Analytical Data
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Gene name
PGAM2
- Application
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Alternative Names
PGAM2;PGAMM;Phosphoglycerate mutase 2
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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
P15259
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Expression Region
1-253aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK
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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
PGAM2 (phosphoglycerate mutase 2) is a crucial enzyme involved in the glycolytic pathway, facilitating the conversion of 2-phosphoglycerate to 3-phosphoglycerate. Research into PGAM2 has gained interest due to its significant role in cellular metabolism, particularly in cancer biology, where altered glycolytic flux is a hallmark of many tumors. In addition, PGAM2 has been linked to genetic disorders, such as myopathy and encephalopathy, highlighting its importance in human health. The study of PGAM2 recombinant protein aims to elucidate its enzymatic mechanisms and regulatory pathways, providing insights into metabolic dysfunctions associated with various diseases. Understanding the structure-function relationships of PGAM2 through recombinant technology can facilitate the development of targeted therapeutics, offering potential strategies for metabolic disorders and cancer treatment. Moreover, the ability to produce PGAM2 in a controlled environment allows for detailed biochemical characterization, paving the way for innovative approaches to manipulate its activity in a therapeutic context. As the scientific community continues to explore the multifaceted roles of PGAM2, its recombinant protein serves as a valuable tool for advancing knowledge in metabolic research and therapeutic development.
