Recombinant Human PKM2 Protein (N-6His)

Name: Recombinant Human PKM2 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1573NP
Availability: InStock

BL-1573NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Pyruvate Kinase Isoform M2 is produced by our E.coli expression system and the target gene encoding Ser2-Pro531 is expressed with a 6His tag at the N-terminus.
Accession	P14618
Synonym	Pyruvate kinase PKM; CTHBP; OIP-3; THBP1
Gene Background	Pyruvate kinase isoform M2 (PKM2) is a member of the pyruvate kinase (PK) family, a pivotal glycolytic enzyme that is consistently changed during tumorigenesis. PKM2 is expressed in some differentiated tissues, such as lung, fat tissue, retina, and pancreatic islets. As the rate-controlling enzyme in glycolysis, PKM2, has also been found to be expressed in embryonic, proliferating, and tumor cells, and it has been considered to be crucial for the metabolism and growth of tumor cells. Recent studies have shown that PKM2 promotes cell proliferation and suppresses cell apoptosis in various tumors. In addition, it has been reported that the PKM2 knockdown affects the Akt and ERK protein kinases.
Molecular Mass	60.1 KDa
Apmol Mass	60 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 50mM NaCl, 0.05% Brij-35, 1mM DTT, pH7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 9021 OMIM: 179050 KEGG: hsa:5315 STRING: 9606.ENSP00000320171 UniGene: Hs.534770
Tissue Specificity	Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.

