Analytical Data
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基因名
FNBP1
- Application
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别名
FBP17
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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
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96RU3
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表达区间
Ala348~Glu529
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分子量
24.5kDa
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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
FNBP1, or Fast Neural Breast Cancer Protein 1, is a multifunctional protein implicated in various cellular processes, including actin dynamics, endocytosis, and signal transduction. Its role as a crucial regulatory component in cellular morphology and motility makes it a significant focus in cancer research, particularly in understanding breast cancer metastasis. The interest in FNBP1 stems from its association with the progression of tumorigenesis and its potential as a therapeutic target. Studies have shown that FNBP1 influences cellular pathways that promote invasive behavior in cancer cells, highlighting its relevance in the dynamics of cancer biology. Given its involvement in key signaling pathways, researchers are now focused on the structural characterization of FNBP1 through recombinant protein techniques. This approach allows for the analysis of its functional domains and interactions with other cellular proteins, paving the way for the development of novel therapeutic strategies aimed at inhibiting its pro-tumorigenic activities. The advancement in recombinant protein technologies facilitates the production of FNBP1 in sufficient quantities for detailed functional studies, which could lead to a better understanding of its role in cancer and other diseases.
