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phosphorylated form  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc phosphorylated form
    Phosphorylated Form, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phosphorylated+form/pm41554462-96-39-46
    Average 86 stars, based on 1 article reviews
    phosphorylated form - by Bioz Stars, 2026-10
    86/100 stars

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    Related Articles

    Western Blot:

    Article Title: Pharmacological targeting of RIG-I can selectively activate the integrated stress response
    Article Snippet: .. Reactions were quenched with 2x Laemmili buffer and separated by SDS-PAGE, and immunoblotting analysis was performed using an antibody specific to the phosphorylated form (Ser 51 ) of eIF2α (Cell Signaling Technology). .. HEK293T cells stably overexpressing FLAG-tagged RIG-I were grown to 50 to 75% confluency and then treated either with DMSO, 5′ppp-dsRNA/LyoVec (1 μg/ml; InvivoGen), or 10 μM compound for 16 hours.

    other:

    Article Title: Methods of enhancing cell survival of stem cells
    Article Snippet: AG825 (Erb2 inhibitor), AG1478 (EGFR inhibitor), PPP (IGFR1 inhibitor) were purchased from Calbiochem.

    Staining:

    Article Title: Low phylloquinone intake deteriorates endothelial function in normolipidemic and dyslipidaemic mice.
    Article Snippet: The aorta tissue slides were deparaffinized, treated with a citrate buffer-based heat-induced antigen retrieval, and incubated with a blocking buffer solution containing 2% dry milk (Gostyn, Poland) and 5% of normal goat serum (Jackson ImmunoResearch, Cambridgeshire, UK) according to a standard protocol. .. The aorta cross-sections were immunohistochemically stained using following primary antibodies: gammaglutamyl carboxylase (GGCX, 16209-1-AP; Proteintech, Manchester, UK), UbiA prenyltransferase domain-containing protein 1 (UBIAD1, ab191691; Abcam), endothelial nitric oxide synthase (NOS-3, 610296; BD Biosciences) and its phosphorylated form (p-NOS-3, 9571; Cell Signaling Technology), von Willebrand factor (vWF, ab174290; Abcam), intercellular adhesion molecule 1 (ICAM-1, 14- 0542-82; Thermo Fisher Scientific, Waltham, MA, USA), and vascular cell adhesion molecule 1 (VCAM-1, MA5-31965; Thermo Fisher Scientific). ..

    Centrifugation:

    Article Title: The THP-1 cell line as a model for the assessment of monoclonal antibodies aggregates' immunological effects.
    Article Snippet: This is a PDF of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability.. This version will undergo additional copyediting, typesetting and review before it is published in its final form.. As such, this version is no longer the Accepted Manuscript, but it is not yet the definitive Version of Record; we are providing this early version to give early visibility of the article.

    SDS Page:

    Article Title: The THP-1 cell line as a model for the assessment of monoclonal antibodies aggregates' immunological effects.
    Article Snippet: This is a PDF of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability.. This version will undergo additional copyediting, typesetting and review before it is published in its final form.. As such, this version is no longer the Accepted Manuscript, but it is not yet the definitive Version of Record; we are providing this early version to give early visibility of the article.

    Incubation:

    Article Title: The THP-1 cell line as a model for the assessment of monoclonal antibodies aggregates' immunological effects.
    Article Snippet: This is a PDF of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability.. This version will undergo additional copyediting, typesetting and review before it is published in its final form.. As such, this version is no longer the Accepted Manuscript, but it is not yet the definitive Version of Record; we are providing this early version to give early visibility of the article.

    Activity Assay:

    Article Title: (+)-a-Longipinene alleviates murine laser-induced choroidal neovascularization: Evidence from in vivo and in vitro experiments.
    Article Snippet: Choroidal neovascularization (CNV) is a progressive, degenerative pathological change.. CNV can lead to severe vision loss, even blindness. (+)-a-Longipinene (LON) is an essential oil isolated from Pinus koraiensis and Hypericum.. It plays anti-inflammatory and anti-angiogenic roles.

    Enzyme-linked Immunosorbent Assay:

    Article Title: (+)-a-Longipinene alleviates murine laser-induced choroidal neovascularization: Evidence from in vivo and in vitro experiments.
    Article Snippet: Choroidal neovascularization (CNV) is a progressive, degenerative pathological change.. CNV can lead to severe vision loss, even blindness. (+)-a-Longipinene (LON) is an essential oil isolated from Pinus koraiensis and Hypericum.. It plays anti-inflammatory and anti-angiogenic roles.

