Analytical Data
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基因名
CNPY2
- Application
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别名
ZSIG9; Cnpy2; MSAP; TMEM4; Transmembrane Protein 4; MIR-interacting saposin-like protein; Putative secreted protein Zsig9
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
Q9QXT0
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表达区间
Arg21~Leu182
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分子量
22kDa
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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
CNPY2, a member of the CNPY (Cyanobacterial Osmostress Protein Y) family, has gained attention in recent years due to its emerging role in various biological processes and potential implications in human health. Originally identified in plants, CNPY proteins are believed to be involved in stress response mechanisms, particularly under osmotic stress conditions. However, research has expanded into mammalian systems, where CNPY2 has been implicated in cellular proliferation, differentiation, and maintaining homeostasis. Abnormal expression of CNPY2 has been linked to several pathological conditions, including cancer and metabolic disorders, prompting investigations into its functions at the molecular level. Structural studies of recombinant CNPY2 protein have aimed to elucidate its conformation and interactions with other cellular molecules, providing insights into its functional roles and potential therapeutic applications. As such, the exploration of CNPY2 as a recombinant protein not only enhances our understanding of its biological function but also underscores its potential as a target for innovative treatment strategies in diseases associated with dysregulated signaling pathways.
