Analytical Data
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基因名
DLGAP5
- Application
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别名
(DAP-5)(Discs large homolog 7)(Disks large-associated protein DLG7)(Hepatoma up-regulated protein)(HURP)
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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
Q15398
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表达区间
1-846aa
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分子量
121.8 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
DLGAP5, a member of the Discs Large (DLG) protein family, plays a crucial role in synaptic signaling and neuronal development. Recent studies have highlighted its importance in various neurological disorders and its potential as a biomarker for certain cancers, particularly gliomas. The protein is involved in the regulation of cell adhesion, signaling pathways, and the organization of the cytoskeleton, making it a significant focus in understanding cellular communication processes. Research into DLGAP5 recombinant proteins aims to elucidate its precise biological functions and interactions at the molecular level. By generating recombinant DLGAP5, scientists can investigate its role in synaptic stability and plasticity, as well as its involvement in tumorigenesis. The ability to produce and purify this protein in a controlled environment allows for more detailed biochemical assays, structural studies, and the exploration of its potential therapeutic applications. Furthermore, as DLGAP5's interaction with other proteins is crucial for its function, studying these interactions through recombinant methods can provide valuable insights into the underlying mechanisms of neurotransmission and cellular behavior in health and disease. Overall, the exploration of DLGAP5 recombinant protein is vital for advancing our understanding of its role in neurobiology and cancer research, paving the way for innovative diagnostic and therapeutic strategies.
