Analytical Data
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Gene name
GLIPR2
- Application
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Alternative Names
GLIPR2;C9orf19;GAPR1;Golgi-associated plant pathogenesis-related Protein 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
Q9H4G4
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Expression Region
1-154aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGKSASKQFHNEVLKAHNEYRQKHGVPPLK LCKNLNREAQQYSEALASTRILKHSPESSRGQCGENLAWASYDQTGKEVA DRWYSEIKNYNFQQPGFTSGTGHFTAMVWKNTKKMGVGKASASDGSSFVV ARYFPAGNVVNEGFFEENVLPPKK
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Molecular Weight
19 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
GLIPR2 (Glioma pathogenesis-related protein 2) is a member of the glioma pathogenesis-related protein family, which has garnered interest due to its potential role in cancer biology, particularly in gliomas and other tumors. Research indicates that GLIPR2 may function as a tumor suppressor, influencing cell proliferation, survival, and apoptosis. Its expression levels are often altered in various cancers, suggesting a correlation with tumor progression and patient prognosis. The study of recombinant GLIPR2 proteins is crucial for understanding its structure-function relationship and elucidating the molecular pathways it may regulate. By engineering and expressing recombinant GLIPR2, researchers can investigate its biological activities, potential interactions with other cellular proteins, and its overall impact on cancer cell behavior. This research not only aims to clarify the exact role of GLIPR2 in tumorigenesis but also explores its potential as a therapeutic target or biomarker in cancer diagnostics and treatment strategies. As the scientific community continues to unravel the complexities of cancer biology, understanding the functional implications of proteins like GLIPR2 will be essential in developing more effective interventions.











