Analytical Data
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基因名
TPD52L1
- Application
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别名
Tumor protein D52-like 1
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q16890
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表达区间
1-144aa
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分子量
49.4 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
TPD52L1 (Tumor Protein D52-Like 1) is a member of the D52 family of proteins, which are implicated in various cellular processes, including cell proliferation, apoptosis, and tumorigenesis. Research has shown that TPD52L1 is overexpressed in several types of cancers, suggesting its potential role as an oncogene and a biomarker for tumor progression. Understanding the molecular mechanisms by which TPD52L1 contributes to cancer biology is crucial for developing targeted therapies. Recent studies have focused on elucidating its structural characteristics and functional interactions at the cellular level, particularly in the context of signaling pathways that regulate cell growth and survival. The recombinant expression of TPD52L1 enables researchers to obtain the protein in sufficient quantities for biochemical assays and structural studies, facilitating the exploration of its potential as a therapeutic target. Additionally, examining TPD52L1's interactions with other oncogenic proteins may provide insights into its role in cancer metastasis and resistance to conventional treatments. Overall, the investigation of TPD52L1 represents a promising area of research in understanding cancer biology and developing novel interventions.
