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Pt183 y185 jnk

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PT183/Y185-JNK is a primary antibody that recognizes the phosphorylated forms of c-Jun N-terminal kinase (JNK) at Thr183 and Tyr185 residues. This antibody can be used to detect the activation of the JNK signaling pathway.

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Lab products found in correlation

Pt202 y204 erk, by Cell Signaling Technology (3 mentions) Ps32 36 iκbα, by Cell Signaling Technology (2 mentions) Ps176 180 ikkα β, by Cell Signaling Technology (2 mentions) Py416 c src, by Cell Signaling Technology (2 mentions) Pt180 y182 p38, by Promega (2 mentions) Mouse trip6, by BD (2 mentions) Traf6, by Santa Cruz Biotechnology (2 mentions) C src, by Santa Cruz Biotechnology (2 mentions) Histone h3, by Cell Signaling Technology (2 mentions) Flag tag (flag), by Merck Group (2 mentions) Gapdh, by Santa Cruz Biotechnology (2 mentions) Caspase 3, by Cell Signaling Technology (2 mentions) Ha h9658, by Merck Group (2 mentions) Ire1α, by Santa Cruz Biotechnology (2 mentions) Sel1l ab78298, by Abcam (2 mentions) Hrd1 nb100 2526, by Novus Biologicals (2 mentions) Hsp90, by Santa Cruz Biotechnology (2 mentions) Ire1β, by Santa Cruz Biotechnology (2 mentions) α tubulin, by Santa Cruz Biotechnology (2 mentions) P erk, by Cell Signaling Technology (2 mentions)

6 protocols using pt183 y185 jnk

1

Immunoblotting, Co-IP, and Recombinant Protein Purification

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Experimental procedures of immunoblotting, co-immunoprecipitation, and purification of recombinant glutathione-S-transferase (GST)-tagged or non-tagged proteins were performed as described previously [19 (link), 34 (link)]. Immunoblotting was performed using antibody specific to human TRIP6, A20 (Bethyl Laboratories), pT183/Y185-JNK, pT202/Y204-ERK, pS32/36-IκBα, pS176/180-IKKα/β, pY416-c-Src, CYLD, IκBα, IKKβ, Histone H3 (Cell Signaling, Danvers, MA, USA), pT180/Y182-p38 (Promega, Madison, WI, USA), ERK, JNK, mouse TRIP6 (BD Biosciences, San Jose, CA, USA), HA (Cayman, Ann Arbor, MI, USA), FLAG (Sigma-Aldrich), GFP, TRAF6, p38, c-Src, GAPDH, GST, ubiquitin, or phosphotyrosine (Santa Cruz Biotechnology, Dallas, TX, USA).
Lin F.T., Lin V.Y., Lin V.T, & Lin W.C. (2016). TRIP6 antagonizes the recruitment of A20 and CYLD to TRAF6 to promote the LPA2 receptor-mediated TRAF6 activation. Cell Discovery, 2, 15048-.
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2

Ras/Raf/MAPK Signaling Pathway Antibodies

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Antibodies to B-Raf (H-145), C-Raf (C-12), β-Tubulin (H-235), and Sos1 (C-23) were from Santa Cruz Biotechnology; antibodies to pS217/221-MEK, pT202/Y204-ERK, pS473-AKT, pS/TP, pS257/T261-MKK4, pT183/Y185-JNK, pT180/Y182-p38, and pS621-C-Raf sites were from Cell Signaling Technologies; antibodies to pERK were from Sigma; antibodies to Ras were from BD Biosciences. The pS642P-C-Raf antibody has been previously described (Dougherty et al., 2005 (link)). Rigosertib, Paxlitaxel/Taxol, SB-590885 (RAFi), Vincristine, Vinblastine, SP-600125 (JNKi) and JNK-IN-8 were from SelleckChem; KG5 was from Tocris Bioscience; N-acetylcystine (NAC) was from Sigma-Aldrich. GST-RafRBD was from Millipore; GST-H-RasG12V was from Cell Sciences.
Ritt D.A., Blanco M.A., Bindu L., Durrant D.E., Zhou M., Specht S.I., Stephen A.G., Holderfield M, & Morrison D.K. (2016). Inhibition of Ras/Raf/MEK/ERK Pathway Signaling by a Stress-induced Phospho-regulatory Circuit. Molecular cell, 64(5), 875-887.
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3

