) and regulated by an AGC C-tail and an N-terminal pseudosubstrate (red), which sits in the active site in the absence of agonist. Phosphorylation occurs at the activation loop (pink), turn motif (orange) and hydrophobic motif (green). F) COS7 cells were transfected for 48 h with HA-empty, or HA-PKCα constructs indicated, before lysis and probing for processing phosphosites by western blot. G) Quantification of HA-PKCα upper band intensity, relative to total HA-PKCα. Bars represent mean +/- SEM from n=3 experiments (**** p < 0.0001, 1-way ANOVA and Tukey multiple comparisons test).
    Btk Substrate, supplied by Sino Biological, 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/product/p61/Poly+(4%3A1+Glu%2C+Tyr)+Peptide/us12162873-1256-52-54
    Average 93 stars, based on 1 article reviews
    btk substrate - by Bioz Stars, 2026-09
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    A) 20 ng GST-PKCα WT , GST-PKCα D463H , GST-PKCα D463N was subject to in vitro kinase assay against MARCKS peptide substrate for 5 min in the presence or absence of activators DG/PS and Ca 2+ . B) Myc-PKCα WT or Myc-PKCα D463H were isolated by immunoprecipitation from HEK293T cells. Proteins were subject to kinase assay for 30 min across a peptide array of PKCα substrates, incubated with purified PKC, PKC activators DG/PS, Calcium and PMA, and ATP [γ-32P]. Array was imaged by autoradiography. C) Autoradiography intensities of peptide spots from D) normalized to scrambled peptide negative controls, n=3. D) Quantification of normalized autoradiography intensities from D), n=3, bar represents mean intensity across all replicates. (**** p < 0.0001, two-tailed Mann-Whitney test) E) Domain Structure of PKCα. PKCα is a member of the conventional PKC family, with 2 tandem DG-binding C1 domains (orange), and a Ca 2+ -binding C2 domain (yellow). Catalysis is performed by a kinase domain (blue) and regulated by an AGC C-tail and an N-terminal pseudosubstrate (red), which sits in the active site in the absence of agonist. Phosphorylation occurs at the activation loop (pink), turn motif (orange) and hydrophobic motif (green). F) COS7 cells were transfected for 48 h with HA-empty, or HA-PKCα constructs indicated, before lysis and probing for processing phosphosites by western blot. G) Quantification of HA-PKCα upper band intensity, relative to total HA-PKCα. Bars represent mean +/- SEM from n=3 experiments (**** p < 0.0001, 1-way ANOVA and Tukey multiple comparisons test).

    Journal: bioRxiv

    Article Title: A Catalytically Inactive Protein Kinase C alpha Mutation Drives Chordoid Glioma by Pathway Rewiring

    doi: 10.1101/2025.05.30.657104

    Figure Lengend Snippet: A) 20 ng GST-PKCα WT , GST-PKCα D463H , GST-PKCα D463N was subject to in vitro kinase assay against MARCKS peptide substrate for 5 min in the presence or absence of activators DG/PS and Ca 2+ . B) Myc-PKCα WT or Myc-PKCα D463H were isolated by immunoprecipitation from HEK293T cells. Proteins were subject to kinase assay for 30 min across a peptide array of PKCα substrates, incubated with purified PKC, PKC activators DG/PS, Calcium and PMA, and ATP [γ-32P]. Array was imaged by autoradiography. C) Autoradiography intensities of peptide spots from D) normalized to scrambled peptide negative controls, n=3. D) Quantification of normalized autoradiography intensities from D), n=3, bar represents mean intensity across all replicates. (**** p < 0.0001, two-tailed Mann-Whitney test) E) Domain Structure of PKCα. PKCα is a member of the conventional PKC family, with 2 tandem DG-binding C1 domains (orange), and a Ca 2+ -binding C2 domain (yellow). Catalysis is performed by a kinase domain (blue) and regulated by an AGC C-tail and an N-terminal pseudosubstrate (red), which sits in the active site in the absence of agonist. Phosphorylation occurs at the activation loop (pink), turn motif (orange) and hydrophobic motif (green). F) COS7 cells were transfected for 48 h with HA-empty, or HA-PKCα constructs indicated, before lysis and probing for processing phosphosites by western blot. G) Quantification of HA-PKCα upper band intensity, relative to total HA-PKCα. Bars represent mean +/- SEM from n=3 experiments (**** p < 0.0001, 1-way ANOVA and Tukey multiple comparisons test).

    Article Snippet: Purified commercial PKCα (SignalChem P61-18G-10) was used as a positive control.

    Techniques: In Vitro, Kinase Assay, Isolation, Immunoprecipitation, Peptide Microarray, Incubation, Purification, Autoradiography, Two Tailed Test, MANN-WHITNEY, Binding Assay, Phospho-proteomics, Activation Assay, Transfection, Construct, Lysis, Western Blot