    Kinase Assay:

    Article Title: (+)-a-Longipinene alleviates murine laser-induced choroidal neovascularization: Evidence from in vivo and in vitro experiments.
    Article Snippet: Choroidal neovascularization (CNV) is a progressive, degenerative pathological change.. CNV can lead to severe vision loss, even blindness. (+)-a-Longipinene (LON) is an essential oil isolated from Pinus koraiensis and Hypericum.. It plays anti-inflammatory and anti-angiogenic roles.

    Cell-Signaling:

    Article Title: Secosteroid–2-Pyrazoline Hybrids: Design, Synthesis, Biological Evaluation and Development of Therapeutic Combinations Against ERα-Positive Breast Cancer Cells
    Article Snippet: .. Primary antibodies against androgen receptor (AR), estrogen receptor α (ERα), GREB1, S6K, and its phosphorylated form (p-S6K), Bcl-2, and its phosphorylated form (p-Bcl-2), and α-tubulin were employed (Cell Signaling Technology, Danvers, MA, USA). .. HRP-conjugated secondary goat anti-rabbit antibodies (Jackson ImmunoResearch, West Grove, PA, USA) were used for detection via enhanced chemiluminescence (ECL), following the method of Mruk and Cheng [ ], using an ImageQuant LAS4000 imaging system (GE HealthCare).



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    86
    Cell Signaling Technology Inc phosphorylated form
    Phosphorylated Form, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phosphorylated form ser51 of eif2α
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    ABclonal Biotechnology phosphorylated forms
    Phosphorylation of CtrBBX32 at Ser‐108 by CtrCBL1/CtrCIPK6 complex promotes protein degradation and relieves its transcriptional inhibition. a) Y2H assay showed that CtrCIPK6 interacted with CtrCBL1. The fusion vector pGBKT7‐CtrCIPK6 and pGADT7‐CtrCBL1 were cotransformed into yeast strain and then grown on SD/‐Trp/‐Leu and SD/‐Trp/‐Leu/‐His/‐Ade + X‐α‐gal medium. The positive control was pGBKT7‐P53 and pGADT7‐T, and pGBKT7 (BD)‐CtrCIPK6 and pGADT7 were used as negative controls. b) BiFC assay showed that CtrCIPK6 interacted with CtrCBL1 in the nucleus and cytoplasm, but did not interact with CtrCBL2. CtrCIPK6 and CtrCBL1/CtrCBL2 were fused to the C‐ or N‐terminus of YFP and coexpressed in N. benthamiana leaves, and the fluorescence of YFP was detected by confocal microscopy. Scale bars: 25 µm. c) LUC (luciferase) complementation imaging assay was used to detect the interaction between CtrCIPK6 and CtrCBL1 in N. benthamiana leaves with designated coexpression infiltration, using nLUC + cLUC‐CtrCIPK6, CtrCBL1‐nLUC + cLUC, and CtrCBL2‐nLUC + cLUC‐CtrCIPK6 as negative controls. d) Pull‐down assay confirmed the interaction between CtrCIPK6 and CtrCBL1 in vitro. The recombinant GST‐CtrCIPK6 or GST was immobilized on glutathione agarose and then incubated with His‐CtrCBL1. e) In vitro phosphorylation analysis of GST‐CtrBBX32 or GST‐CtrBBX32 S108A (a mutation from serine to alanine at 108 site) by the CtrCBL1/CtrCIPK6 complex. GST‐CtrCIPK6 was incubated with GST‐CtrBBX32 or GST‐CtrBBX32 S108A in the kinase buffer without or with λ‐PPase, in the presence or absence of His‐CtrCBL1, at 30 °C for 60 min. <t>Phosphorylated</t> GST‐CtrBBX32 and GST‐CtrBBX32 S108A were detected by anti‐pSer/pThr antibody. GST‐CtrCIPK6, GST‐CtrBBX32, and GST‐CtrBBX32 S108A were detected by anti‐GST antibody, and His‐CtrCBL1 was detected by anti‐His antibody. f–i) Luciferase (LUC) bioluminescence imaging (f) and (h) or LUC/REN ratios (g) and (i) of the N. benthamiana leaves infiltrated with 35S:CtrBBX32‐Flag or 35S:CtrBBX32 S108A ‐Flag and LUC reporter driven by the promoter of CtrSTP1 (p CtrSTP1 :LUC), along with CtrCIPK6‐MYC alone or CtrCIPK6‐MYC and CtrCBL1‐GFP together. Infiltration of p CtrSTP1 :LUC and empty vector (EV) was used as a control. Protein levels of CtrBBX32/CtrBBX32 S108A , CtrCIPK6, and CtrCBL1 were detected using the antibodies against Flag (anti‐Flag), MYC (anti‐MYC), and GFP (anti‐GFP), respectively. +, presence; −, absence. Error bars denote ± standard deviation (SD, n = 3). Two‐tailed Student ’ s t ‐test was conducted for analyzing the significant difference (* P < 0.05, *** P < 0.001; P > 0.05, ns, no significance).
    Phosphorylated Forms, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phosphorylated+form/DDDDK-Tag+Rabbit+mAb/pmc12697822-398-3-13
    Average 96 stars, based on 1 article reviews
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    96/100 stars
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    Image Search Results


