Analytical Data
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Gene name
lush
- Application
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Alternative Names
lush; Obp76a; Obp76c; CG8807; General odorant-binding protein lush
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Species
Drosophila melanogaster
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O02372
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Expression Region
30-153aa
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Molecular Weight
19.2 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
LUSH (Lysine- and Ubiquitin-Specific protease Homolog) is a crucial protein that has garnered significant attention in recent years due to its role in various biological processes, particularly in cellular signaling and membrane traffic. Understanding LUSH's structure and function is essential, as it is implicated in critical physiological mechanisms, including receptor trafficking and degradation, which are vital for maintaining cellular homeostasis. Research has shown that LUSH operates as a chaperone, assisting in the correct folding and assembly of proteins within the endoplasmic reticulum. Furthermore, aberrations in LUSH function have been linked to several diseases, including neurodegenerative disorders and cancers, making it a potential target for therapeutic intervention. Recent advancements in protein engineering and structural biology have enabled researchers to explore LUSH's conformational dynamics, providing insights into its interaction with other cellular components and elucidating its role in disease mechanisms. This research is paving the way for innovative strategies to manipulate LUSH activity, offering promising avenues for clinical applications and the development of novel treatments.
