Phospho-JNK1/2/3 (Thr183+Tyr185) Antibody - AF3318

	Price	Size
	$280	100ul
	$350	200ul

Product Information

Alternative Names:Expand▼

C Jun kinase 2; c Jun N terminal kinase 1; c Jun N terminal kinase 2; c Jun N terminal kinase 3; c-Jun N-terminal kinase 1; JNK 46; JNK 55; JNK; JNK-46; JNK1; JNK1A2; JNK2; JNK21B1/2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; JNK3 alpha protein kinase; JNK3; JNK3A; Jun kinase; JUN N terminal kinase; MAP kinase 10; MAP kinase 8; MAP kinase 9; MAP kinase p49 3F12; MAPK 10; MAPK 8; MAPK 9; MAPK10; mapk8; MAPK9; Mitogen activated protein kinase 10; Mitogen activated protein kinase 8; Mitogen activated protein kinase 8 isoform JNK1 alpha1; Mitogen activated protein kinase 8 isoform JNK1 beta2; Mitogen activated protein kinase 9; Mitogen-activated protein kinase 8; MK08_HUMAN; p493F12; p54a; p54aSAPK; p54bSAPK; PRKM10; PRKM8; PRKM9; SAPK; SAPK(beta); SAPK1; SAPK1a; SAPK1b; SAPK1c; Stress activated protein kinase 1; Stress activated protein kinase 1a; Stress activated protein kinase 1b; Stress activated protein kinase 1c; Stress activated protein kinase beta; Stress activated protein kinase JNK1; Stress activated protein kinase JNK2; Stress activated protein kinase JNK3; Stress-activated protein kinase 1c; Stress-activated protein kinase JNK1; c Jun kinase 2; C Jun N terminal kinase 2; c-Jun N-terminal kinase 2; JNK 55; JNK-55; JNK2 alpha; JNK2; JNK2 beta; JNK2A; JNK2alpha; JNK2B; JNK2BETA; Jun kinase; MAP kinase 9; MAPK 9; Mapk9; Mitogen activated protein kinase 9; Mitogen-activated protein kinase 9; MK09_HUMAN; P54a; p54aSAPK; PRKM9; Protein kinase, mitogen-activated, 9; SAPK alpha; SAPK; SAPK1a; Stress activated protein kinase 1a; Stress-activated protein kinase JNK2; c Jun kinase 3; c-Jun N-terminal kinase 3; cJun N terminal kinase 3; FLJ12099; FLJ33785; JNK3 alpha protein kinase; JNK3; JNK3A; MAP kinase 10; MAP kinase; MAP kinase p49 3F12; MAPK 10; Mapk10; MGC50974; mitogen activated protein kinase 10; Mitogen-activated protein kinase 10; MK10_HUMAN; p493F12; p54bSAPK; PRKM10; protein kinase mitogen activated 10; SAPK1b; Stress activated protein kinase 1b; stress activated protein kinase beta; Stress activated protein kinase JNK3; Stress-activated protein kinase JNK3;

Applications:

WB 1:500-1:2000, IHC 1:100-1:500, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.

Reactivity:

Human, Mouse, Rat

Predicted Reactivity:

Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)

Source:

Rabbit

Clonality:

Polyclonal

Purification:

The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.

Specificity:

Phospho-JNK1/2/3 (Thr183+Tyr185) Antibody detects endogenous levels of JNK1/2/3 only when phosphorylated at Threonine 183+Tyrosine 185.

RRID:

AB_2834737
Please cite this product as: Affinity Biosciences Cat# AF3318, RRID:AB_2834737.

Format:

Liquid

Concentration:

1mg/ml

Storage Condition and Buffer:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.

Immunogen Information

Immunogen:

A synthesized peptide derived from human JNK1/2/3 around the phosphorylation site of Thr183+Tyr185.

Uniprot:

>>Visit The Human Protein Atlas

Gene ID:

Gene Name:

MAPK10,MAPK8,MAPK9

Molecular Weight:

Observed Mol.Wt.: 46,54kD.
Predicted Mol.Wt.: 48kDa,48kDa,53kDa(Calculated)..

Subcellular Location:

Cytoplasm. Nucleus.

Tissue Specificity:

P53779 MK10_HUMAN:
Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

Description:

JNK3 a protein kinase of the MAPK family that is potently activated by a variety of environmental stress and pro-inflammatory cytokines. Brain-selective JNK isoform.

Sequence:

P45983 MK08_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR

P45984 MK09_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR

P53779 MK10_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR

Research Background

Function:

Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (By similarity). Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1 (By similarity). In neurons, phosphorylates SYT4 which captures neuronal dense core vesicles at synapses (By similarity).

JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.

Post-translational Modifications:

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Phosphorylated by TAOK2. May be phosphorylated at Thr-183 and Tyr-185 by MAP3K1/MEKK1. Phosphorylated form is more concentrated at synapses than none-phosphorylated (By similarity).

Subcellular Location:

Cytoplasm. Nucleus. Cell junction>Synapse.
Note: In the cortical neurons, predominantly cytoplasmic and associated with the Golgi apparatus and endosomal fraction. Increased neuronal activity increases phosphorylated form at synapses (By similarity). Colocalizes with POU5F1 in the nucleus.