Inflammatory Signaling Pathway Assays

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Insulin was obtained from Life Technologies (Saint Aubin, France), LPS ultrapure from InvivoGen (San Diego, USA) and IL-1β from PeproTech France (Neuilly sur seine, France). Antibodies were obtained from the following companies: REDD1 from Proteintech (Chicago, IL); pT180/Y182 p38 MAPK, p38 MAPK, JNK, pT183/Y185 JNK, pS536p65 NF-κB, IL1β, pT308PKB, PKB, ERK from Cell Signaling Technology (Beverly, MA); NFκB, HSP90 from Santa Cruz Biotechnology (Heidelberg, Germany); tubulin from Sigma-Aldrich; NLRP3, caspase-1 (p20) from Adipogen (San Diego, USA). The primer sets for real time PCR were purchased from Eurogentec (Seraing, Belgium) and Qiagen (Courtaboeuf, France). Culture media were obtained from Life Technologies (Saint Aubin, France). Rapamycin was obtained from Calbiochem (Nottingham, UK).
Pastor F., Dumas K., Barthélémy M.A., Regazzetti C., Druelle N., Peraldi P., Cormont M., Tanti J.F, & Giorgetti-Peraldi S. (2017). Implication of REDD1 in the activation of inflammatory pathways. Scientific Reports, 7, 7023.
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4

Quantitative Western Blot Analysis of ER Stress Signaling

Cited 2 times
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Preparation of cell and tissue lysates and Western blot were performed as previously described27 (link). IRE1α phosphorylation was measured by a Phos-tag-based Western blot method27 (link)–29 (link). For non-reducing SDS-PAGE, lysates were prepared in 5 X non-denaturing sample buffer (250 mM Tris HCl pH 6.8, 1% SDS, 50% glycerol and 0.05% bromophenyl blue) without boiling prior to be separated on a SDS-PAGE gel. Antibodies used in this study were: HSP90 (sc-7947, 1:6,000), GFP (sc-8334, 1:2000), BiP (sc-1051, 1:1,000), IRE1β (sc-20575, 1:1000), JNK1 (sc-571, 1:1000), α-Tubulin (sc-5286, 1:2000) from Santa Cruz; IRE1α (#3294, 1:2000), PERK (#3192, 1:2,000), Caspase-3 (#9665, 1:1000), p-T183/Y185-JNK (#9255, 1:2000), from Cell Signaling; Sel1L (ab78298, 1:2,000), OS9 (ab109510, 1:10,000) from Abcam; Hrd1 (NB100-2526, 1:8,000) from Novus Biologicals; Calnexin (SPA-860, 1:8,000) and PDIA1 (SPA-890, 1:8,000) from Enzo Life Sciences; Flag-HRP (A-8592, 1:8,000), HA (H9658, 1:5,000) from Sigma. Antibodies for Bag6 (rabbit, 1:10,000) and H2A (rabbit, 1:10,000) were kind gifts from Dr. Yihong Ye (NIDDK). Band density was quantitated using the Image Lab software on the ChemiDOC XRS+ system (Bio-Rad). Protein levels were normalized to HSP90 or α-Tubulin and are presented as mean ± s.e.m. unless otherwise specified.
Sun S., Shi G., Sha H., Ji Y., Han X., Shu X., Ma H., Inoue T., Gao B., Kim H., Bu P., Guber R.D., Shen X., Lee A.H., Iwawaki T., Paton A.W., Paton J.C., Fang D., Tsai B., Yates JR I.I.I., Wu H., Kersten S., Long Q., Duhamel G.E., Simpson K.W, & Qi L. (2015). IRE1α is an endogenous substrate of endoplasmic reticulum-associated degradation. Nature cell biology, 17(12), 1546-1555.
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5

