Analytical Data
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Gene name
YPEL2
- Application
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Alternative Names
YPEL2; FKSG4; Protein yippee-like 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96QA6
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Expression Region
1-119 aa
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AA Sequence
MVKMTRSKTFQAYLPSCHRTYSCIHCRAHLANHDELISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIYCENCKTTLGWKYEHAFESSQKYKEGKYIIELAHMIKDNGWD
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Molecular Weight
13.1 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
YPEL2, a member of the YPEL family of proteins, has garnered significant attention in recent years due to its involvement in various cellular processes and potential implications in human health and disease. Initially identified through genomic studies, YPEL2 has been linked to roles in cell proliferation, apoptosis, and differentiation. Research has indicated that it may act as a regulator of the cell cycle and is implicated in the modulation of oncogenic pathways, suggesting its potential as a tumor suppressor or promoter. Recent advances in molecular biology techniques have allowed for a more detailed characterization of YPEL2, revealing its interactions with multiple signaling pathways and cellular structures. Moreover, studies have highlighted its expression levels in various cancers, which further piques interest in its function and therapeutic potential. Understanding the structure and function of YPEL2 at a molecular level can provide insights into its biological roles and its contribution to disease mechanisms, paving the way for novel approaches in cancer treatment and other diseases where YPEL2 is implicated. Thus, ongoing research into YPEL2 aims to elucidate its precise functions and regulatory mechanisms, potentially positioning it as a biomarker or target for therapeutic strategies in oncology and other medical fields.