Subunit Structure:

Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway. Interacts with TP53 and WWOX. Interacts with JAMP (By similarity). Forms a complex with MAPK8IP1 and ARHGEF28 (By similarity). Interacts with HSF1 (via D domain and preferentially with hyperphosphorylated form); this interaction occurs under both normal growth conditions and immediately upon heat shock. Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells (By similarity). Interacts with NFATC4. Interacts with MECOM; regulates JNK signaling. Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates. Interacts with GRIPAP1. Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-355'. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8IP1/JIP1. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2 (By similarity).

Similarity:

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Function:

Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (By similarity).

MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.

Post-translational Modifications:

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro.

Subcellular Location:

Cytoplasm. Nucleus.
Note: Colocalizes with POU5F1 in the nucleus.

Subunit Structure:

Interacts with MECOM (By similarity). Interacts with DCLK2 (By similarity). Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway (By similarity). Interacts with NFATC4. Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Interacts with BCL10. Interacts with CTNNB1 and GSK3B. Interacts with MAPKBP1. Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-355'. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (By similarity).

Similarity:

Function:

Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock. Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1.

Post-translational Modifications:

Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, which activates the enzyme. MAP2K7 shows a strong preference for Thr-221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly autophosphorylated on threonine and tyrosine residues in vitro.

Palmitoylation regulates subcellular location and axonal development.

Subcellular Location:

Cytoplasm. Membrane>Lipid-anchor. Nucleus. Mitochondrion.
Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 (By similarity).

Tissue Specificity:

Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

Subunit Structure:

Interacts with MAPKBP1 (By similarity). Interacts with MAPK8IP1/JIP-1 and MAPK8IP3/JIP-3/JSAP1 (By similarity). Interacts with SPAG9/MAPK8IP4/JIP4. Interacts with HDAC9. Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5. Interacts with SARM1 (By similarity). Interacts with JUND; interaction is inhibited in the presence of MEN1.

Similarity:

Research Fields

Research Fields:

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Tight junction.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis.(View pathway)
· Cellular Processes > Transport and catabolism > Autophagy - animal.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis - multiple species.(View pathway)
· Cellular Processes > Cell growth and death > Necroptosis.(View pathway)
· Environmental Information Processing > Signal transduction > TNF signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > MAPK signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > ErbB signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Wnt signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > FoxO signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Ras signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > cAMP signaling pathway.(View pathway)
· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.(View pathway)
· Human Diseases > Cancers: Specific types > Pancreatic cancer.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Colorectal cancer.(View pathway)
· Human Diseases > Endocrine and metabolic diseases > Type II diabetes mellitus.
· Human Diseases > Infectious diseases: Bacterial > Pertussis.
· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.
· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.
· Human Diseases > Cancers: Overview > Choline metabolism in cancer.(View pathway)
· Human Diseases > Infectious diseases: Bacterial > Shigellosis.
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Infectious diseases: Viral > Hepatitis C.
· Human Diseases > Infectious diseases: Viral > Hepatitis B.
· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).
· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.
· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.
· Human Diseases > Infectious diseases: Viral > Influenza A.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).
· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.
· Human Diseases > Drug resistance: Antineoplastic > Endocrine resistance.
· Organismal Systems > Immune system > Th1 and Th2 cell differentiation.(View pathway)
· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > Toll-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > IL-17 signaling pathway.(View pathway)
· Organismal Systems > Immune system > Fc epsilon RI signaling pathway.(View pathway)
· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.
· Organismal Systems > Endocrine system > Relaxin signaling pathway.
· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.
· Organismal Systems > Endocrine system > Insulin signaling pathway.(View pathway)
· Organismal Systems > Immune system > Th17 cell differentiation.(View pathway)
· Organismal Systems > Endocrine system > Prolactin signaling pathway.(View pathway)
· Organismal Systems > Nervous system > Neurotrophin signaling pathway.(View pathway)
· Organismal Systems > Nervous system > Dopaminergic synapse.
· Organismal Systems > Development > Osteoclast differentiation.(View pathway)
· Organismal Systems > Sensory system > Inflammatory mediator regulation of TRP channels.(View pathway)
· Organismal Systems > Immune system > NOD-like receptor signaling pathway.(View pathway)
· Organismal Systems > Nervous system > Retrograde endocannabinoid signaling.(View pathway)

ELISA analysis of AF3318 showing specificity to Phospho-JNK1/2/3 (Thr183+Tyr185) Blocking Peptide peptide. Peptides concentration: 1ug/ml.
P-peptide: phospho-peptide; N-peptide: non-phospho-peptide.

Reference Citations:

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30). Wang R et al. PM2.5 upregulates rat mesenteric arteries 5-HT2A receptor via inflammatory-mediated mitogen-activated protein kinases signaling pathway. Environ Toxicol 2019 Jun 14 (PubMed: 31199065) [IF=3.118]

31). Tang Q et al. Ferroptosis is newly characterized form of neuronal cell death in response to arsenite exposure. Neurotoxicology 2018 Jul;67:27-36 (PubMed: 29678591) [IF=3.105]

32). Ji M et al. The p75 neurotrophin receptor might mediate sepsis-induced synaptic and cognitive impairments. Behav Brain Res 2018 Jul 16;347:339-349 (PubMed: 29604364)

33). Zhang BB et al. Neuroprotective Effects of Dammarane-Type Saponins from Panax notoginseng on Glutamate-Induced Cell Damage in PC12 Cells. Planta Med 2019 Feb 21 (PubMed: 30791058)

