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First, the gene fragment coding for the 2-531aa of human PKM is cloned into a vector. The N-terminal 6xHis-tag gene is also inserted into the vector. Secondly, the recombinant vector is selected and then transfected into the E.coli. Finally, the E.coli cells are cultured to induce the protein expression. The recombinant human PKM protein is isolated from the cell lysate and purified through affinity chromatography. Its purity is up to 85% as measured by SDS-PAGE. Human PKM is a crucial enzyme in the glycolytic pathway, primarily responsible for catalyzing the conversion of phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP) into pyruvate and adenosine triphosphate (ATP) [1][2]. PKM exists in two major isoforms: PKM1 and PKM2. PKM1 is predominantly expressed in adult muscle and brain tissues, while PKM2 is found in embryonic cells, stem cells, and various tumor cells, reflecting its role in normal and pathological cellular proliferation [2][3]. PKM2's involvement in tumorigenesis is underscored by its expression patterns in various cancers. High levels of PKM2 are often associated with poor prognosis, as they facilitate the metabolic adaptations necessary for rapid cell division and growth in tumors [4]. It also participates in non-metabolic functions, such as regulating cell cycle progression and influencing gene expression through interactions with various signaling pathways [5]. References:[1] W. Luo and G. Semenza, Emerging roles of pkm2 in cell metabolism and cancer progression, Trends in Endocrinology and Metabolism, vol. 23, no. 11, p. 560-566, 2012. https://doi.org/10.1016/j.tem.2012.06.010[2] J. Deng, S. Lu, H. Liu, B. Liu, C. Jiang, Q. Xuet al., Homocysteine activates b cells via regulating pkm2-dependent metabolic reprogramming, The Journal of Immunology, vol. 198, no. 1, p. 170-183, 2017. https://doi.org/10.4049/jimmunol.1600613[3] M. Chen, J. Zhang, & J. Manley, Turning on a fuel switch of cancer: hnrnp proteins regulate alternative splicing of pyruvate kinase mrna, Cancer Research, vol. 70, no. 22, p. 8977-8980, 2010. https://doi.org/10.1158/0008-5472.can-10-2513[4] D. Lu, W. Lv, W. Li, & Y. Gao, High pkm2 expression is independently correlated with decreased overall survival in hepatocellular carcinoma, Oncology Letters, 2018. https://doi.org/10.3892/ol.2018.9100[5] Z. Lu, Nonmetabolic functions of pyruvate kinase isoform m2 in controlling cell cycle progression and tumorigenesis, Chinese Journal of Cancer, vol. 32, no. 5, p. 5-7, 2013. https://doi.org/10.5732/cjc.011.10446
First, the gene fragment coding for the 2-531aa of human PKM is cloned into a vector. The N-terminal 6xHis-tag gene is also inserted into the vector. Secondly, the recombinant vector is selected and then transfected into the E.coli. Finally, the E.coli cells are cultured to induce the protein expression. The recombinant human PKM protein is isolated from the cell lysate and purified through affinity chromatography. Its purity is up to 85% as measured by SDS-PAGE.
Human PKM is a crucial enzyme in the glycolytic pathway, primarily responsible for catalyzing the conversion of phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP) into pyruvate and adenosine triphosphate (ATP) [1][2]. PKM exists in two major isoforms: PKM1 and PKM2. PKM1 is predominantly expressed in adult muscle and brain tissues, while PKM2 is found in embryonic cells, stem cells, and various tumor cells, reflecting its role in normal and pathological cellular proliferation [2][3].
PKM2’s involvement in tumorigenesis is underscored by its expression patterns in various cancers. High levels of PKM2 are often associated with poor prognosis, as they facilitate the metabolic adaptations necessary for rapid cell division and growth in tumors [4]. It also participates in non-metabolic functions, such as regulating cell cycle progression and influencing gene expression through interactions with various signaling pathways [5].
References:[1] W. Luo and G. Semenza, Emerging roles of pkm2 in cell metabolism and cancer progression, Trends in Endocrinology and Metabolism, vol. 23, no. 11, p. 560-566, 2012. https://doi.org/10.1016/j.tem.2012.06.010[2] J. Deng, S. Lu, H. Liu, B. Liu, C. Jiang, Q. Xuet al., Homocysteine activates b cells via regulating pkm2-dependent metabolic reprogramming, The Journal of Immunology, vol. 198, no. 1, p. 170-183, 2017. https://doi.org/10.4049/jimmunol.1600613[3] M. Chen, J. Zhang, & J. Manley, Turning on a fuel switch of cancer: hnrnp proteins regulate alternative splicing of pyruvate kinase mrna, Cancer Research, vol. 70, no. 22, p. 8977-8980, 2010. https://doi.org/10.1158/0008-5472.can-10-2513[4] D. Lu, W. Lv, W. Li, & Y. Gao, High pkm2 expression is independently correlated with decreased overall survival in hepatocellular carcinoma, Oncology Letters, 2018. https://doi.org/10.3892/ol.2018.9100[5] Z. Lu, Nonmetabolic functions of pyruvate kinase isoform m2 in controlling cell cycle progression and tumorigenesis, Chinese Journal of Cancer, vol. 32, no. 5, p. 5-7, 2013. https://doi.org/10.5732/cjc.011.10446
| Cat.No | ACP09236 | Target Name | PKM |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 2-531aa | Mol Weight | 61.8 kDa |
| Protein Length | Full Length of Mature Protein | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P14618 |
|---|
Uniprot Id
P14618
Target Species
Human
Target Name
PKM
Target Full Name
Pyruvate kinase PKM
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.
Target Subcellular Location
Cytoplasm. Nucleus.
Target Protein Families
Pyruvate kinase family
Target Tissue Specificity
Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.
Target Research Area
Signal Transduction
Target Synonyms
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
Target Background
This gene encodes 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. This protein has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. This protein 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.
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