    Phosphorylation of CtrBBX32 at Ser‐108 by CtrCBL1/CtrCIPK6 complex promotes protein degradation and relieves its transcriptional inhibition. a) Y2H assay showed that CtrCIPK6 interacted with CtrCBL1. The fusion vector pGBKT7‐CtrCIPK6 and pGADT7‐CtrCBL1 were cotransformed into yeast strain and then grown on SD/‐Trp/‐Leu and SD/‐Trp/‐Leu/‐His/‐Ade + X‐α‐gal medium. The positive control was pGBKT7‐P53 and pGADT7‐T, and pGBKT7 (BD)‐CtrCIPK6 and pGADT7 were used as negative controls. b) BiFC assay showed that CtrCIPK6 interacted with CtrCBL1 in the nucleus and cytoplasm, but did not interact with CtrCBL2. CtrCIPK6 and CtrCBL1/CtrCBL2 were fused to the C‐ or N‐terminus of YFP and coexpressed in N. benthamiana leaves, and the fluorescence of YFP was detected by confocal microscopy. Scale bars: 25 µm. c) LUC (luciferase) complementation imaging assay was used to detect the interaction between CtrCIPK6 and CtrCBL1 in N. benthamiana leaves with designated coexpression infiltration, using nLUC + cLUC‐CtrCIPK6, CtrCBL1‐nLUC + cLUC, and CtrCBL2‐nLUC + cLUC‐CtrCIPK6 as negative controls. d) Pull‐down assay confirmed the interaction between CtrCIPK6 and CtrCBL1 in vitro. The recombinant GST‐CtrCIPK6 or GST was immobilized on glutathione agarose and then incubated with His‐CtrCBL1. e) In vitro phosphorylation analysis of GST‐CtrBBX32 or GST‐CtrBBX32 S108A (a mutation from serine to alanine at 108 site) by the CtrCBL1/CtrCIPK6 complex. GST‐CtrCIPK6 was incubated with GST‐CtrBBX32 or GST‐CtrBBX32 S108A in the kinase buffer without or with λ‐PPase, in the presence or absence of His‐CtrCBL1, at 30 °C for 60 min. Phosphorylated GST‐CtrBBX32 and GST‐CtrBBX32 S108A were detected by anti‐pSer/pThr antibody. GST‐CtrCIPK6, GST‐CtrBBX32, and GST‐CtrBBX32 S108A were detected by anti‐GST antibody, and His‐CtrCBL1 was detected by anti‐His antibody. f–i) Luciferase (LUC) bioluminescence imaging (f) and (h) or LUC/REN ratios (g) and (i) of the N. benthamiana leaves infiltrated with 35S:CtrBBX32‐Flag or 35S:CtrBBX32 S108A ‐Flag and LUC reporter driven by the promoter of CtrSTP1 (p CtrSTP1 :LUC), along with CtrCIPK6‐MYC alone or CtrCIPK6‐MYC and CtrCBL1‐GFP together. Infiltration of p CtrSTP1 :LUC and empty vector (EV) was used as a control. Protein levels of CtrBBX32/CtrBBX32 S108A , CtrCIPK6, and CtrCBL1 were detected using the antibodies against Flag (anti‐Flag), MYC (anti‐MYC), and GFP (anti‐GFP), respectively. +, presence; −, absence. Error bars denote ± standard deviation (SD, n = 3). Two‐tailed Student ’ s t ‐test was conducted for analyzing the significant difference (* P < 0.05, *** P < 0.001; P > 0.05, ns, no significance).

