Analytical Data
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基因名
SLC30A8
- Application
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别名
ZNT8; Zinc Transporter 8
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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 95% as determined by SDS-PAGE.
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蛋白编号
Q8IWU4
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表达区间
Thr263~Asp369
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分子量
42kDa
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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
SLC30A8, a member of the SLC (solute carrier) family, encodes a zinc transporter predominantly expressed in pancreatic beta cells, where it plays a crucial role in insulin secretion and glucose homeostasis. Genetic studies have identified SLC30A8 as a significant risk factor for type 2 diabetes, with certain polymorphisms associated with increased susceptibility to the disease. The protein facilitates the transport of zinc ions, which are essential for insulin crystallization and storage within secretory granules. Understanding the functional mechanisms of SLC30A8 and its influence on beta-cell function is vital for elucidating the pathophysiology of diabetes. Research has increasingly focused on the recombinant expression of SLC30A8 to explore its structure-function relationships, enabling the investigation of how specific mutations might affect protein activity. Recent advances in techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into its molecular architecture, further guiding therapeutic interventions. By studying the recombinant protein in various cellular contexts, researchers aim to identify potential targets for drug development, paving the way for novel strategies to combat type 2 diabetes.
