Analytical Data
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Gene name
PGK1
- Application
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Alternative Names
PGK1;PGKA;Phosphoglycerate kinase 1
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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
P00558
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Expression Region
1-417aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSLSNKLTLDKLDVKGKRVVMRVDFNVPMK NNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEP VAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEG KGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVN LPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDK VNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKI TLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTR AKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCC AKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI
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Molecular Weight
47 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
PGK1, or Phosphoglycerate Kinase 1, plays a crucial role in the glycolytic pathway, catalyzing the conversion of 1,3-bisphosphoglycerate to 3-phosphoglycerate while transferring a phosphate group to ADP to form ATP. This enzyme is not only vital for energy metabolism but also serves as a key regulator of various cellular processes, including cell proliferation and apoptosis. Dysregulation of PGK1 has been implicated in various diseases, particularly cancer, where it exhibits aberrant expression patterns, contributing to the metabolic reprogramming typical of tumor cells. Research on recombinant PGK1 has advanced significantly, as scientists seek to obtain large quantities of the protein for structural and functional studies, aiming to elucidate its mechanism of action and potential as a therapeutic target. The development of recombinant PGK1 involves the use of various expression systems, such as bacterial or yeast platforms, allowing for the generation of active, purified protein suitable for in vitro assays and potential therapeutic applications. Understanding the biochemical properties and interactions of PGK1 in disease states can lead to novel insights into metabolic pathways and contribute to the development of targeted treatments, underscoring the importance of PGK1 in both fundamental research and clinical contexts.
