Analytical Data
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Gene name
Pkm
- Application
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Alternative Names
Pkm；OIP3；PK2；PK3；Pyruvate kinase PKM
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14618
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Expression Region
185-461aa
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AA Sequence
VKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTAR
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Molecular Weight
57.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Pkm, or pyruvate kinase M, is a crucial enzyme involved in the glycolytic pathway, facilitating the conversion of phosphoenolpyruvate to pyruvate while generating ATP. The study of Pkm has gained significant interest due to its role in cellular metabolism, particularly in cancer biology. Cancer cells often exhibit altered metabolic pathways, favoring aerobic glycolysis, known as the Warburg effect, which allows for rapid growth and proliferation. Pkm exists in two main isoforms, M1 and M2, with M2 being predominantly expressed in tumors. Research has shown that the M2 isoform can promote cancer cell proliferation by influencing metabolic flux and supporting anabolic processes. Moreover, the regulation of Pkm activity is intricately linked with cellular signaling pathways, including those regulated by oncogenes and tumor suppressors. Understanding the structural and functional properties of recombinant Pkm, including its allosteric regulation and interaction with metabolites, is essential for developing targeted therapeutic strategies. Recent advances in recombinant protein technology have enabled the production of active Pkm for biochemical studies, facilitating investigations into its role in cancer metabolism and potential as a therapeutic target. Utilizing recombinant Pkm in research not only enhances our understanding of glycolytic regulation in cancer cells but also opens avenues for novel drug development aimed at reversing the metabolic adaptations of tumors. Overall, the exploration of Pkm provides vital insights into metabolism and its implications in oncogenesis, marking it as a promising candidate for further investigation in cancer therapeutics.