34). An S et al. Administration of CoCl2 Improves Functional Recovery in a Rat Model of Sciatic Nerve Transection Injury. Int J Med Sci 2018 Sep 7;15(13):1423-1432 (PubMed: 30443161)

35). An S et al. Administration of CoCl2 Improves Functional Recovery in a Rat Model of Sciatic Nerve Transection Injury. Int J Med Sci 2018 Sep 7;15(13):1423-1432 (PubMed: 30443161)

36). Geng H et al. Cigarette smoke extract-induced proliferation of normal human urothelial cells via the MAPK/AP-1 pathway. Oncol Lett 2017 Jan;13(1):469-475 (PubMed: 28123584)

Application: WB Species:human; Sample:SV-HUC-1 cells

Figure 4. (A) Fold change in cell viability of SV-HUC-1 cells treated with 0, 0.10 and 0.25% CSE for 7 days in combination with 5 µM U0126, 5 µM SB203580 or 2 µM SP600125. Data are representative of three independent experiments and are expressed as the mean ± standard deviation. * P

37). Zhao L et al. MAPK/AP-1 pathway regulates benzidine-induced cell proliferation through the control of cell cycle in human normal bladder epithelial cells. Oncol Lett 2018 Oct;16(4):4628-4634 (PubMed: 30197677)

38). Zhao L et al. MAPK/AP-1 pathway regulates benzidine-induced cell proliferation through the control of cell cycle in human normal bladder epithelial cells. Oncol Lett 2018 Oct;16(4):4628-4634 (PubMed: 30197677)

39). Jin X et al. 11-O-acetylcyathatriol inhibits MAPK/p38-mediated inflammation in LPS-activated RAW 264.7 macrophages and has a protective effect on ethanol-induced gastric injury. Mol Med Rep 2016 Jul;14(1):874-80 (PubMed: 27222252)

Application: WB Species:mouse; Sample:Not available

Figure 3. Effects of 11‑O‑acetylcyathatriol on the protein expression levels of iNOS and COX‑2. The RAW 264.7 cells were treated by 1 µg/ml of LPS with indicated concentrations of 11-O‑acetylcyathatriol (12.5, 25, 50 and 100 µM) for 24 h, and the expression levels of (A) iNOS and COX‑2 were detected using western blot analysis. (B) Effects of 11‑O-acetylcyathatriol on the phosphorylation of ERK1/2, JNK and p38 proteins. RAW 264.7 cells were treated with 1 µg/ml LPS with 11‑O‑acetylcyathatriol (12.5, 25, 50 and 100 µM) for 30 min, and the protein expression levels of p‑ERK1/2, p‑JNK and p‑p38 were detected using western blot analysis. (C) Effects of 11‑O-acetylcyathatriol on the protein degradation of IκB-α. RAW 264.7 cells were treated with 1 µg/ml of LPS with 11-O‑acetylcyathatriol (12.5, 25, 50 and 100 µM) for 10 min, and the protein expression of IκB-α was detected using western blot analysis. iNOS, inducible nitric oxide synthase; COX‑2, cyclooxygenase‑2; LPS, lipopolysaccharide; ERK, extracellular signal‑regulated kinase; JNK, c‑Jun N‑terminal kinase; IκB-α, inhibitor of nuclear factor-κB-α; p‑, phosphorylated.

40). Li H et al. Dysifragilone A inhibits LPS‑induced RAW264.7 macrophage activation by blocking the p38 MAPK signaling pathway. Mol Med Rep 2018 Jan;17(1):674-682 (PubMed: 29115475)

41). Zhang X et al. Neuroprotective Effect of Modified Xijiao Dihuang Decoction against Oxygen-Glucose Deprivation and Reoxygenation-Induced Injury in PC12 Cells: Involvement of TLR4-MyD88/NF-κB Signaling Pathway. Evid Based Complement Alternat Med 2017;2017:3848595 (PubMed: 29234386)

42). Jin X et al. Tiliroside, the major component of Agrimonia pilosa Ledeb ethanol extract, inhibits MAPK/JNK/p38-mediated inflammation in lipopolysaccharide-activated RAW 264.7 macrophages. Exp Ther Med 2016 Jul;12(1):499-505 (PubMed: 27347085)

Application: WB Species:mouse; Sample:Not available

Figure 7. Effect of tiliroside on the phosphorylation of mitogen‑activated protein kinase‑ERK/JNK/p38 proteins. (A) RAW 264.7 cells were treated with LPS 1 µg/ml with or without tiliroside (12.5, 25, 50, and 100 µM) for 45 min and the expression of p‑ERK1/2, p‑JNK and p‑p38 was assessed by western blot analysis. Detection of β‑actin was conducted to confirm the equal loading of proteins. Densitometric analysis of p‑ERK1/2 (B) p‑JNK (C) and p‑p38 (D) expression represent the mean±standard deviation of three separate experiments. Data were normalized with respect to β‑actin levels. **P

43). Zhang Q et al. Anti-inflammatory action of ambuic acid, a natural product isolated from the solid culture of Pestalotiopsis neglecta, through blocking ERK/JNK mitogen-activated protein kinase signaling pathway. Exp Ther Med 2018 Aug;16(2):1538-1546 (PubMed: 30116402)

44). Peng J et al. MiR-377 promotes white adipose tissue inflammation and decreases insulin sensitivity in obesity via suppression of sirtuin-1 (SIRT1). Oncotarget 2017 Jul 31;8(41):70550-70563 (PubMed: 29050301)

