Analytical Data
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Gene name
PGAM4
- Application
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Alternative Names
PGAM4; PGAM3; Probable phosphoglycerate mutase 4; EC 5.4.2.11; EC 5.4.2.4
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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
Q8N0Y7
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Expression Region
2-254 aa
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AA Sequence
AAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC KAIEAVAAQG KAKK
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Molecular Weight
28.7 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
PGAM4 (phosphoglycerate mutase 4) is a member of the phosphoglycerate mutase family, which plays a crucial role in the glycolytic pathway by catalyzing the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. Research on PGAM4 has gained momentum due to its overexpression in various cancers, suggesting its potential as a biomarker for cancer diagnosis and a therapeutic target. Unlike other phosphoglycerate mutases, PGAM4 is unique in that it is predominantly localized in the nucleus and is involved in not only energy metabolism but also cellular signaling and regulation of gene expression. The exploration of PGAM4 as a recombinant protein enables researchers to study its structure, function, and interactions in detail. Advances in recombinant DNA technology have made it feasible to produce PGAM4 in heterologous systems, allowing for a better understanding of its enzymatic properties and its role in oncogenesis. Investigating PGAM4’s involvement in metabolic reprogramming in cancerous cells might uncover new avenues for targeted therapies aimed at disrupting cancer cell metabolism. As a result, PGAM4 is emerging as a potential target in cancer therapeutics, highlighting the importance of studying this protein to develop innovative strategies for cancer treatment.
