Analytical Data
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Gene name
PGAM1
- Application
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Alternative Names
PGAM1;PGAMA;Phosphoglycerate mutase 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
P18669
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Expression Region
1-254aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG KAKK
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Molecular Weight
31 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
PGAM1 (Phosphoglycerate Mutase 1) is a crucial enzyme in the glycolytic pathway, catalyzing the conversion of 3-phosphoglycerate to 2-phosphoglycerate, which is essential for cellular energy production and metabolism. Abnormal expression of PGAM1 has been implicated in various pathological conditions, including cancer, where it has been identified as a potential biomarker and therapeutic target. The study of recombinant PGAM1 protein has gained significance due to its role in understanding the enzyme's biochemical properties, regulatory mechanisms, and its interaction with other metabolic pathways. Researchers are interested in producing recombinant PGAM1 to investigate its structure, function, and the effects of post-translational modifications on enzymatic activity. This knowledge can provide insights into metabolic dysregulation in diseases and advance the development of novel diagnostic and therapeutic strategies. Furthermore, recombinant PGAM1 can serve as a tool for screening small-molecule inhibitors that may have anti-cancer properties, highlighting its importance in both basic research and clinical applications. The growing interest in PGAM1 necessitates robust methods for its expression and purification, which can facilitate further studies and enhance our understanding of its biological significance.
