Recombinant Mouse PKM Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10022P

Recombinant Mouse PKM Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10022P
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Product Overview

Host Species Mouse
Accession P52480
Synonym CTHBP Cytosolic thyroid hormone-binding protein KPYM_HUMAN OIP-3 Opa-interacting protein 3 p58 pkm PKM1 PKM2 Pyruvate kinase 2/3 Pyruvate kinase muscle isozyme Pyruvate kinase PKM THBP1 Thyroid hormone-binding protein 1 Tumor M2-PK
Description Recombinant Mouse PKM Protein (Tagged) was expressed in Mammalian. It is a Full length protein
Source Mammalian
Molecular Weight 58 kDa
Purity >90% by SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. 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. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. In addition to its role in glycolysis, also regulates transcription. Stimulates POU5F1-mediated transcriptional activation. Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages. Also acts 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. Plays a general role in caspase independent cell death of tumor cells.
Subcellular Location Cytoplasm. Nucleus.
Protein Families Pyruvate kinase family
Database References
Tissue Specificity Embryonic stem cells and embryonal carcinoma cells.

Gene Functions References

  1. PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23. PMID: 28067230
  2. PKM1 interacts with A-Raf, an upstream regulator of the MEK/ERK pathway, and that this interaction contributes to MEK1 phosphorylation by A-Raf. PMID: 28743549
  3. infiltrated/activated neutrophils at wound site release pyruvate kinase M2 (PKM2) by its secretive mechanisms during early stages of wound repair; the released extracellular PKM2 facilitates early wound healing by promoting angiogenesis at wound site PMID: 26808610
  4. The results suggested that targeting PKM2 with an oncolytic adenovirus produced a strong antitumor effect. PMID: 28569774
  5. PKM2 activation may protect against DN by increasing glucose metabolic flux, inhibiting the production of toxic glucose metabolites and inducing mitochondrial biogenesis to restore mitochondrial function. PMID: 28436957
  6. our results demonstrate that PKM2 is required to support metabolic reprogramming for homocysteine-induced B cell activation and function PMID: 27903739
  7. Jmjd8 is upregulated during endothelial differentiation and regulates endothelial sprouting and metabolism by interacting with pyruvate kinase M2. PMID: 27199445
  8. this study identifies a new signaling pathway for CD43 through the regulation of alternative functions of pyruvate kinase isoform M2, favoring cell survival following activation PMID: 27606486
  9. results show that the Aha1-Hsp90-PKM2/HIF-1alpha axis mediates the induction of aromatase in Li-Fraumeni Syndrome. PMID: 27467582
  10. in addition to its role in cancer metabolism, PKM2 plays a role in controlling systemic metabolic homeostasis and inflammation, thereby preventing hepatocellular carcinoma by a non-cell-autonomous mechanism. PMID: 27125672
  11. Evidence That Does Not Support Pyruvate Kinase M2 (PKM2)-catalyzed Reaction as a Rate-limiting Step in Cancer Cell Glycolysis. PMID: 26917721
  12. PKM2 promotes cell proliferation and insulin secretion, and inhibits apoptosis in pancreatic beta cells via Wnt/CTNNB1 signaling. PMID: 26823761
  13. Using [(32)P]-phosphoenolpyruvate (PEP) we examine the direct substrates of PKM2 using recombinant enzyme and in vitro systems where PKM2 is genetically deleted. The findings argue against a role for PKM2 as a protein kinase. PMID: 26300261
  14. LPS-induced PKM2 enters into a complex with Hif-1alpha, which can directly bind to the IL-1beta promoter, an event that is inhibited by activation of PKM2. PMID: 25565206
  15. observed a shift in the enzyme pyruvate kinase from the adult M1 (PKM1) isoform to the fetal M2 (PKM2) isoform, a hallmark of the Warburg Effect, in the heart after sunitinib treatment PMID: 25735978
  16. Muller glia compensate for their unique metabolic adaptations by using lactate and aspartate from neurons as surrogates for their missing PK and AGC1. PMID: 25313047
  17. PKM1 expression promotes a metabolic state that is unable to support DNA synthesis and cell proliferation. PMID: 25482511
  18. Up-regulation of PKM2 might protect intestinal epithelial cells against apoptosis possibly through Bcl-xl in Crohn's disease. PMID: 24817408
  19. This study provides the first evidence linking natural mutations in PKM2 with cancer. PMID: 24492614
  20. Our data reveal a complex interaction between STAT6 and PPARgamma in the regulation of liver and adipose tissue lipid depot distribution and design STAT6 as a novel link between inflammatory cell metabolism and adipocyte and hepatocyte function. PMID: 23917405
  21. PKM2 activity in beta-cells is oscillatory and are consistent with pulsatile PFK1 being the mediator of slow glycolytic oscillations. PMID: 24100037
  22. These data suggest that regulation of pyruvate kinase M2 isoform activity supports the different metabolic requirements of proliferating and nonproliferating tumor cells. PMID: 24120138
  23. PKM2 expression induces changes in type 1 fibers associated with muscle atrophy and muscle weakness in myotonic dystrophy type 1. PMID: 23901116
  24. PPARgamma contributes to PKM2 and HK2 expression in fatty liver PMID: 22334075
  25. Components of the mTOR/HIF1alpha/Myc-hnRNPs/PKM2 glycolysis signaling network could be targeted for the treatment of cancer caused by an aberrant RTK/PI3K/AKT/mTOR signaling pathway PMID: 21325052
  26. histidine-phosphorylated PGAM1 correlated with expression of PKM2 in cancer cell lines; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway PMID: 20847263
  27. splicing repressors hnRNP A1 and A2, as well as the polypyrimidine-tract-binding protein PTB, contribute to control of pyruvate kinase isoform M1 and M2 expression PMID: 20133837
  28. Findings suggest that tyrosine phosphorylation regulates PKM2 to provide a metabolic advantage to tumor cells, thereby promoting tumor growth. PMID: 19920251
  29. study showed IL-3-induced nuclear translocation of the M2 isoform of pyruvate kinase (M2-PK) and examined its significance in cell proliferation [pyruvate kinase M2 isoform] PMID: 17446165
  30. results demonstrate that M2 expression is necessary for aerobic glycolysis and that this metabolic phenotype provides a selective growth advantage for tumour cells in vivo PMID: 18337823
  31. These findings suggest that M2 pyruvate kinase is a metabolic sensor which regulates cell proliferation, cell growth and apoptotic cell death in a glucose supply-dependent manner. PMID: 19563799


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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