Phospho threonine antibody

Manufactured by Cell Signaling Technology

Sourced in United States

Phospho-threonine antibodies are affinity-purified antibodies that specifically recognize proteins phosphorylated at threonine residues. These antibodies are used to detect and study the phosphorylation of cellular proteins, a key mechanism of signal transduction and regulation of cellular processes.

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Lab products found in correlation

Sigmafast bcip nbt, by LI COR (2 mentions) Signalfire elite ecl reagent, by LI COR (2 mentions) C digit chemiluminescent blot scanner, by LI COR (2 mentions) Monoclonal murine anti polyhistidine antibody, by Merck Group (2 mentions) Mouse anti rabbit igg antibody alkaline phosphatase, by Merck Group (2 mentions) Anti mouse igg whole molecule alkaline phosphatase antibody, by Merck Group (2 mentions) Anti rabbit igg hrp linked antibody, by Cell Signaling Technology (2 mentions) Trans blot turbo transfer system, by Bio-Rad (2 mentions) Anti gfp antibody, by Transgene (1 mentions)

Close spelling variants of this product

Phospho-Threonine/Tyrosine Antibody Anti-phospho-Threonine–Proline antibody Anti-phospho-threonine antibody Phospho-threonine

5 protocols using phospho threonine antibody

Immunoblotting of Mycobacterial Proteins

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Proteins were separated on 4–20% gradient SERVA gels and transferred onto a nitrocellulose membrane using a Trans‐Blot® Turbo™ Transfer System (Bio‐Rad). SIGMAFAST™ BCIP®/NBT or SignalFire™ Elite ECL Reagent were used to visualise proteins on C‐DiGit Chemiluminescent Blot Scanner (LI‐COR Biosciences). The following antibodies were used: custom polyclonal antibody raised against Lsr2 in rabbit (Gemini Biosciences); monoclonal murine anti‐polyhistidine antibody (Sigma‐Aldrich); phospho‐threonine antibody (Cell Signaling Technology); monoclonal anti‐MtbGroEL2 (Rv0440), clone IT‐70 (BEIResources); mouse anti‐rabbit IgG antibody:alkaline phosphatase (Sigma‐Aldrich; anti‐mouse IgG (whole molecule:alkaline phosphatase antibody produced in rabbit (Sigma‐Aldrich), and anti‐rabbit IgG, HRP‐linked antibody (Cell Signaling Technology).

Alqaseer K., Turapov O., Barthe P., Jagatia H., De Visch A., Roumestand C., Wegrzyn M., Bartek I.L., Voskuil M.I., O'Hare H.M., Ajuh P., Bottrill A.R., Witney A.A., Cohen‐Gonsaud M., Waddell S.J, & Mukamolova G.V. (2019). Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112. Molecular Microbiology, 112(6), 1847-1862.

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Thylakoid Isolation and Immunoblot Analysis

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Thylakoid isolation was performed as reported^{47 (link)} from 4-week-old plants. For immunoblot analyses, thylakoid proteins, corresponding to 3 μg of chlorophyll, were prepared as described^{48 (link)} and fractionated by SDS–PAGE (12% w/v acrylamide^{49 (link)}). Proteins were then transferred onto polyvinylidene difluoride membranes^{50 (link)}, and replicate filters were immunodecorated using specific antibodies. The PGR5-specific antibody was obtained from Toshiharu Shikanai, Phospho-Threonine Antibody from Cell Signaling Technology, PsbS from Agrisera whereas D1^{51 (link)}, PGRL1A^{27 (link)}, STN7 and STN8^{52 (link)} antibodies were produced in our laboratory.

Barbato R., Tadini L., Cannata R., Peracchio C., Jeran N., Alboresi A., Morosinotto T., Bajwa A.A., Paakkarinen V., Suorsa M., Aro E.M, & Pesaresi P. (2020). Higher order photoprotection mutants reveal the importance of ΔpH-dependent photosynthesis-control in preventing light induced damage to both photosystem II and photosystem I. Scientific Reports, 10, 6770.

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Western Blot Analysis of Lsr2 Protein

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Proteins were separated on 4–20% gradient SERVA gels and transferred onto a nitrocellulose membrane using a Trans-Blot® Turbo™ Transfer System (Bio-Rad). SIGMAFAST™ BCIP®/NBT or SignalFire™ Elite ECL Reagent were used to visualise proteins on C-DiGit Chemiluminescent Blot Scanner (LI-COR Biosciences). The following antibodies were used: custom polyclonal antibody raised against Lsr2 in rabbit (Gemini Biosciences); monoclonal murine anti-polyhistidine antibody (Sigma-Aldrich); phospho-threonine antibody (Cell Signaling Technology); monoclonal anti-MtbGroEL2 (Rv0440), clone IT-70 (BEIResources); mouse anti-rabbit IgG antibody:alkaline phosphatase (Sigma-Aldrich; anti-mouse IgG (whole molecule:alkaline phosphatase antibody produced in rabbit (Sigma-Aldrich), and anti-rabbit IgG, HRP-linked antibody (Cell Signaling Technology).

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Protein Gel Blot Analysis of Photosynthetic Complexes

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Protein gel blot assay was performed according to Towbin et al.^{46 (link)}. Accordingly, 5 µg of thylakoid membrane protein was denaturized by boiling with SDS sample buffer for 5 min and separated by SDS-PAGE using 15% (w/v) acrylamide gel. PsbA (D1 protein), Lhcb1, Lhcb2, Lhcb4 (CP29 protein), Lhca1, Lhca2, Cytb6f, and ATPase were detected using corresponding antibodies provided by Agrisera, Sweden. PasA/B protein was detected by using an antibody that was used in Nath et al.^{12 (link)}. Phosphorylation of PSII proteins and LHCII proteins were detected using phosphothreonine antibody (Cell Signaling, USA). For separation of phosphorylated and fragmented CP29, Phospho-tag (NARD Institute, ltd. Japan) was added into 15% acrylamide gel according to the manufacturer’s instruction.

Poudyal R.S., Rodionova M.V., Kim H., Lee S., Do E., Allakhverdiev S.I., Nam H.G., Hwang D, & Kim Y. (2020). Combinatory actions of CP29 phosphorylation by STN7 and stability regulate leaf age-dependent disassembly of photosynthetic complexes. Scientific Reports, 10, 10267.

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In vivo NRAMP1 kinase assay

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The in vitro kinase assay was conducted according to a previously published method (37 (link)). For the in vivo kinase assay, constructs of NRAMP1-GFP, NRAMP1^T498A-GFP were transformed into WT or cpk21/23 mediated by Agrobacterium tumefaciens. The GFP signals were detected with anti-GFP antibody (TransGen Biotech), and the phosphorylation signals were analyzed by Western blotting using a phospho-threonine antibody (Cell Signaling Technology).

Fu D., Zhang Z., Wallrad L., Wang Z., Höller S., Ju C., Schmitz-Thom I., Huang P., Wang L., Peiter E., Kudla J, & Wang C. (2022). Ca2+-dependent phosphorylation of NRAMP1 by CPK21 and CPK23 facilitates manganese uptake and homeostasis in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 119(40), e2204574119.

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