Analytical Data
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Gene name
PGAM1
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简介
PGAM1 protein plays a pivotal role in glycolysis by catalyzing the vital interconversion of 2-phosphoglycerate and 3-phosphoglycerate. Additionally, it is instrumental in the conversion of (2R)-2,3-bisphosphoglycerate to (2R)-3-phospho-glyceroyl phosphate, further contributing to the intricate metabolic processes associated with glycolytic pathways. PGAM1 Protein, Human is the recombinant human-derived PGAM1 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
PGAM1; Phosphoglycerate mutase 1; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; PGAM-B
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18669
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Expression Region
M1-K254
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Protein Length
Full Length
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Molecular Weight
28.9 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
PGAM1 (Phosphoglycerate Mutase 1) is an essential enzyme in the glycolytic pathway, responsible for catalyzing the conversion of 3-phosphoglycerate to 2-phosphoglycerate. Its role in energy metabolism makes it crucial for cellular functions, and aberrations in its activity have been linked to various diseases, including cancer. In recent years, researchers have focused on the potential of PGAM1 as a therapeutic target, given its involvement in the metabolic reprogramming of cancer cells. Moreover, PGAM1 has been implicated in the regulation of cellular signaling pathways, making it a vital protein for understanding tumor biology. The production and characterization of recombinant PGAM1 protein have become pivotal for studying its structure, function, and interactions with other biomolecules. By utilizing recombinant DNA technology, scientists can generate PGAM1 in various systems, allowing for detailed biochemical analyses and the exploration of its potential as a drug target. The study of PGAM1 and its recombinant forms not only enhances our understanding of metabolic regulation but also opens avenues for the development of novel therapeutic strategies aimed at targeting metabolic pathways dysregulated in cancer and other diseases. Overall, research into PGAM1 holds significant promise for advancing our knowledge of metabolic diseases and improving treatment options.
