Analytical Data
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Gene name
YPEL3
- Application
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Alternative Names
YPEL3；Protein yippee-like 3
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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
P61236
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Expression Region
1-119aa
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AA Sequence
MVRISKPKTFQAYLDDCHRRYSCAHCRAHLANHDDLISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIHCENCKTTLGWKYEQAFESSQKYKEGKYIIELNHMIKDNGWD
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Molecular Weight
29.6 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
YPEL3 (Yip1 domain family member 3) is a member of the Yipel protein family, which is known for its involvement in various cellular processes, including cell proliferation, differentiation, and apoptosis. Recent studies have suggested that YPEL3 plays a significant role in tumor biology, where it may act as a tumor suppressor. Alterations in YPEL3 expression have been observed in various cancers, indicating its potential as a biomarker for cancer diagnosis and prognostication. The protein's structure features a Yip1 domain, which is implicated in membrane trafficking, hinting at its possible role in cellular signaling pathways. Given its importance in cellular functions and disease progression, researchers are keen to explore the biochemical properties and interactions of YPEL3 through recombinant protein technology. This approach enables the production of purified YPEL3 protein to facilitate in-depth studies on its molecular mechanisms, functional assays, and potential therapeutic applications. Understanding the background of YPEL3 and elucidating its roles through recombinant studies could contribute to advancing cancer therapies and improving patient outcomes.
