Analytical Data
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Gene name
POTEG
- Application
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Alternative Names
POTEG;A26C2;POTE14;POTE ankyrin domain family member G
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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
Q6S5H5
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Expression Region
1-508aa
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AA Sequence
MVAEAGSMPA ASSVKKPFGL RSKMGKWCRH CFPWCRGSGK SNVGTSGDHD DSAMKTLRSK MGKWCRHCFP WCRGSSKSNV GTSGDHDDSA MKTLRSKMGK WCCHCFPCCR GSGKSKVGPW GDYDDSAFME PRYHVRREDL DKLHRAAWWG KVPRKDLIVM LKDTDMNKKD KQKRTALHLA SANGNSEVVK LLLDRRCQLN ILDNKKRTAL TKAVQCREDE CALMLLEHGT DPNIPDEYGN TALHYAIYNE DKLMAKALLL YGADIESKNK HGLTPLLLGV HEQKQQVVKF LIKKKANLNA LDRYGRTALI LAVCCGSASI VSLLLEQNID VSSQDLSGQT AREYAVSSHH NVICQLLSDY KEKQMLKVSS ENSNPEQDLK LTSEEESQRL KGSENSQPEE MSQEPEINKG GDRKVEEEMK KHGSTHMGFP ENLPNGATAD NGDDGLIPPR KSRTPESQQF PDTENEQYHS DEQNDTQKQL SEEQNTGILQ DEILIHEEKQ IEVAENEF
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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 Proline-rich Oligopeptide, has emerged as a significant focus in the field of protein research due to its potential applications in various biological and medical contexts. This protein is characterized by a unique structural motif that enhances its interaction with cellular receptors and other biomolecules, which is critical for its biological functions. Research on POTEG has been spurred by its possible role in modulating cellular processes, including signaling pathways and immune responses. Additionally, the interest in recombinant POTEG protein production has increased as scientists seek to explore its therapeutic potential, particularly in the context of drug development and biotechnology. Through various recombinant DNA techniques, researchers aim to produce POTEG in sufficient quantities to study its structure-function relationships and to investigate its efficacy in treating diseases. Understanding the mechanisms by which POTEG operates can provide insights into its potential roles in health and disease, making it a valuable target for future research and development in the fields of molecular biology and pharmacology.











