Analytical Data
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基因名
lush
- Application
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别名
lush; Obp76a; Obp76c; CG8807; General odorant-binding protein lush
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种属
Drosophila melanogaster
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O02372
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表达区间
30-153aa
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分子量
19.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
