Analytical Data
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Gene name
PFKM
- Application
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Alternative Names
PFK1; PFKX; Phosphofructokinase 1; Phosphofructo-1-kinase isozyme A; 6-Phosphofructokinase Polypeptide X; Fructose-6-Phosphate 1-Phosphotransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08237
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Expression Region
Thr2-Val780
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Molecular Weight
90kDa
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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
Phosphofructokinase M (PFKM) is a key regulatory enzyme in the glycolytic pathway, responsible for converting fructose-6-phosphate into fructose-1,6-bisphosphate, a critical step in glucose metabolism. The PFKM enzyme is primarily expressed in muscle and brain tissues, playing an essential role in energy production, cellular respiration, and metabolic regulation. Alterations in PFKM activity have been associated with various metabolic disorders, including obesity, diabetes, and certain types of cancers, highlighting its significance in both physiological and pathological contexts. Recent studies have focused on the recombinant expression of PFKM in heterologous systems, enabling researchers to investigate its structure, function, and regulation under different conditions. Such studies aim to provide insights into the enzyme's kinetic properties and its role in metabolic pathways. Additionally, recombinant PFKM can serve as a valuable tool in drug discovery and the development of therapeutic interventions targeting metabolic diseases. Understanding the biochemical properties of this enzyme at the molecular level is crucial for elucidating its role in health and disease, paving the way for novel treatment strategies aimed at modulating glycolytic flux and energy metabolism in affected tissues.
