Analytical Data
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基因名
Kallikrein-8
- Application
-
别名
Neuropsin
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种属
Mouse
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表达系统
Yeast
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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
Q61955
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表达区间
33-260aa
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分子量
27.1 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
Kallikrein-8 (KLK8), a member of the kallikrein family of serine proteases, has garnered significant attention due to its potential roles in various biological processes and diseases. Initially identified in the brain, KLK8 is involved in neurodevelopment and is implicated in the modulation of neurogenic and inflammatory pathways. Its dysregulation has been linked to neurological disorders, including Alzheimer's disease, where KLK8 may influence amyloid precursor protein processing and tau pathology. Furthermore, KLK8 has been suggested as a biomarker for certain malignancies, notably in breast cancer, where its expression levels may correlate with tumor aggressiveness and patient prognosis. The recombinant production of KLK8 allows for detailed biochemical characterization, functional assays, and investigations into its substrate specificity, thereby elucidating its physiological functions and potential therapeutic applications. Advances in recombinant DNA technology have facilitated the expression and purification of KLK8, enabling researchers to study its enzymatic properties and interactions within various biological contexts. Understanding KLK8's mechanisms of action could pave the way for novel diagnostic and therapeutic strategies targeting a range of diseases associated with its aberrant activity, underscoring the importance of this protease in both basic science and clinical applications.












