Analytical Data
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Gene name
GPM1
- Application
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Alternative Names
BPG-dependent PGAM 1 MPGM 1 Phosphoglyceromutase 1
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Species
Saccharomyces cerevisiae
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Source
Yeast
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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
P00950
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Expression Region
2-247aa
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Molecular Weight
29.5 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
GPM1, or phosphoglycerate mutase 1, is a key enzyme in the glycolytic pathway, facilitating the conversion of 3-phosphoglycerate to 2-phosphoglycerate. This enzymatic function is vital for cellular metabolism and energy production, linking glycolysis with other metabolic pathways. Studies have shown that GPM1 plays a crucial role in cancer metabolism, particularly in the Warburg effect, where cancer cells preferentially produce energy through glycolysis, even in the presence of oxygen. The aberrant expression of GPM1 has been associated with various malignancies, suggesting its potential as a therapeutic target. In recent years, the recombinant production of GPM1 has been pursued to understand its structural and functional characteristics, enabling the exploration of its role in metabolic diseases and providing a basis for developing enzyme inhibitors. Advances in recombinant DNA technology have facilitated the expression of GPM1 in heterologous systems, allowing for large-scale production and detailed biochemical analyses. Additionally, studying the post-translational modifications and interactions of GPM1 can shed light on the regulatory mechanisms governing its activity, furthering our understanding of its implications in disease. Overall, research on GPM1 recombinant protein holds significant promise for elucidating its biological roles and developing innovative strategies for cancer therapy and metabolic disease management.
