Analytical Data
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Gene name
YPEL3
- Application
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Alternative Names
Protein yippee-like 3; Small ubiquitinated apoptotic protein; Yippee like 3; Yippee-like 3 (Drosophila); Ypel3; YPEL3_HUMAN
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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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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 (YDR536C) is a member of the YPEL family of proteins, which are characterized by their role in various cellular processes, including cell proliferation, differentiation, and apoptosis. Research has shown that YPEL3 is involved in significant biological pathways, potentially influencing tumorigenesis and cell signaling. Its expression has been linked to several cancers, making it a target of interest for cancer research. Investigating the structural and functional properties of YPEL3, particularly its reorganization into recombinant forms, provides insights into its mechanism of action and interactions within the cell. Recombinant protein studies allow for the analysis of YPEL3’s biochemical properties, potential regulatory roles, and interactions with other proteins. By expressing YPEL3 in heterologous systems, researchers can obtain sufficient quantities for detailed studies, including crystallography and functional assays, further elucidating its role in disease contexts. The understanding of YPEL3’s structure and function could lead to novel therapeutic strategies targeting its pathways, especially in cancer treatment. Thus, the research surrounding the recombinant expression of YPEL3 is crucial for uncovering its biological significance and potential as a biomarker or therapeutic target.
