h3t3ph Search Results


90
GenScript corporation h3t3ph
Spontaneous metal incorporation in purified PP1‐EDTA. (A) In vitro phosphatase activity assay of PP1‐EDTA at pH 7 following pre‐incubation of the phosphatase at pH 4 or pH 7 with the indicated metal ions. DiFMUP was used a substrate and released phosphate was detected colorimetrically. (B) Same as in panel (A) but with <t>H3T3ph</t> as substrate. (C) Same as in panel (A) but with 32 P labeled glycogen phosphorylase a as substrate. Released radioactive phosphate was measured after precipitation of glycogen phosphorylase with tri‐chloro‐acetic acid. The results are shown as means ± SEM. The activity was normalized against the Mn 2+ treated condition at pH 4. A 2‐way ANOVA was performed, only significant differences are marked on the graphs (*: P < 0.05; **: P < 0.01; ****: P < 0.0001). The results are shown as means ± SEM. AU, arbitrary units.
H3t3ph, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h3t3ph/h3t3ph/pmc11626998-39-107-108
Average 90 stars, based on 1 article reviews
h3t3ph - by Bioz Stars, 2026-09
90/100 stars
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90
GL Biochem anti-h3t3ph antibody
Spontaneous metal incorporation in purified PP1‐EDTA. (A) In vitro phosphatase activity assay of PP1‐EDTA at pH 7 following pre‐incubation of the phosphatase at pH 4 or pH 7 with the indicated metal ions. DiFMUP was used a substrate and released phosphate was detected colorimetrically. (B) Same as in panel (A) but with <t>H3T3ph</t> as substrate. (C) Same as in panel (A) but with 32 P labeled glycogen phosphorylase a as substrate. Released radioactive phosphate was measured after precipitation of glycogen phosphorylase with tri‐chloro‐acetic acid. The results are shown as means ± SEM. The activity was normalized against the Mn 2+ treated condition at pH 4. A 2‐way ANOVA was performed, only significant differences are marked on the graphs (*: P < 0.05; **: P < 0.01; ****: P < 0.0001). The results are shown as means ± SEM. AU, arbitrary units.
Anti H3t3ph Antibody, supplied by GL Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/h3t3ph/anti+h3t3ph+antibody/pm29032586-187-2-7
Average 90 stars, based on 1 article reviews
anti-h3t3ph antibody - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier

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HISTONE H3T3PH MONOCLONAL ANTIBODY
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Image Search Results


Spontaneous metal incorporation in purified PP1‐EDTA. (A) In vitro phosphatase activity assay of PP1‐EDTA at pH 7 following pre‐incubation of the phosphatase at pH 4 or pH 7 with the indicated metal ions. DiFMUP was used a substrate and released phosphate was detected colorimetrically. (B) Same as in panel (A) but with H3T3ph as substrate. (C) Same as in panel (A) but with 32 P labeled glycogen phosphorylase a as substrate. Released radioactive phosphate was measured after precipitation of glycogen phosphorylase with tri‐chloro‐acetic acid. The results are shown as means ± SEM. The activity was normalized against the Mn 2+ treated condition at pH 4. A 2‐way ANOVA was performed, only significant differences are marked on the graphs (*: P < 0.05; **: P < 0.01; ****: P < 0.0001). The results are shown as means ± SEM. AU, arbitrary units.

Journal: Febs Letters

Article Title: Spontaneous and chaperone‐assisted metal loading in the active site of protein phosphatase‐1

doi: 10.1002/1873-3468.15012

Figure Lengend Snippet: Spontaneous metal incorporation in purified PP1‐EDTA. (A) In vitro phosphatase activity assay of PP1‐EDTA at pH 7 following pre‐incubation of the phosphatase at pH 4 or pH 7 with the indicated metal ions. DiFMUP was used a substrate and released phosphate was detected colorimetrically. (B) Same as in panel (A) but with H3T3ph as substrate. (C) Same as in panel (A) but with 32 P labeled glycogen phosphorylase a as substrate. Released radioactive phosphate was measured after precipitation of glycogen phosphorylase with tri‐chloro‐acetic acid. The results are shown as means ± SEM. The activity was normalized against the Mn 2+ treated condition at pH 4. A 2‐way ANOVA was performed, only significant differences are marked on the graphs (*: P < 0.05; **: P < 0.01; ****: P < 0.0001). The results are shown as means ± SEM. AU, arbitrary units.

