Analytical Data
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Gene name
PFKP
- Application
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Alternative Names
PFK-C; PFKF; ATP-dependent 6-phosphofructokinase, platelet type; 6-phosphofructokinase type C; Phosphofructo-1-kinase isozyme C; Phosphohexokinase
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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
Q01813
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Expression Region
Asp553~Lys753
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Molecular Weight
26kDa
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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
PFKP, or phosphofructokinase, is a key enzyme in the glycolytic pathway, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a crucial step in cellular energy production. Research into PFKP has gained traction due to its significant role in regulating glucose metabolism and overall cellular energy homeostasis, which are vital processes in various biological systems. Dysregulation of PFKP activity has been implicated in several metabolic disorders, including diabetes and cancer, where altered energy production pathways often contribute to disease progression. Furthermore, PFKP exists in multiple isoforms, with distinct tissue distributions and regulatory mechanisms, leading to an interest in understanding its specific functions and regulatory networks. The study of PFKP recombinant proteins has enabled researchers to investigate the enzyme's structural and kinetic properties, as well as its interaction with various metabolites and regulatory molecules. This advances our understanding of its biological significance and potential as a therapeutic target. Utilizing techniques such as site-directed mutagenesis, crystallography, and kinetic assays, the research aims to elucidate the mechanisms governing PFKP activity and its role in metabolic regulation. Overall, the exploration of PFKP recombinant proteins serves not only to deepen our comprehension of metabolic processes but also to pave the way for novel therapeutic strategies aimed at correcting metabolic dysregulations associated with PFKP.
