Recombinant human PKM2 protein is a Human Full Length protein, in the 1 to 531 aa range, expressed in Escherichia coli, with >=80% purity and suitable for SDS-PAGE, FuncS.
M H H H H H H S K P H S E A G T A F I Q T Q Q L H A A M A D T F L E H M C R L D I D S P P I T A R N T G I I C T I G P A S R S V E T L K E M I K S G M N V A R L N F S H G T H E Y H A E T I K N V R T A T E S F A S D P I L Y R P V A V A L D T K G P E I R T G L I K G S G T A E V E L K K G A T L K I T L D N A Y M E K C D E N I L W L D Y K N I C K V V E V G S K I Y V D D G L I S L Q V K Q K G A D F L V T E V E N G G S L G S K K G V N L P G A A V D L P A V S E K D I Q D L K F G V E Q D V D M V F A S F I R K A S D V H E V R K V L G E K G K N I K I I S K I E N H E G V R R F D E I L E A S D G I M V A R G D L G I E I P A E K V F L A Q K M M I G R C N R A G K P V I C A T Q M L E S M I K K P R P T R A E G S D V A N A V L D G A D C I M L S G E T A K G D Y P L E A V R M Q H L I A R E A E A A M F H R K L F E E L V R A S S H S T D L M E A M A M G S V E A S Y K C L A A A L I V L T E S G R S A H Q V A R Y R P R A P I I A V T R N P Q T A R Q A H L Y R G I F P V L C K D P V Q E A W A E D V D L R V N F A M N V G K A R G F F K K G D V V I V L T G W R P G S G F T N T M R V V P V P
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. |
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).
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
Recombinant human PKM2 protein is a Human Full Length protein, in the 1 to 531 aa range, expressed in Escherichia coli, with >=80% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Preservative: 0.45% Imidazole
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
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).
Belongs to the pyruvate kinase family.
ISGylated.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
The target PKM2 also known as pyruvate kinase M2 is a type of enzyme that catalyzes the final step of glycolysis converting phosphoenolpyruvate (PEP) to pyruvate and generating ATP. The PKM2 protein has a molecular weight of about 58 kDa. PKM2 expresses in various tissues including muscles and certain cancer cells where it plays a significant role in metabolic processes. It exists in different isoforms with PKM1 being an alternative form found in pacemaker locations such as the brain and heart.
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.
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.
PKM2 has a link to cancer and metabolic diseases. PKM2 is often re-expressed in cancer cells where it shifts cellular metabolism to favor rapid growth and proliferation a process known as the Warburg effect. Additionally PKM2 has connections to metabolic disorders such as type 2 diabetes where dysregulated glucose metabolism plays an important role. PKM2’s interaction with proteins like Akt and mTOR can impact signaling pathways associated with cancer progression and metabolic dysregulation.
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Specific activity of ab196081 was determined to be 54 pmol/min/μg
SDS-PAGE using 13.5 μg ab196081 (Lane 1). Lane 2 shows protein marker.
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