Application: WB Species:mouse; Sample:Not available

Figure 4: MiR-377 promotes inﬂammation and insulin-resistance in mature 3T3-L1 cells. After transfection with 100 nM miR-377 mimics or inhibitor for 24 h, differentiated 3T3-L1 adipocytes were treated with 10 ng/ml TNFα for 24 h and then stimulated with 100 nM insulin for 15 min. Cells were then harvested for real-time PCR and immunoblotting analyses. (A) The effect of miR-377 overexpression on inﬂammation-related gene expression. *P < 0.05, **P < 0.01 vs. NC 0.1% BSA; ##P < 0.01 vs. NC 10 ng/ml TNFα; ns, not signifcant (n = 3). (B) The effect of miR-377 inhibition on inﬂammation-related gene expression under conditions of TNFα-induced insulin-resistance. ##P < 0.01 vs. NC 10 ng/ml TNFα(n = 3). (C) The effect of miR-377 overexpression on JNK phosphorylation under conditions of TNFα-induced insulin-resistance. *P < 0.05 vs. NC without insulin; #P < 0.05 vs. NC with insulin (n = 3). (D and E) The effect of miR-377 overexpression on AKT and ERK phosphorylation. *P < 0.05 vs. NC with 0.1% BSA and insulin; #P < 0.05 vs. NC with 10 ng/ml TNFα and insulin (n = 3). (F) The effect of miR-377 inhibition on JNK phosphorylation under conditions of TNFα-induced insulin-resistance. *P < 0.05 vs. NC without insulin; #P < 0.05 vs. NC with insulin (n = 3). (G and H) The effect of miR-377 inhibition on AKT and ERK phosphorylation. *P < 0.05 vs. NC with 0.1% BSA and insulin; #P < 0.05 vs. NC with 10 ng/ml TNFα and insulin (n = 3).

45). et al. Study on β-Chitosan against the binding of SARS-CoV-2S-RBD/ACE2.

46). et al. Reversibility of Hat-mscs Phenotypic and Metabolic Changes After Exposure to and Withdrawal Form Hccconditioned Medium Through Regulation of the Ros/mapk/hif-1α Signalling Pathway.

47). Miao Z et al. Transcriptome sequencing reveals fibrotic associated-genes involved in bovine mammary fibroblasts with Staphylococcus aureus. Int J Biochem Cell Biol 2020 Apr;121:105696 (PubMed: 32001362)

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Catalog Number :

AF3318-BP
(Blocking peptide available as AF3318-BP)

Price/Size :

$350/1mg.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).

Function :

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.

Format and storage :

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.

Precautions :

This product is for research use only. Not for use in diagnostic or therapeutic procedures.

Xenopus

100%

Chicken

100%

Rabbit

100%

Pig

100%

Dog

100%

Bovine

100%

Sheep

100%

Horse

100%

Zebrafish

79%

High similarity Medium similarity Low similarity No similarity

P45983/P45984/P53779 as Substrate

Site	PTM Type	Enzyme	Source
S2	Phosphorylation		Uniprot
K30	Ubiquitination		Uniprot
K56	Ubiquitination		Uniprot
K68	Ubiquitination		Uniprot
C116	S-Nitrosylation		Uniprot
S129	Phosphorylation	Q05655 (PRKCD)	Uniprot
S144	Phosphorylation		Uniprot
K153	Ubiquitination		Uniprot
S155	Phosphorylation		Uniprot
K160	Ubiquitination		Uniprot
K166	Ubiquitination		Uniprot
T178	Phosphorylation		Uniprot
S179	Phosphorylation		Uniprot
T183	Phosphorylation	P45985 (MAP2K4) , O14733 (MAP2K7) , Q99683 (MAP3K5) , O95382 (MAP3K6)	Uniprot
Y185	Phosphorylation	P45985 (MAP2K4) , P07949 (RET) , Q99683 (MAP3K5) , O14733 (MAP2K7) , O95382 (MAP3K6)	Uniprot
T188	Phosphorylation		Uniprot
T243	Phosphorylation		Uniprot
K250	Ubiquitination		Uniprot
K251	Ubiquitination		Uniprot
T255	Phosphorylation		Uniprot
T258	Phosphorylation		Uniprot
Y259	Phosphorylation		Uniprot
K265	Ubiquitination		Uniprot
K273	Ubiquitination		Uniprot
K288	Ubiquitination		Uniprot
S292	Phosphorylation		Uniprot
K300	Ubiquitination		Uniprot
S307	Phosphorylation		Uniprot
K308	Acetylation		Uniprot
K308	Ubiquitination		Uniprot
K336	Ubiquitination		Uniprot
K353	Ubiquitination		Uniprot
Y357	Phosphorylation		Uniprot
T367	Phosphorylation		Uniprot
S377	Phosphorylation		Uniprot

