Analytical Data
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Gene name
DLEU2
- Application
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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
O43262
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Expression Region
1-84aa
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AA Sequence
MRLRFNNDRMKTTIKETTILSSAILTFLTYLMKMSFERCTARNKMFVNSPFYPRVDNYCTSSWKKFYLKCYFSLNTIKKEKKMT
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Molecular Weight
36.6 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
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Protein Description
DLEU2, a long non-coding RNA (lncRNA), has garnered significant attention in recent years due to its potential involvement in various biological processes and diseases, particularly in cancer progression. Located at chromosome 13q14, DLEU2 plays a critical role in regulating gene expression and has been implicated in cellular pathways associated with tumorigenesis and metastasis. Studies suggest that DLEU2 may act as a tumor suppressor, influencing cell proliferation, apoptosis, and migration in various cancers, including chronic lymphocytic leukemia (CLL). The reprogramming of DLEU2 expression in malignancies highlights its potential as a biomarker for diagnosis and prognosis, as well as a promising target for therapeutic interventions. Recent advances in recombinant protein technology have facilitated the production and characterization of DLEU2 protein, providing insights into its molecular mechanisms. Understanding the structure-function relationships of DLEU2 and its interactions with other cellular components can pave the way for novel cancer treatment strategies and improve our comprehension of lncRNA biology. This growing body of research underscores the importance of DLEU2 in cancer research and its potential implications in therapeutic development.
