Analytical Data
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基因名
Claudin-1 Protein-VLP
- Application
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别名
CLD1; ILVASC; SEMP1; Senescence-Associated Epithelial Membrane Protein 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- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O95832
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表达区间
Leu50~Arg197
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分子量
46kDa
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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
Claudin-1 is a crucial protein that forms tight junctions in epithelial and endothelial cells, playing a key role in maintaining the integrity of cellular barriers. Its dysregulation has been implicated in various pathological conditions, including cancer progression and inflammatory diseases. The development of Claudin-1 Protein Virus-Like Particles (VLPs) represents a novel approach for both therapeutic and diagnostic applications. By utilizing VLPs to present Claudin-1 in a native conformation, researchers aim to enhance the immune response against tumors that overexpress this protein. Moreover, this technology facilitates the study of Claudin-1's role in cellular processes and its potential as a biomarker for diseases. The ability to generate stable, non-infectious VLPs that mimic the structure of viruses, while displaying the Claudin-1 protein on their surface, provides an innovative platform for vaccine development and targeted drug delivery. Investigations into Claudin-1 VLPs are paving the way for improved strategies in immunotherapy, potentially leading to more effective treatments for cancers and other diseases associated with tight junction dysregulation.
