JNK2 Antibody (YA4034)
(Synonyms: JNK2; SAPK; p54a; JNK2A; JNK2B; PRKM9; JNK-55; SAPK1a; JNK2BETA; p54aSAPK; JNK2ALPHA)JNK2 Antibody (YA4034) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to JNK2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, FC, ELISA
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Reactivity :
Human
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Formulation:
Supplied in PBS with 0.05% sodium azide
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:400 | 1:10000 |
Product Details
JNK2 Antibody (YA4034) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to JNK2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 48 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 48 kDa
Purified recombinant fragment of human MAPK9 (AA: 227-382) expressed in E. Coli.
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS with 0.05% sodium azide
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
JNK2 (MAPK9) is a member of the c-Jun N-terminal kinase (JNK) family, a stress-activated branch of the mitogen-activated protein kinase (MAPK) network that transduces extracellular stress, cytokine, and growth-factor signals into cellular responses regulating proliferation, survival, apoptosis, differentiation, and inflammation[1][2]. Mechanistically, JNK signaling is activated through a kinase cascade involving MAP3Ks, MKK4, and MKK7, leading to phosphorylation of transcriptional regulators such as c-Jun and other stress-responsive substrates that control gene expression programs[3][4]. In disease-associated contexts, dysregulated JNK signaling has been linked to cancer, obesity, type 2 diabetes, inflammatory disorders, neurodegenerative diseases, and pathological cell death, making the pathway a widely studied experimental target[1][2][3]. Compared with related isoforms, JNK1 and JNK2 are broadly expressed across tissues, whereas JNK3 shows a more restricted distribution, primarily in the brain, heart, and testis[1][3]. Importantly, JNK1 and JNK2 can exhibit both redundant and opposing biological functions, and experimental studies have demonstrated that JNK1, but not JNK2, is required for specific TNF-α-induced responses including c-Jun kinase activation and apoptosis, highlighting isoform-specific signaling properties[1][4]. For experimental applications, the growing recognition of isoform-dependent JNK biology has stimulated the development of JNK inhibitors, with current research emphasizing improved selectivity and on-target specificity for mechanistic studies and therapeutic evaluation[1][2].
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Subcellular Localization
Cytoplasm; Nucleus
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Isoforms & Post-Translational Modification
P45984 has 5 isomers: P45984-1: 48139 Da (predicted); P45984-2: 44051 Da (predicted); P45984-3: 44223 Da (predicted); P45984-4: 48311 Da (predicted); P45984-5: 27334 Da (predicted).
Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro -
Subunit
Interacts with NFATC4 (PubMed:17875713). Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN (PubMed:10376527). Interacts with BCL10 (PubMed:17189706).
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SwissProt ID
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Synonyms
JNK2; SAPK; p54a; JNK2A; JNK2B; PRKM9; JNK-55; SAPK1a; JNK2BETA; p54aSAPK; JNK2ALPHA
Documentation
[1]. Harrison R, et al. Enacting open disclosure in the UK National Health Service: A qualitative exploration. J Eval Clin Pract. 2017 Aug;23(4):713-718. [Content Brief]
[2]. Karnam S, et al. Biochemical and biomechanical characteristics of dystrophin-deficient mdx3cv mouse lens. Biochim Biophys Acta Mol Basis Dis. 2021 Jan 1;1867(1):165998. [Content Brief]
[4]. Das D, et al. Secondary Structure Preferences of the Anthrax Toxin Protective Antigen Translocase. J Mol Biol. 2017 Mar 10;429(5):753-762. [Content Brief]