Analytical Data
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基因名
Transferrin
- Application
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别名
TRF; Siderophilin; Serotransferrin; Beta-1 metal-binding globulin
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种属
Dog
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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
P02787
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表达区间
Val26~Glu350
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分子量
56kDa
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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
Transferrin is a glycoprotein that plays a critical role in iron transport and homeostasis in the human body. It binds iron ions in the bloodstream and facilitates their delivery to various tissues, which is essential for numerous biological processes, including erythropoiesis and cellular metabolism. Given the importance of transferrin in iron regulation, recombinant transferrin proteins have emerged as a subject of intense research. Scientists aim to produce these proteins using recombinant DNA technology, allowing for precise control over their structure and function. This production not only provides insights into the protein’s biochemical properties but also facilitates the development of potential therapeutic applications, such as targeted drug delivery systems and iron deficiency treatments. Moreover, understanding the molecular mechanisms of transferrin could lead to breakthroughs in addressing disorders related to iron overload or deficiency, which are prevalent globally. The ability to engineer transferrin variants with altered affinity for iron or enhanced stability opens up avenues for innovative treatments and biotechnological applications, making it a focal point in both basic and applied research.
