Recombinant human PKM2 protein (Active) (His tag N-Terminus)
- Bioactive
- What is this?
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(9 Publications)
Recombinant human PKM2 protein (Active) (His tag N-Terminus) is a Human Full Length protein, in the 1 to 531 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, WB, FuncS.
View Alternative Names
OIP3, PK2, PK3, PKM2, PKM, Pyruvate kinase PKM, Cytosolic thyroid hormone-binding protein, Opa-interacting protein 3, Pyruvate kinase 2/3, Pyruvate kinase muscle isozyme, Threonine-protein kinase PKM2, Thyroid hormone-binding protein 1, Tumor M2-PK, Tyrosine-protein kinase PKM2, p58, CTHBP, OIP-3, THBP1
- WB
Unknown
Western blot - Recombinant human PKM2 protein (Active) (His tag N-Terminus) (AB89364)
All lanes:
Anti-PKM antibody (<a href='/en-us/products/unavailable/pkm-antibody-ab85542'>ab85542</a>) at 1/1000 dilution
All lanes:
Western blot - Recombinant human PKM2 protein (Active) (His tag N-Terminus) (ab89364) at 0.1 µg
Secondary
All lanes:
Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution
true
Exposure time: 30s
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human PKM2 protein (Active) (His tag N-Terminus) (AB89364)
3ug of reduced ab89364 on SDS-PAGE under reducing condition and visualized by coomassie blue stain.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PKM2 is important in cellular energy metabolism and regulates the balance between glycolysis and oxidative phosphorylation. This enzyme can exist in both dimeric and tetrameric forms with its activity level depending on its structural state. PKM2 is part of multi-protein complexes that interact with other metabolic enzymes influencing metabolic pathways that impact growth and proliferation in cells.
Pathways
PKM2 is significant in the glycolytic pathway and is also involved in the regulation of the pentose phosphate pathway. It interacts with proteins like HIF-1α a transcription factor that responds to low oxygen levels to modulate metabolic and growth pathways under hypoxic conditions. This interaction affects biosynthetic processes and energy production in rapidly dividing cells such as those in tumors.
Specifications
Form
Liquid
Additional notes
ab89364 is purified using conventional chromatography techniques.
General info
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).. 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).. 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).
Sequence similarities
Belongs to the pyruvate kinase family.
Post-translational modifications
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.. 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).. 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).. FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35.
Subcellular localisation
Nucleus
Target data
Publications (9)
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Cell reports 43:115001 PubMed39580803
2024
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Chinese medicine 19:45 PubMed38454519
2024
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Molecular medicine reports 27: PubMed36799163
2023
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Cell death discovery 8:306 PubMed35790734
2022
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Frontiers in pharmacology 13:830312 PubMed35754468
2022
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Journal of the American Heart Association 11:e024854 PubMed35656980
2022
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Bioengineered 13:13089-13107 PubMed35615982
2022
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Molecular oncology 15:1466-1485 PubMed33314660
2020
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Cell communication and signaling : CCS 18:25 PubMed32054489
2020
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Product promise
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