PKM2 Antibody (YA5244)
(Synonyms: CTHBP; Cytosolic thyroid hormone binding protein; Cytosolic thyroid hormone-binding protein; KPYM_HUMAN; MGC3932; OIP 3; OIP-3; OIP3; OPA interacting protein 3; Opa-interacting protein 3; p58; PK muscle type; PK, muscle type; PK2; PK3; PKM; PKM2; pykm; Pyruvate kinase 2/3; Pyruvate kinase 3; Pyruvate kinase isozymes M1/M2; Pyruvate kinase muscle; Pyruvate kinase muscle isozyme; pyruvate kinase PKM; Pyruvate kinase, muscle 2; TCB; THBP1; Thyroid hormone binding protein 1; Thyroid hormone binding protein cytosolic; Thyroid hormone-binding protein 1; Tumor M2 PK; Tumor M2-PK.)PKM2 Antibody (YA5244) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to PKM2.
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Host:
Mouse
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Application:
WB, ICC/IF
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Reactivity :
Human, Mouse, Rat, Monkey
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000 | 1:400 | 1:50-200 |
Product Details
PKM2 Antibody (YA5244) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to PKM2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat, Monkey
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Observed Molecular WeightObserved band size: 60 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
Purified recombinant human PKM2 protein fragments expressed in E.coli.
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% 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
Pyruvate kinase M2 (PKM2) is a glycolytic enzyme that catalyzes the final rate-limiting step of glycolysis, converting phosphoenolpyruvate to pyruvate and ATP, and it is highly expressed in proliferating cells and many tumor types[1]. PKM2 contributes to metabolic reprogramming by maintaining a relatively low catalytic state that redirects glucose-derived intermediates from energy production toward anabolic biosynthesis required for rapid cell growth[1][2]. Mechanistically, PKM2 functions not only as a metabolic enzyme but also as a regulator of gene expression and signaling, with nuclear PKM2 supporting transcriptional programs associated with proliferation, tumor growth, and metabolic adaptation[2][3]. In disease contexts, PKM2 expression has been closely associated with cancer metabolism, embryonic development, tissue repair, and multiple models of tumor progression[4][5]. Compared with the related isoform PKM1, which forms constitutively active tetramers with high catalytic activity, PKM2 exists in multiple oligomeric states and exhibits distinct regulatory properties that enable dynamic control of glycolytic flux and cellular biosynthetic pathways[1][6]. This functional distinction is considered a key determinant of the metabolic phenotype observed in proliferating cells and tumors[4][6]. For experimental applications, PKM2 has become a widely studied therapeutic target because modulation of its oligomeric state can alter both metabolic and non-metabolic functions[2]. Small-molecule activators that promote PKM2 tetramer formation, including TEPP-46, have been used extensively to investigate the relationship between PKM2 activity, glycolytic regulation, and disease-associated cellular phenotypes[2][7].
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Subcellular Localization
Cytoplasm; Nucleus; Cytoplasm
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Expression
Tissue_specificity:It is specifically expressed in proliferating cells, such as embryonic stem cells, embryonic cancer cells, and cancer cells; it is expressed in adult tissues (PubMed:18337823) . It is not expressed in tumor cells (PubMed:18337823) . -
Isoforms & Post-Translational Modification
P14618 has 3 isomers: P14618-1: 57937 Da (predicted); P14618-2: 58062 Da (predicted); P14618-3: 56273 Da (predicted).
ISGylated;Under hypoxia, hydroxylated by EGLN3;Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy;Acetylated at Lys-433 by EP300, leading to impair phosphoenolpyruvate substrate-binding and promote its homodimerization and subsequent translocation to the nucleus (PubMed:24120661). Deacetylation at Lys-433 by SIRT6 promotes its nuclear export into the cytoplasm, leading to suppress its nuclear localization and oncogenic function (PubMed:26787900);S-nitrosylation at Cys-423 and Cys-424 inhibits homotetramerization and pyruvate kinase activity (PubMed:30487609). S-nitrosylation is indirectly inhibited by AKR1A1 which degrades S-nitroso-CoA, a cofactor required to S-nitrosylate proteins (PubMed:30487609);FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35 -
Subunit
Monomer and homotetramer; exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). The monomeric form binds 3,3',5-triiodo-L-thyronine (T3) (PubMed:15996096). Tetramer formation induces pyruvate kinase activity (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). FBP stimulates the formation of tetramers from dimers (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). Homodimer; exists in a dimeric form in tumor cells and the dimeric form has less affinity for the phosphoenolpyruvate substrate (PubMed:22306293, PubMed:24120661). The homodimer converts into a protein kinase (PubMed:22306293, PubMed:24120661). Interacts with HERC1, POU5F1 and PML (PubMed:12650930, PubMed:18191611). Interacts with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A (PubMed:21483450, PubMed:21620138). Interacts with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (PubMed:21620138). Interacts with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (PubMed:25263439). Interacts with JMJD8 (PubMed:27199445). Interacts with TRAF4 (PubMed:32268273). Interacts with (phosphorylated) CTNNB1; leading to activate transcription (PubMed:22056988). Interacts with TSC22D2; the interaction results in reduced nuclear levels of PKM isoform M2, leading to repression of cyclin CCND1 transcription and reduced cell growth (PubMed:27573352)
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SwissProt ID
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Synonyms
CTHBP; Cytosolic thyroid hormone binding protein; Cytosolic thyroid hormone-binding protein; KPYM_HUMAN; MGC3932; OIP 3; OIP-3; OIP3; OPA interacting protein 3; Opa-interacting protein 3; p58; PK muscle type; PK, muscle type; PK2; PK3; PKM; PKM2; pykm; Pyruvate kinase 2/3; Pyruvate kinase 3; Pyruvate kinase isozymes M1/M2; Pyruvate kinase muscle; Pyruvate kinase muscle isozyme; pyruvate kinase PKM; Pyruvate kinase, muscle 2; TCB; THBP1; Thyroid hormone binding protein 1; Thyroid hormone binding protein cytosolic; Thyroid hormone-binding protein 1; Tumor M2 PK; Tumor M2-PK.
Documentation
[1]. Wang RH, et al. Hydrogen sulfide coordinates glucose metabolism switch through destabilizing tetrameric pyruvate kinase M2. Nat Commun. 2024 Aug 29;15(1):7463. [Content Brief]
[2]. Huang Y, et al. The adjuvant treatment role of ω-3 fatty acids by regulating gut microbiota positively in the acne vulgaris. J Dermatolog Treat. 2024 Dec;35(1):2299107. [Content Brief]
[3]. Snaebjornsson MT, et al. Non-canonical functions of enzymes facilitate cross-talk between cell metabolic and regulatory pathways. Exp Mol Med. 2018 Apr 16;50(4):1-16. [Content Brief]
[4]. Dayton TL, et al. PKM2, cancer metabolism, and the road ahead. EMBO Rep. 2016 Dec;17(12):1721-1730. [Content Brief]
[5]. Wei Y, et al. Pyruvate kinase type M2 promotes tumour cell exosome release via phosphorylating synaptosome-associated protein 23. Nat Commun. 2017 Jan 9;8:14041. [Content Brief]
[6]. Chen X, et al. Protein kinase function of pyruvate kinase M2 and cancer. Cancer Cell Int. 2020 Oct 29;20(1):523. [Content Brief]
[7]. Yu C, et al. Pyruvate kinase M2 -mediated histone lactylation alters three-dimensional genomic architecture in polycystic ovary syndrome. Signal Transduct Target Ther. 2025 Nov 19;10(1):376. [Content Brief]
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