    Journal: Advanced Science

    Article Title: The CtrCBL1/CtrCIPK6 Complex of Citrus Phosphorylates CtrBBX32 to Regulate CtrSTP1‐Mediated Sugar Accumulation and Cold Tolerance

    doi: 10.1002/advs.202508372

    Figure Lengend Snippet: Phosphorylation of CtrBBX32 at Ser‐108 by CtrCBL1/CtrCIPK6 complex promotes protein degradation and relieves its transcriptional inhibition. a) Y2H assay showed that CtrCIPK6 interacted with CtrCBL1. The fusion vector pGBKT7‐CtrCIPK6 and pGADT7‐CtrCBL1 were cotransformed into yeast strain and then grown on SD/‐Trp/‐Leu and SD/‐Trp/‐Leu/‐His/‐Ade + X‐α‐gal medium. The positive control was pGBKT7‐P53 and pGADT7‐T, and pGBKT7 (BD)‐CtrCIPK6 and pGADT7 were used as negative controls. b) BiFC assay showed that CtrCIPK6 interacted with CtrCBL1 in the nucleus and cytoplasm, but did not interact with CtrCBL2. CtrCIPK6 and CtrCBL1/CtrCBL2 were fused to the C‐ or N‐terminus of YFP and coexpressed in N. benthamiana leaves, and the fluorescence of YFP was detected by confocal microscopy. Scale bars: 25 µm. c) LUC (luciferase) complementation imaging assay was used to detect the interaction between CtrCIPK6 and CtrCBL1 in N. benthamiana leaves with designated coexpression infiltration, using nLUC + cLUC‐CtrCIPK6, CtrCBL1‐nLUC + cLUC, and CtrCBL2‐nLUC + cLUC‐CtrCIPK6 as negative controls. d) Pull‐down assay confirmed the interaction between CtrCIPK6 and CtrCBL1 in vitro. The recombinant GST‐CtrCIPK6 or GST was immobilized on glutathione agarose and then incubated with His‐CtrCBL1. e) In vitro phosphorylation analysis of GST‐CtrBBX32 or GST‐CtrBBX32 S108A (a mutation from serine to alanine at 108 site) by the CtrCBL1/CtrCIPK6 complex. GST‐CtrCIPK6 was incubated with GST‐CtrBBX32 or GST‐CtrBBX32 S108A in the kinase buffer without or with λ‐PPase, in the presence or absence of His‐CtrCBL1, at 30 °C for 60 min. Phosphorylated GST‐CtrBBX32 and GST‐CtrBBX32 S108A were detected by anti‐pSer/pThr antibody. GST‐CtrCIPK6, GST‐CtrBBX32, and GST‐CtrBBX32 S108A were detected by anti‐GST antibody, and His‐CtrCBL1 was detected by anti‐His antibody. f–i) Luciferase (LUC) bioluminescence imaging (f) and (h) or LUC/REN ratios (g) and (i) of the N. benthamiana leaves infiltrated with 35S:CtrBBX32‐Flag or 35S:CtrBBX32 S108A ‐Flag and LUC reporter driven by the promoter of CtrSTP1 (p CtrSTP1 :LUC), along with CtrCIPK6‐MYC alone or CtrCIPK6‐MYC and CtrCBL1‐GFP together. Infiltration of p CtrSTP1 :LUC and empty vector (EV) was used as a control. Protein levels of CtrBBX32/CtrBBX32 S108A , CtrCIPK6, and CtrCBL1 were detected using the antibodies against Flag (anti‐Flag), MYC (anti‐MYC), and GFP (anti‐GFP), respectively. +, presence; −, absence. Error bars denote ± standard deviation (SD, n = 3). Two‐tailed Student ’ s t ‐test was conducted for analyzing the significant difference (* P < 0.05, *** P < 0.001; P > 0.05, ns, no significance).

    Article Snippet: CtrCIPK6‐Flag and its phosphorylated forms were probed using an anti‐Flag antibody (Cat. AE063; ABclonal, Wuhan, China).

    Techniques: Phospho-proteomics, Inhibition, Y2H Assay, Plasmid Preparation, Positive Control, Bimolecular Fluorescence Complementation Assay, Fluorescence, Confocal Microscopy, Luciferase, Imaging, Pull Down Assay, In Vitro, Recombinant, Incubation, Mutagenesis, Control, Standard Deviation, Two Tailed Test