Analytical Data
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Gene name
POTEG
- Application
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Alternative Names
A26C2; POTE14; POTE14a; CT104.4; ANKRD26-Like Family C Member 2; Cancer/Testis Antigen Family 104,Member 4; Prostate, ovary, testis-expressed protein on chromosome 14
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Species
Human
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Source
E. coli
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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
Q6S5H5
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Expression Region
Leu177~Asp330
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Molecular Weight
21kDa
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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
POTEG, or the putative oncogene, is a protein that has garnered attention in recent years due to its potential implications in cancer biology and therapeutic interventions. Research surrounding POTEG has been driven by its intriguing association with various malignant processes, notably in the regulation of cellular proliferation, apoptosis, and tumor microenvironment interactions. Initial studies have suggested that POTEG may influence signaling pathways essential for tumor growth, making it a compelling target for drug development. The need for understanding the functional mechanisms of POTEG has intensified, as evidence indicates its aberrant expression in several cancer types, raising questions about its role as a biomarker for diagnosis and prognosis. Recent advancements in recombinant protein technology have enabled the production of POTEG in sufficient quantities for in-depth structural and functional analyses. Such research not only aims to elucidate the biological properties of POTEG but also seeks to explore its interactions with other cellular molecules, paving the way for potential therapeutic strategies that could inhibit its oncogenic activity. As a result, ongoing studies are focusing on characterizing POTEG's precise function and its promise as a novel target in precision medicine, underscoring the urgent need for comprehensive investigations into this protein's potential in combating cancer.
