Recombinant Mouse PKM2 Protein (His Tag)

Name: Recombinant Mouse PKM2 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3834
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_001240812.1
Synonym	AA414905, AL024370, AL024424, Pk-2, Pk-3, Pk3, Pkm2
Background	Pyruvate kinase isozymes M2 also known as pyruvate kinase muscle isozyme 2 (PKM2), pyruvate kinase type K, cytosolic thyroid hormone-binding protein (CTHBP), thyroid hormone-binding protein 1 (THBP1), or opa-interacting protein 3 (OIP3), is an isoenzyme of the glycolytic enzyme pyruvate kinase. Pyruvate kinase isozymes M2 / PKM2 is a protein involved in glycolysis. The encoded protein is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. PKM2 has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. PKM2 has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Several alternatively spliced transcript variants encoding a few distinct isoforms have been reported. PKM2 functions as a glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. PKM2 may stimulates POU5F1-mediated transcriptional activation. This protein Plays a general role in caspase independent cell death of tumor cells. The ratio betwween 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 of PKM2 contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Description	A DNA sequence encoding the mouse PKM (NP_001240812.1) (Pro2-Pro531) was expressed with a His tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	His
AA Sequence	Pro2-Pro531
Molecular Weight	The recombinant mouse PKM consists of 548 a.a. and predicts a molecular mass of 60 KDa. It migrates as an approximately 59 KDa band in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 8.0..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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	KEGG: mmu:18746 STRING: 10090.ENSMUSP00000034834 UniGene: Mm.326167
Tissue Specificity	Embryonic stem cells and embryonal carcinoma cells.

Gene Functions References

PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23. PMID: 28067230
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
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
The results suggested that targeting PKM2 with an oncolytic adenovirus produced a strong antitumor effect. PMID: 28569774
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
our results demonstrate that PKM2 is required to support metabolic reprogramming for homocysteine-induced B cell activation and function PMID: 27903739
Jmjd8 is upregulated during endothelial differentiation and regulates endothelial sprouting and metabolism by interacting with pyruvate kinase M2. PMID: 27199445
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
results show that the Aha1-Hsp90-PKM2/HIF-1alpha axis mediates the induction of aromatase in Li-Fraumeni Syndrome. PMID: 27467582
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
Evidence That Does Not Support Pyruvate Kinase M2 (PKM2)-catalyzed Reaction as a Rate-limiting Step in Cancer Cell Glycolysis. PMID: 26917721
PKM2 promotes cell proliferation and insulin secretion, and inhibits apoptosis in pancreatic beta cells via Wnt/CTNNB1 signaling. PMID: 26823761
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
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
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
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
PKM1 expression promotes a metabolic state that is unable to support DNA synthesis and cell proliferation. PMID: 25482511
Up-regulation of PKM2 might protect intestinal epithelial cells against apoptosis possibly through Bcl-xl in Crohn's disease. PMID: 24817408
This study provides the first evidence linking natural mutations in PKM2 with cancer. PMID: 24492614
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
PKM2 activity in beta-cells is oscillatory and are consistent with pulsatile PFK1 being the mediator of slow glycolytic oscillations. PMID: 24100037
These data suggest that regulation of pyruvate kinase M2 isoform activity supports the different metabolic requirements of proliferating and nonproliferating tumor cells. PMID: 24120138
PKM2 expression induces changes in type 1 fibers associated with muscle atrophy and muscle weakness in myotonic dystrophy type 1. PMID: 23901116
PPARgamma contributes to PKM2 and HK2 expression in fatty liver PMID: 22334075
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
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
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
Findings suggest that tyrosine phosphorylation regulates PKM2 to provide a metabolic advantage to tumor cells, thereby promoting tumor growth. PMID: 19920251
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
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
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.

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