Gene Functions References

results reveal that nBP1a/PKM2 interaction activates lipid metabolism genes in cancer cells and that Thr-59 phosphorylation of SREBP-1a plays an important role in cancer cell proliferation. PMID: 29514980
we demonstrated that knockdown of PKM2 can inhibit GC cell proliferation, G1-S phase transition, can, especially, attenuate GC cell migration in vivo and in vitro, per contra, promote the autophagy, which may depend on mediating the PI3K-Akt signaling. PMID: 28588255
PKM1 activated glucose catabolism and stimulated autophagy/mitophagy, favoring malignancy PMID: 29533781
miRNA-139-5p inhibited cell proliferation, migration, and glycolysis in GBC, at least in part, by repressing pyruvate kinase M2 PMID: 30105813
Mammalian target of rapamycin pathway promotes aerobic glycolysis in esophageal squamous cell carcinoma by upregulating pyruvate kinase M2 isoform PMID: 29916308
PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23. PMID: 28067230
proteins such as MMP2 and MMP9 as well as P38 expression were also affected by the PKM2 expression changes. These results proved that PKM2 could be involved in the progression of bladder cancer by mitogen-activated protein kinases signaling pathway. PMID: 30249877
hypoxic stress in the hepatocellular carcinoma (HCC)cells promoted YAP binding to HIF-1a in the nucleus and sustained HIF-1a protein stability to bind to PKM2 gene and directly activates PKM2 transcription to accelerate glycolysis PMID: 30180863
overexpressed PKM2 led to increased CCND1 and decreased CDKN1A expression, whereas underexpressed PKM2 led to decreased CCND1 and increased CDKN1A expression in ovarian cancer cells. PMID: 29752805
Our current study thus unveils a distinct regulatory function of PKM2, providing new options for therapeutic intervention targeting HIV-1-host interactions. PMID: 29607934
PKM2 as a novel target of RUNX1-ETO and is specifically downregulated in RUNX1-ETO positive AML patients, indicating that PKM2 level might have a diagnostic potential in RUNX1-ETO associated AML. PMID: 28092997
High M2-PK expression is associated with pancreatic cancer and peri-ampullary cancer. PMID: 29540198
The activity of PKM2 was indispensable for the development and metastasis of OS. PMID: 29155364
fFndings demonstrate that mDC activation requires an elevated intrinsic PKM2 level and that PKM2 improves the immune status of patients with SAA by enhancing the functions of mDCs and, consequently, CTLs. PMID: 29636835
EGFR activation results in c-Src-mediated Cdc25A phosphorylation at Y59, which interacts with nuclear pyruvate kinase M2 (PKM2). PMID: 27485204
Study demonstrate that PKM2 plays an important role in metabolic activities, as well as in the malignancy of pancreatic ductal adenocarcinoma cells. PMID: 29393401
Suggest a critical role for pyruvate kinase isozyme M2 in mediating the interaction between pancreatic cancer cells and pancreatic stellate cells. PMID: 29619774
Results show that PK2 expression level is regulated by HSP90 in hepatocellular carcinoma (HCC). HSP90 enhances PKM2 stability by inducing the phosphorylation of PKM2 at Thr-328. PMID: 29262861
O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect. PMID: 29229835
Results indicate that PKM2 is positively correlated with Sp1 expression and demonstrate that Sp1 directly regulates its expression in castration-resistant prostate cancer. PMID: 29094170
High PKM2 expression is associated with lung adenocarcinoma. PMID: 28489603
Epigenetic silencing of miR-338 facilitates glioblastoma progression by preventing suppression the PKM2/beta-catenin axis. PMID: 28858851
this study correlates TuM2PK with tumor size, CRP and CA 15-3 in metastatic breast carcinomas. PMID: 28869444
PKM2 modulates the glycolysis and extracellular matrix generation, providing the vital role of PKM2 on osteoarthritis (OA) pathogenesis and a novel therapeutic target for OA. PMID: 29356574
This work suggested that OA increased PKM1/PKM2 ratio, resulting in HNF-4alpha activation and hepatoma differentiation. PMID: 28726775
the present findings enriched our knowledge by demonstrating a significant association of PKM2 and GLS1 with oxaliplatin-resistance in CRC. PMID: 28498807
Elevated expression of PKM2 is a prognostic factor for poor gallbladder cancer (GBC) clinical outcomes, implied involving of PKM2 in GBC progression. PMID: 27283076
PKM2 knockdown resulted in increased p53 expression and prolonged half-life of p53. PKM2 could directly bind with both p53 and MDM2 and promote MDM2-mediated p53 ubiquitination. The dimeric PKM2 significantly suppressed p53 expression compared with the other PKM2 mutants. PMID: 27801666
Inhibition of the mTOR pathway abolished TGF-beta1-induced EMT and reduced mTOR/p70s6k signaling, which downregulated PKM2 expression. PMID: 28446743
Study indicates that nitric oxide induces PKM2 nuclear translocation and promotes glycolysis in ovarian cancer cells. PMID: 28380434
Authors report that AKT directly interacts with PKM2 and phosphorylates it at Ser-202, which is essential for the nuclear translocation of PKM2 protein under stimulation of IGF-1. In the nucleus, PKM2 binds to STAT5A and induces IGF-1-stimulated cyclin D1 expression, suggesting that PKM2 acts as an important factor inducing STAT5A activation under IGF-1 signaling. PMID: 27340866
The results suggested that targeting PKM2 with an oncolytic adenovirus produced a strong antitumor effect. PMID: 28569774
our results demonstrated that miR-let-7a inhibits cell proliferation, migration and invasion by down-regulation of PKM2 in cervical cancer PMID: 28415668
Data show that cytomegalovirus encoded chemokine receptor US28 (US28) signaling in activation of the HIF-1alpha/PKM2 feedforward loop in fibroblasts and glioblastoma cells. PMID: 27602585
High PKM2 expression is associated urothelial tumorigenesis. PMID: 26992222
Report that PKM2 is succinylated at lysine 498 and succinylation increases its activity. SIRT5 binds to, desuccinylates and inhibits PKM2 activity. Increased levels of reactive oxygen species (ROS) decreases succinylation and activity of PKM2 by increasing its binding to SIRT5. PMID: 28036303
over-expression of PKM2 is associated with poor prognosis in most solid cancers and it might be a potentially useful biomarker for predicting cancer prognosis in future clinical applications. PMID: 27911861
Interdependence of GLO I and PKM2 in the Metabolic shift to escape apoptosis in GLO I-dependent cancer cells PMID: 29225125
This study demonstrates that lapachol inhibits glycolysis in cancer cells by targeting PKM2. Unlike the previously reported inhibitor shikonin, lapachol does not target mitochondria in tumor cell growth inhibition. PMID: 29394289
In this study, we indicate that P53 (N340Q/L344R) promotes hepatocarcinogenesis through upregulation of PKM2 PMID: 27167190
These findings indicate that shRNA-mediated silencing of PKM2 gene promotes apoptosis and inhibits aerobic glycolysis, proliferation, migration, and invasion in colorectal cancer cells. PMID: 28543190
Due to achieved results concerning expression of PKM2 there is a lack of evidence for its diagnostic and prognostic usage in ovarian cancer. PMID: 29277786
UCP2 stimulates hnRNPA2/B1, GLUT1 and PKM2 expression and sensitizes pancreatic cancer cells to glycolysis inhibition. PMID: 27989750
These findings uncover a novel mechanism through which mitochondrial PKM2 phosphorylates Bcl2 and inhibits apoptosis directly. PMID: 28035139
These findings suggested that PKM2 and GLS might play important roles in the proliferation of hypoxic gastric cancer cells PMID: 29032577
demonstrated that lincRNA-p21 blunted the prostate cancer cell proliferation and tumorigenic capacity through down-regulation of PKM2 PMID: 28994148
we demonstrated that SHP-1 dephosphorylates PKM2Y105 to inhibit the Warburg effect and nucleus-dependent cell proliferation, and the dephosphorylation of PKM2Y105 by SHP-1 determines the efficacy of targeted drugs for hepatocellular carcinoma treatment PMID: 26959741
The PKM2-shRNA group exhibited reduced PKM2 mRNA and protein expression, whereas p53 and p21 expression was increased compared with the blank and empty plasmid groups. PMID: 28746922
The CARM1-PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis. PMID: 29058718
PKM2 activity is higher in patients with NSCLC than in healthy subjects. The level of PKM2 activity is associated with advanced stage of cancer. PMID: 27683215

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.