Site	PTM Type	Enzyme	Source
K56	Ubiquitination		Uniprot
K68	Ubiquitination		Uniprot
S144	Phosphorylation		Uniprot
K153	Ubiquitination		Uniprot
S155	Phosphorylation		Uniprot
K160	Ubiquitination		Uniprot
C163	S-Nitrosylation		Uniprot
K166	Ubiquitination		Uniprot
T178	Phosphorylation		Uniprot
T183	Phosphorylation	O14733 (MAP2K7)	Uniprot
Y185	Phosphorylation	P45985 (MAP2K4) , P07949 (RET) , O14733 (MAP2K7)	Uniprot
T188	Phosphorylation		Uniprot
K250	Acetylation		Uniprot
K250	Ubiquitination		Uniprot
K251	Ubiquitination		Uniprot
S292	Phosphorylation		Uniprot
K300	Ubiquitination		Uniprot
S311	Phosphorylation		Uniprot
K353	Ubiquitination		Uniprot
Y357	Phosphorylation		Uniprot
T386	Phosphorylation		Uniprot
T404	Phosphorylation	O14733 (MAP2K7) , P68400 (CSNK2A1)	Uniprot
S407	Phosphorylation	P68400 (CSNK2A1) , O14733 (MAP2K7)	Uniprot

Site	PTM Type	Enzyme	Source
K94	Ubiquitination		Uniprot
K106	Ubiquitination		Uniprot
T131	Phosphorylation	Q00535 (CDK5)	Uniprot
S182	Phosphorylation		Uniprot
K191	Ubiquitination		Uniprot
S193	Phosphorylation		Uniprot
K198	Ubiquitination		Uniprot
K204	Ubiquitination		Uniprot
T216	Phosphorylation		Uniprot
S217	Phosphorylation		Uniprot
T221	Phosphorylation	O14733 (MAP2K7)	Uniprot
Y223	Phosphorylation	P45985 (MAP2K4)	Uniprot
T226	Phosphorylation		Uniprot
T281	Phosphorylation		Uniprot
K288	Ubiquitination		Uniprot
K289	Ubiquitination		Uniprot
S330	Phosphorylation		Uniprot
K346	Acetylation		Uniprot
K391	Ubiquitination		Uniprot

