Analytical Data
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基因名
PRR4
- Application
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别名
LPRP; PROL4; Lacrimal proline-rich protein; Nasopharyngeal carcinoma-associated proline-rich protein 4
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种属
Human
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q16378
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表达区间
Gln17~Trp134
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分子量
41kDa
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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
PRR4 (Proline-Rich Protein 4) is a member of the proline-rich protein family, which has garnered attention due to its potential roles in cellular processes, particularly in the context of cancer and inflammation. Research indicates that PRR4 is significantly upregulated in various types of cancers, suggesting a potential link between its expression and tumor progression. Understanding the molecular mechanisms underlying PRR4's function can provide insights into its role in the tumor microenvironment and cell signaling pathways. Moreover, PRR4 is thought to play a role in modulating immune responses, reinforcing its significance in both oncological and inflammatory diseases. The study of recombinant PRR4 proteins enables researchers to explore their structure-function relationships and interactions with other biomolecules, paving the way for the development of therapeutic strategies targeting PRR4-related pathways. Furthermore, advances in protein engineering techniques offer opportunities to create modified forms of PRR4 that may enhance its therapeutic efficacy or act as biomarkers for disease progression. Overall, PRR4 presents a promising avenue for research focused on understanding complex disease mechanisms and developing novel interventions in the fields of cancer biology and immunology.












