Analytical Data
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基因名
LYAR
- Application
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别名
Cell growth regulating nucleolar protein; Cell growth-regulating nucleolar protein; Likely ortholog of mouse Ly1 reactive clone ; Ly1 reactive; Ly1 reactive homolog (mouse) ; Ly1 reactive homolog; LYAR; LYAR_HUMAN; ZC2HC2; ZLYAR
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种属
Human
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表达系统
Yeast
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NX58
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表达区间
1-379aa
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分子量
45.6 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
LYAR (Lysine-rich nucleolar protein) is a highly conserved protein that plays a significant role in ribosome biogenesis and cellular stress responses. The research into LYAR has intensified due to its involvement in critical cellular processes, including gene regulation, cell proliferation, and apoptosis. Notably, LYAR is implicated in various diseases, particularly cancer, where its expression levels are often altered, suggesting a potential role in tumorigenesis and a possible target for therapeutic interventions. Studies have shown that LYAR interacts with various nucleolar and chromatin-associated proteins, influencing RNA synthesis and ribosome assembly. Additionally, its lysine-rich domain allows for post-translational modifications, which can modulate its function and stability. Understanding the molecular mechanisms governing LYAR's action may pave the way for novel cancer treatments and improve our overall knowledge of nucleolar dynamics. The ongoing research aims to unravel LYAR's exact roles in these cellular processes, the regulation of its expression, and the implications of its dysregulation in disease contexts. Overall, LYAR represents an intriguing subject in molecular biology with potential applications in therapeutic strategies against various pathologies.