P45983/P45984/P53779 as PTM Enzyme

Substrate	Site	Source
O00418 (EEF2K)	S396	Uniprot
O43521-2 (BCL2L11)	S44	Uniprot
O43521-17 (BCL2L11)	T56	Uniprot
O43521-2 (BCL2L11)	S58	Uniprot
O43521-1 (BCL2L11)	S59	Uniprot
O43521-1 (BCL2L11)	S69	Uniprot
O43521-1 (BCL2L11)	S77	Uniprot
O43521-1 (BCL2L11)	S104	Uniprot
O43521 (BCL2L11)	T116	Uniprot
O43521-1 (BCL2L11)	S118	Uniprot
O43524 (FOXO3)	S574	Uniprot
O43561-2 (LAT)	T155	Uniprot
O43561 (LAT)	T184	Uniprot
O95644 (NFATC1)	S172	Uniprot
P01106 (MYC)	T58	Uniprot
P01106 (MYC)	S62	Uniprot
P01106 (MYC)	S71	Uniprot
P01106-2 (MYC)	S77	Uniprot
P01106-2 (MYC)	S86	Uniprot
P04150 (NR3C1)	S226	Uniprot
P04637 (TP53)	S20	Uniprot
P04637 (TP53)	S37	Uniprot
P04637-1 (TP53)	T81	Uniprot
P05067-4 (APP)	T668	Uniprot
P05067 (APP)	T743	Uniprot
P05412 (JUN)	S63	Uniprot
P05412 (JUN)	S73	Uniprot
P05412 (JUN)	T91	Uniprot
P05412 (JUN)	T93	Uniprot
P05787 (KRT8)	S74	Uniprot
P05787 (KRT8)	S432	Uniprot
P08047 (SP1)	T278	Uniprot
P08047 (SP1)	T739	Uniprot
P10275 (AR)	S651	Uniprot
P10276 (RARA)	T181	Uniprot
P10276 (RARA)	S445	Uniprot
P10276 (RARA)	S461	Uniprot
P10415-1 (BCL2)	T69	Uniprot
P10415 (BCL2)	S70	Uniprot
P10415 (BCL2)	S87	Uniprot
P10636-8 (MAPT)	T181	Uniprot
P10636-8 (MAPT)	S202	Uniprot
P10636-8 (MAPT)	T231	Uniprot
P10636-8 (MAPT)	S396	Uniprot
P10636 (MAPT)	T498	Uniprot
P10636 (MAPT)	S516	Uniprot
P10636 (MAPT)	S519	Uniprot
P10636 (MAPT)	T522	Uniprot
P10636 (MAPT)	T529	Uniprot
P10636 (MAPT)	T534	Uniprot
P10636 (MAPT)	S713	Uniprot
P10636 (MAPT)	S721	Uniprot
P10636 (MAPT)	S739	Uniprot
P14618-2 (PKM)	T365	Uniprot
P15336 (ATF2)	T69	Uniprot
P15336 (ATF2)	T71	Uniprot
P15336 (ATF2)	S90	Uniprot
P16104 (H2AFX)	S140	Uniprot
P16949 (STMN1)	S25	Uniprot
P16949 (STMN1)	S38	Uniprot
P17275 (JUNB)	T102	Uniprot
P17275 (JUNB)	T104	Uniprot
P17535 (JUND)	S90	Uniprot
P17535 (JUND)	S100	Uniprot
P17535 (JUND)	T117	Uniprot
P19419 (ELK1)	S383	Uniprot
P19419 (ELK1)	S389	Uniprot
P19793 (RXRA)	S56	Uniprot
P19793 (RXRA)	S70	Uniprot
P19793 (RXRA)	T82	Uniprot
P19793 (RXRA)	S260	Uniprot
P22736 (NR4A1)	S95	Uniprot
P23443 (RPS6KB1)	S434	Uniprot
P29353 (SHC1)	S36	Uniprot
P30305-2 (CDC25B)	S101	Uniprot
P30305-2 (CDC25B)	S103	Uniprot
P30305 (CDC25B)	S115	Uniprot
P30305 (CDC25B)	S117	Uniprot
P30307 (CDC25C)	S168	Uniprot
P31946 (YWHAB)	S186	Uniprot
P31947 (SFN)	S186	Uniprot
P35222 (CTNNB1)	S33	Uniprot
P35222 (CTNNB1)	S37	Uniprot
P35222 (CTNNB1)	T41	Uniprot
P35568 (IRS1)	S307	Uniprot
P35568 (IRS1)	S312	Uniprot
P35568 (IRS1)	S315	Uniprot
P35568 (IRS1)	S616	Uniprot
P35568 (IRS1)	S636	Uniprot
P36956-3 (SREBF1)	T81	Uniprot
P36956-3 (SREBF1)	S93	Uniprot
P36956 (SREBF1)	S117	Uniprot
P37231-2 (PPARG)	S84	Uniprot
P37231 (PPARG)	S112	Uniprot
P38936 (CDKN1A)	T57	Uniprot
P38936 (CDKN1A)	S98	Uniprot
P38936 (CDKN1A)	S130	Uniprot
P40763-2 (STAT3)	S726	Uniprot
P40763 (STAT3)	S727	Uniprot
P41970 (ELK3)	S357	Uniprot
P41970 (ELK3)	S363	Uniprot
P41970 (ELK3)	S396	Uniprot
P41970 (ELK3)	S401	Uniprot
P42224 (STAT1)	S727	Uniprot
P42226 (STAT6)	S707	Uniprot
P49023 (PXN)	S178	Uniprot
P54259 (ATN1)	S739	Uniprot
P55957 (BID)	T59	Uniprot
P61978 (HNRNPK)	S216	Uniprot
P61978 (HNRNPK)	S353	Uniprot
P63104-1 (YWHAZ)	S184	Uniprot
P68431 (HIST1H3J)	S29	Uniprot
P78352 (DLG4)	S295	Uniprot
P84243 (H3F3B)	S29	Uniprot
P98177 (FOXO4)	T227	Uniprot
P98177 (FOXO4)	S230	Uniprot
P98177 (FOXO4)	T451	Uniprot
P98177 (FOXO4)	T455	Uniprot
Q00613-1 (HSF1)	S363	Uniprot
Q01844 (EWSR1)	T79	Uniprot
Q05639 (EEF1A2)	S205	Uniprot
Q05639 (EEF1A2)	S358	Uniprot
Q06481 (APLP2)	T736	Uniprot
Q07817 (BCL2L1)	T47	Uniprot
Q07817 (BCL2L1)	S62	Uniprot
Q07817 (BCL2L1)	T115	Uniprot
Q07820 (MCL1)	S64	Uniprot
Q07820 (MCL1)	S121	Uniprot
Q07820 (MCL1)	T163	Uniprot
Q12904 (AIMP1)	S140	Uniprot
Q12904 (AIMP1)	T164	Uniprot
Q13043 (STK4)	S82	Uniprot
Q13363 (CTBP1)	S422	Uniprot
Q13950 (RUNX2)	S118	Uniprot
Q14653 (IRF3)	S173	Uniprot
Q14934 (NFATC4)	S213	Uniprot
Q14934 (NFATC4)	S217	Uniprot
Q15672 (TWIST1)	S68	Uniprot
Q16621 (NFE2)	S157	Uniprot
Q5JR12 (PPM1J)	S93	Uniprot
Q5JR12 (PPM1J)	T201	Uniprot
Q5JR12 (PPM1J)	T204	Uniprot
Q8N122 (RPTOR)	S696	Uniprot
Q8N122 (RPTOR)	T706	Uniprot
Q8N122 (RPTOR)	S863	Uniprot
Q8WYK2-1 (JDP2)	T148	Uniprot
Q92934 (BAD)	S75	Uniprot
Q92934 (BAD)	S91	Uniprot
Q93045 (STMN2)	S62	Uniprot
Q93045 (STMN2)	S73	Uniprot
Q96EB6 (SIRT1)	S27	Uniprot
Q96EB6 (SIRT1)	S47	Uniprot
Q96EB6 (SIRT1)	T530	Uniprot
Q96J02 (ITCH)	S240	Uniprot
Q96J02 (ITCH)	T263	Uniprot
Q96J02 (ITCH)	S273	Uniprot
Q96LC9-2 (BMF)	S74	Uniprot
Q96LC9-2 (BMF)	S77	Uniprot
Q99607 (ELF4)	S641	Uniprot
Q99640 (PKMYT1)	S83	Uniprot
Q9H211 (CDT1)	T29	Uniprot
Q9H2B2 (SYT4)	S135	Uniprot
Q9NPI6 (DCP1A)	S315	Uniprot
Q9NR28 (DIABLO)	S6	Uniprot
Q9NR28 (DIABLO)	S9	Uniprot
Q9NRA8 (EIF4ENIF1)	S301	Uniprot
Q9NRA8 (EIF4ENIF1)	S374	Uniprot
Q9NRA8 (EIF4ENIF1)	S513	Uniprot
Q9NRA8 (EIF4ENIF1)	S587	Uniprot
Q9NRA8 (EIF4ENIF1)	S693	Uniprot
Q9NRA8 (EIF4ENIF1)	S752	Uniprot
Q9UPT6-1 (MAPK8IP3)	T265	Uniprot
Q9UPT6-1 (MAPK8IP3)	T275	Uniprot
Q9UPT6 (MAPK8IP3)	T286	Uniprot
Q9UQF2 (MAPK8IP1)	S15	Uniprot
Q9UQF2 (MAPK8IP1)	S29	Uniprot
Q9UQF2 (MAPK8IP1)	T103	Uniprot
Q9UQF2 (MAPK8IP1)	S197	Uniprot
Q9UQF2 (MAPK8IP1)	T205	Uniprot
Q9UQF2 (MAPK8IP1)	T284	Uniprot
Q9UQF2 (MAPK8IP1)	S341	Uniprot
Q9UQF2 (MAPK8IP1)	S421	Uniprot
Q9Y4H2 (IRS2)	T350	Uniprot
Q9Y4H2 (IRS2)	S491	Uniprot
Q9Y5Q3 (MAFB)	T62	Uniprot
Q9Y6Q9 (NCOA3)	T24	Uniprot
Q9Y6Q9 (NCOA3)	S505	Uniprot
Q9Y6Q9 (NCOA3)	S543	Uniprot
Q9Y6Q9 (NCOA3)	S860	Uniprot
Q9Y6Q9 (NCOA3)	S867	Uniprot