Article Snippet: The source of the used chemicals and materials, in alphabetical order (company, cat no.), is as follows: acetic acid (Chem‐Lab, Zedelgem, Belgium; CL00.0116.1000), AmershamTM Hybond 0.45 μm PVDF membrane (Cytiva, Marlborough, MA, USA; 10600023), ampicillin (Roth, Karlsruhe, Germany; K029.1), benzamidine (Across Organics, Gent, Belgium; 105241000), BIOMOL ® Green (Enzo, Long Island, NY, USA; BML‐AK111‐0250), BL21‐Gold(DE3) competent cells (Agilent, Santa Clara, CA, USA; 230132), BSA (Sigma‐Aldrich, St. Louis, MO, USA; 03116956001), chitin beads (New England BioLabs, Ipswich, MA, USA; S6651L), DiFMUP (AAT Bioquest, Pleasanton, CA, USA; 11627), dithiothreitol (Fisher, Plano, TX, USA; BP172‐25), EDTA (Chem‐Lab, CL00.0503.0500), FeCl 2 (ThermoFisher, 31141), glycerol (ThermoFisher, 158920010), HisPurTM Ni‐NTA Agarose (ThermoFisher, 88222), H3T3ph (Genscript, Piscataway, NJ, USA; custom‐made), Imidazole (Alfa Aesar, Haverhill, MA, USA; 47274), IPTG (BioWORLD, Dublin, OH, USA; 21530057‐5), kanamycin (AppliChem, Darmstadt, Germany; A1493.0025), leupeptin (Apollo Scientific, Bredbury, UK; APOSBIMI1322), MES (Sigma‐Aldrich, M‐81250), Microplate‐384 well‐PS‐F bottom‐Clear (Greiner Bio‐one, Kremsmünster, Austria; 781901), Microplate‐384 well‐PS‐F Bottom‐White (Greiner Bio‐one, 781904), MnCl 2 (Sigma‐Aldrich, M3634), MOPS (Invitrogen, Waltham, MA, USA; NP0001‐02), PMSF (Roth, 6367.2), NuPAGE 4–12% Bis‐Tris gels (Invitrogen, NP0322BOX), Pan‐PP1 (home‐made, NA), Rabbit Anti‐Mouse Immunoglobulins/HRP (Dako, Santa Clara, CA, USA; P0260), R11 (Eurogentec, Seraing, Belgium; custom‐made), R2 (R&D Systems, Minneapolis, MN, USA; AF4719), SDS22 (Santa Cruz, Dallas, TX, USA; sc‐398864), Sodium acetate (Sigma‐Aldrich, S8750‐5006), Swine Anti‐Rabbit Immunoglobulins/HRP (Dako, P0217), TCEP (Sigma‐Aldrich, C4706), Tween20 (AppliChem, A4974.0500), Tris (Thermo Scientific, 167620010), Triton X‐100 (Fisher Chemical, T/3751/08), Trypsin (Thermo Fisher Scientific, 90058), Urea (Sigma‐Aldrich, 51456), Western Lightning Plus‐ECL, Enhanced Chemiluminescence (PerkinElmer, Waltham, MA, USA; NEL105001EA), ZnSO 4 (Merck, Rahway, NJ, USA; 1.08883.0500).

Techniques: Purification, In Vitro, Phosphatase Assay, Incubation, Labeling, Activity Assay