Quantitative Western Blot Analysis of ER Stress Signaling

Cited 2 times
Check if the same lab product or an alternative is used in the 5 most similar protocols
Preparation of cell and tissue lysates and Western blot were performed as previously described27 (link). IRE1α phosphorylation was measured by a Phos-tag-based Western blot method27 (link)–29 (link). For non-reducing SDS-PAGE, lysates were prepared in 5 X non-denaturing sample buffer (250 mM Tris HCl pH 6.8, 1% SDS, 50% glycerol and 0.05% bromophenyl blue) without boiling prior to be separated on a SDS-PAGE gel. Antibodies used in this study were: HSP90 (sc-7947, 1:6,000), GFP (sc-8334, 1:2000), BiP (sc-1051, 1:1,000), IRE1β (sc-20575, 1:1000), JNK1 (sc-571, 1:1000), α-Tubulin (sc-5286, 1:2000) from Santa Cruz; IRE1α (#3294, 1:2000), PERK (#3192, 1:2,000), Caspase-3 (#9665, 1:1000), p-T183/Y185-JNK (#9255, 1:2000), from Cell Signaling; Sel1L (ab78298, 1:2,000), OS9 (ab109510, 1:10,000) from Abcam; Hrd1 (NB100-2526, 1:8,000) from Novus Biologicals; Calnexin (SPA-860, 1:8,000) and PDIA1 (SPA-890, 1:8,000) from Enzo Life Sciences; Flag-HRP (A-8592, 1:8,000), HA (H9658, 1:5,000) from Sigma. Antibodies for Bag6 (rabbit, 1:10,000) and H2A (rabbit, 1:10,000) were kind gifts from Dr. Yihong Ye (NIDDK). Band density was quantitated using the Image Lab software on the ChemiDOC XRS+ system (Bio-Rad). Protein levels were normalized to HSP90 or α-Tubulin and are presented as mean ± s.e.m. unless otherwise specified.
Sun S., Shi G., Sha H., Ji Y., Han X., Shu X., Ma H., Inoue T., Gao B., Kim H., Bu P., Guber R.D., Shen X., Lee A.H., Iwawaki T., Paton A.W., Paton J.C., Fang D., Tsai B., Yates JR I.I.I., Wu H., Kersten S., Long Q., Duhamel G.E., Simpson K.W, & Qi L. (2015). IRE1α is an endogenous substrate of endoplasmic reticulum-associated degradation. Nature cell biology, 17(12), 1546-1555.
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6

Immunoblotting and Protein Purification Protocols

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Experimental procedures of immunoblotting, co-immunoprecipitation, and purification of recombinant glutathione-S-transferase (GST)-tagged or non-tagged proteins were performed as described previously [19 (link), 34 (link)]. Immunoblotting was performed using antibody specific to human TRIP6, A20 (Bethyl Laboratories), pT183/Y185-JNK, pT202/Y204-ERK, pS32/36-IκBα, pS176/180-IKKα/β, pY416-c-Src, CYLD, IκBα, IKKβ, Histone H3 (Cell Signaling, Danvers, MA, USA), pT180/Y182-p38 (Promega, Madison, WI, USA), ERK, JNK, mouse TRIP6 (BD Biosciences, San Jose, CA, USA), HA (Cayman, Ann Arbor, MI, USA), FLAG (Sigma-Aldrich), GFP, TRAF6, p38, c-Src, GAPDH, GST, ubiquitin, or phospho-tyrosine (Santa Cruz Biotechnology, Dallas, TX, USA).
Lin F.T., Lin V.Y., Lin V.T, & Lin W.C. (2016). TRIP6 antagonizes the recruitment of A20 and CYLD to TRAF6 to promote the LPA2 receptor-mediated TRAF6 activation. Cell Discovery, 2, 15048-.
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