Substrate	Site	Source
O00418 (EEF2K)	S396	Uniprot
O43521-2 (BCL2L11)	T56	Uniprot
O43521-1 (BCL2L11)	S59	Uniprot
O43521 (BCL2L11)	S69	Uniprot
O43521-1 (BCL2L11)	S77	Uniprot
O43602-2 (DCX)	T321	Uniprot
O43602-2 (DCX)	T331	Uniprot
O43602-2 (DCX)	S334	Uniprot
O60239-2 (SH3BP5)	S194	Uniprot
O60239-2 (SH3BP5)	S264	Uniprot
O60239 (SH3BP5)	S351	Uniprot
O60239-1 (SH3BP5)	S421	Uniprot
O95140 (MFN2)	S27	Uniprot
P01106 (MYC)	S62	Uniprot
P01106 (MYC)	S71	Uniprot
P04150 (NR3C1)	S226	Uniprot
P04637 (TP53)	S6	Uniprot
P04637 (TP53)	S20	Uniprot
P04637 (TP53)	S37	Uniprot
P04637 (TP53)	T81	Uniprot
P05067-4 (APP)	T668	Uniprot
P05067 (APP)	T743	Uniprot
P05412 (JUN)	S63	Uniprot
P05412 (JUN)	S73	Uniprot
P10636-8 (MAPT)	T181	Uniprot
P10636-8 (MAPT)	S202	Uniprot
P10636-8 (MAPT)	T212	Uniprot
P10636-8 (MAPT)	T217	Uniprot
P10636-8 (MAPT)	T231	Uniprot
P10636 (MAPT)	T498	Uniprot
P10636 (MAPT)	S516	Uniprot
P10636 (MAPT)	S519	Uniprot
P10636 (MAPT)	T529	Uniprot
P10636 (MAPT)	T548	Uniprot
P10636 (MAPT)	S713	Uniprot
P10636 (MAPT)	S721	Uniprot
P10636 (MAPT)	S739	Uniprot
P15036 (ETS2)	T72	Uniprot
P15336 (ATF2)	T69	Uniprot
P15336 (ATF2)	T71	Uniprot
P15336 (ATF2)	S90	Uniprot
P16104 (H2AFX)	S140	Uniprot
P16949 (STMN1)	S25	Uniprot
P16949 (STMN1)	S38	Uniprot
P19419-1 (ELK1)	S383	Uniprot
P19419 (ELK1)	S389	Uniprot
P19793 (RXRA)	S56	Uniprot
P19793 (RXRA)	S70	Uniprot
P19793 (RXRA)	T82	Uniprot
P19793 (RXRA)	S260	Uniprot
P23443 (RPS6KB1)	S434	Uniprot
P29353 (SHC1)	S36	Uniprot
P30307 (CDC25C)	S168	Uniprot
P31645 (SLC6A4)	T616	Uniprot
P31947 (SFN)	S186	Uniprot
P35222 (CTNNB1)	S191	Uniprot
P35222 (CTNNB1)	S605	Uniprot
P35568 (IRS1)	S307	Uniprot
P35568 (IRS1)	S315	Uniprot
P35568 (IRS1)	Y612	Uniprot
P35568 (IRS1)	Y632	Uniprot
P40763 (STAT3)	S727	Uniprot
P41970 (ELK3)	S357	Uniprot
P41970 (ELK3)	S363	Uniprot
P41970 (ELK3)	S396	Uniprot
P41970 (ELK3)	S401	Uniprot
P42224 (STAT1)	S727	Uniprot
P46937 (YAP1)	T119	Uniprot
P46937 (YAP1)	S138	Uniprot
P46937 (YAP1)	T154	Uniprot
P46937 (YAP1)	S367	Uniprot
P49768 (PSEN1)	S319	Uniprot
P49768 (PSEN1)	T320	Uniprot
P50616 (TOB1)	S152	Uniprot
P50616 (TOB1)	S154	Uniprot
P50616 (TOB1)	S164	Uniprot
P52945 (PDX1)	S61	Uniprot
P52945 (PDX1)	S66	Uniprot
P54259 (ATN1)	S739	Uniprot
P55957 (BID)	T59	Uniprot
P63104 (YWHAZ)	S184	Uniprot
P68431 (HIST1H3J)	S29	Uniprot
P84243 (H3F3B)	S29	Uniprot
P98177 (FOXO4)	T451	Uniprot
P98177 (FOXO4)	T455	Uniprot
Q06481 (APLP2)	T736	Uniprot
Q07817 (BCL2L1)	T47	Uniprot
Q07817 (BCL2L1)	S62	Uniprot
Q07817 (BCL2L1)	T115	Uniprot
Q12968 (NFATC3)	S163	Uniprot
Q12968-1 (NFATC3)	S165	Uniprot
Q14653 (IRF3)	S173	Uniprot
Q14934 (NFATC4)	S213	Uniprot
Q14934 (NFATC4)	S217	Uniprot
Q5JR12 (PPM1J)	S93	Uniprot
Q8IW41 (MAPKAPK5)	T182	Uniprot
Q8WYK2 (JDP2)	T148	Uniprot
Q9BQQ3 (GORASP1)	S274	Uniprot
Q9NYV6 (RRN3)	T200	Uniprot
Q9UIG0 (BAZ1B)	S158	Uniprot
Q9UPT6 (MAPK8IP3)	T265	Uniprot
Q9UPT6 (MAPK8IP3)	T275	Uniprot
Q9UPT6 (MAPK8IP3)	T286	Uniprot
Q9UQF2 (MAPK8IP1)	T103	Uniprot

