Mouse PKM2 Protein 2382

$300.00 – $1,000.00

Summary

Expression: Baculovirus-Insect Cells
Pure: Yes (SDS-PAGE)
Amino Acid Range: Pro2-Pro531

SKU: 2382parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_001240812
express system	Baculovirus-Insect Cells
product tag	N-His
purity	> 95% as determined by Tris-Bis PAGE
background	Pyruvate kinase M2 (PKM2), a key rate-limiting enzyme of glycolysis, is a critical regulator in tumor metabolism. PKM2 has been demonstrated to overexpressed in various cancers and promoted proliferation and metastasis of tumor cells.
molecular weight	The protein has a predicted MW of 58.95 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Mouse PKM2 Protein 2382

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Pyruvate kinase M2 (PKM2), a key rate-limiting enzyme of glycolysis, is a critical regulator in tumor metabolism. PKM2 has been demonstrated to overexpressed in various cancers and promoted proliferation and metastasis of tumor cells.
Protein names Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (p58)
Protein family Pyruvate kinase family
Mass 57937Da
Function Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263). {ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:1854723, ECO:0000269\|PubMed:20847263}.; [Isoform M2]: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100). {ECO:0000250\|UniProtKB:P52480, ECO:0000269\|PubMed:17308100, ECO:0000269\|PubMed:18191611, ECO:0000269\|PubMed:18337823, ECO:0000269\|PubMed:20847263, ECO:0000269\|PubMed:21620138, ECO:0000269\|PubMed:22056988, ECO:0000269\|PubMed:22306293, ECO:0000269\|PubMed:22901803, ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:26787900}.; [Isoform M1]: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed:18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed:20847263). {ECO:0000269\|PubMed:18337823, ECO:0000269\|PubMed:20847263}.
Catalytic activity CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:1854723, ECO:0000269\|PubMed:20847263}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159; Evidence={ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:1854723, ECO:0000269\|PubMed:20847263}; CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000269\|PubMed:22306293, ECO:0000269\|PubMed:24120661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597; Evidence={ECO:0000269\|PubMed:22306293, ECO:0000269\|PubMed:24120661}; CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269\|PubMed:22901803, ECO:0000269\|PubMed:24120661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269\|PubMed:22901803, ECO:0000269\|PubMed:24120661}; CATALYTIC ACTIVITY: [Isoform M1]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000269\|PubMed:20847263};
Pathway PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:1854723}.
Subellular location [Isoform M2]: Cytoplasm {ECO:0000269\|PubMed:25263439, ECO:0000269\|PubMed:26787900, ECO:0000269\|PubMed:27573352, ECO:0000269\|PubMed:32268273}. Nucleus {ECO:0000269\|PubMed:17308100, ECO:0000269\|PubMed:18191611, ECO:0000269\|PubMed:22056988, ECO:0000269\|PubMed:22901803, ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:26787900, ECO:0000269\|PubMed:27573352, ECO:0000269\|PubMed:32268273}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli (PubMed:17308100, PubMed:22056988, PubMed:24120661). Nuclear translocation is promoted by acetylation by EP300 (PubMed:24120661). Deacetylation by SIRT6 promotes its nuclear export in a process dependent of XPO4, thereby suppressing its ability to activate transcription and promote tumorigenesis (PubMed:26787900). {ECO:0000269\|PubMed:17308100, ECO:0000269\|PubMed:22056988, ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:26787900}.; [Isoform M1]: Cytoplasm {ECO:0000305}.
Tissues [Isoform M2]: Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells. {ECO:0000269\|PubMed:18191611, ECO:0000269\|PubMed:18337823}.; [Isoform M1]: Expressed in adult tissues (PubMed:18337823). Not expressed in tumor cells (PubMed:18337823). {ECO:0000269\|PubMed:18337823}.
Structure [Isoform M2]: 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). {ECO:0000269\|PubMed:12650930, ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:18191611, ECO:0000269\|PubMed:18298799, ECO:0000269\|PubMed:18337815, ECO:0000269\|PubMed:1854723, ECO:0000269\|PubMed:21483450, ECO:0000269\|PubMed:21620138, ECO:0000269\|PubMed:22056988, ECO:0000269\|PubMed:22306293, ECO:0000269\|PubMed:23064226, ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:25263439, ECO:0000269\|PubMed:27199445, ECO:0000269\|PubMed:27573352, ECO:0000269\|PubMed:2813362, ECO:0000269\|PubMed:32268273}.; (Microbial infection) Binding to certain oncoproteins such as HPV-16 E7 oncoprotein promotes homodimerization. {ECO:0000269\|PubMed:24120661}.
Post-translational modification ISGylated. {ECO:0000269\|PubMed:16139798}.; Under hypoxia, hydroxylated by EGLN3. {ECO:0000269\|PubMed:21620138}.; Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:0000269\|PubMed:21700219, ECO:0000269\|Ref.11}.; [Isoform M2]: 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). {ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:26787900}.; [Isoform M2]: 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). {ECO:0000269\|PubMed:30487609}.; FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35. {ECO:0000269\|PubMed:25263439}.
Target Relevance information above includes information from UniProt accession: P14618
The UniProt Consortium

Mouse PKM2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.