Analytical Data
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Gene name
PKM2
- Application
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Alternative Names
Pyruvate kinase muscle isozyme Pkm2, Pykm
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Species
Rat
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11980
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Expression Region
1-531aa
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Molecular Weight
62.8 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
Related Products
Protein Description
Pyruvate kinase M2 (PKM2) is a crucial enzyme involved in cellular metabolism and energy production, primarily functioning as a regulator of glycolysis. This enzyme has garnered significant attention in cancer research due to its unique role in the Warburg effect, where cancer cells preferentially metabolize glucose to lactate even in the presence of oxygen, leading to enhanced biosynthesis and tumor growth. Unlike its M1 isoform, PKM2 can exist in both active and inactive states, allowing it to play a vital role in various signaling pathways and gene expression regulation. The study of recombinant PKM2 proteins is pivotal for understanding its structural and functional properties, as well as its regulatory mechanisms. Researchers aim to elucidate the enzyme's roles in metabolic reprogramming in cancer and other diseases, exploring its potential as a therapeutic target. Advances in recombinant protein technology have enabled the production of PKM2 variants, facilitating biochemical assays and structural analyses, which are essential for drug design and the development of PKM2 inhibitors. Consequently, the investigation of PKM2 not only enhances our comprehension of cellular metabolism but also opens avenues for novel cancer therapies, making it a focal point in contemporary biomedical research.