Substrate	Site	Source
O43521-2 (BCL2L11)	S58	Uniprot
O43521-1 (BCL2L11)	S59	Uniprot
O43521-1 (BCL2L11)	S69	Uniprot
O43521-1 (BCL2L11)	S77	Uniprot
O43521 (BCL2L11)	T116	Uniprot
O60282 (KIF5C)	S176	Uniprot
O95644 (NFATC1)	S172	Uniprot
P01106 (MYC)	T58	Uniprot
P01106 (MYC)	S62	Uniprot
P01106 (MYC)	S71	Uniprot
P04150 (NR3C1)	S226	Uniprot
P04637 (TP53)	S37	Uniprot
P05067-4 (APP)	T668	Uniprot
P05067 (APP)	T743	Uniprot
P05412 (JUN)	S63	Uniprot
P05412 (JUN)	S73	Uniprot
P10415 (BCL2)	T56	Uniprot
P10415 (BCL2)	S70	Uniprot
P10415 (BCL2)	T74	Uniprot
P10415 (BCL2)	S87	Uniprot
P10636 (MAPT)	T498	Uniprot
P10636 (MAPT)	S516	Uniprot
P10636 (MAPT)	S519	Uniprot
P10636 (MAPT)	T522	Uniprot
P10636 (MAPT)	T529	Uniprot
P10636 (MAPT)	T534	Uniprot
P10636 (MAPT)	S713	Uniprot
P10636 (MAPT)	S721	Uniprot
P10636 (MAPT)	S739	Uniprot
P16949 (STMN1)	S25	Uniprot
P16949 (STMN1)	S38	Uniprot
P29353 (SHC1)	S36	Uniprot
P30307 (CDC25C)	S168	Uniprot
P31947 (SFN)	S186	Uniprot
P54259 (ATN1)	S739	Uniprot
P55957 (BID)	T59	Uniprot
P61978-1 (HNRNPK)	S216	Uniprot
P61978-1 (HNRNPK)	S284	Uniprot
P61978-1 (HNRNPK)	S353	Uniprot
P63104 (YWHAZ)	S184	Uniprot
Q06481 (APLP2)	T736	Uniprot
Q07820 (MCL1)	S121	Uniprot
Q07820 (MCL1)	T163	Uniprot
Q16600 (ZNF239)	S38	Uniprot
Q16600 (ZNF239)	S129	Uniprot
Q5JR12 (PPM1J)	S93	Uniprot
Q93045 (STMN2)	S62	Uniprot
Q93045 (STMN2)	S73	Uniprot
Q9UPT6 (MAPK8IP3)	T265	Uniprot
Q9UPT6 (MAPK8IP3)	T275	Uniprot
Q9UPT6-1 (MAPK8IP3)	T286	Uniprot

IMPORTANT: For western blots, incubate membrane with diluted antibody in 5% w/v milk , 1X TBS, 0.1% Tween®20 at 4°C with gentle shaking, overnight.

Secondary antibody Goat Anti-Rabbit IgG (H+L) HRP (S0001) Goat Anti-Rabbit IgG (H+L) AP (S0003) Goat Anti-Rabbit IgG (H+L) Fluor594-conjugated (S0006) Goat Anti-Rabbit IgG (H+L) FITC-conjugated (S0008) Goat Anti-Rabbit IgG (H+L) CY3-conjugated (S0011) Goat Anti-Rabbit IgG (H+L) Fluor647-conjugated (S0013) Goat Anti-Rabbit IgG (H+L) TRITC-conjugated (S0015) Goat Anti-Rabbit IgG (H+L) Fluor488-conjugated (S0018)

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