Analytical Data
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基因名
Serotransferrin
- Application
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别名
Serotransferrin；Serotransferrin
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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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
20-698aa
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氨基酸序列
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
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分子量
75.2 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
Serotransferrin, also known as transferrin, is a crucial iron-binding glycoprotein that plays a vital role in iron metabolism and homeostasis in humans. It is primarily synthesized in the liver and functions to transport iron from absorption sites in the intestine and storage sites in the liver and spleen to various tissues, where it is utilized for essential biological processes such as hemoglobin synthesis and cellular respiration. The study of recombinant serotransferrin has gained prominence due to its potential applications in medicine and biotechnology, particularly in the development of therapeutic agents for iron deficiency disorders and anemia, as well as in drug delivery systems. The recombinant production of serotransferrin allows for the generation of high-purity protein with well-defined properties, facilitating detailed investigations into its structure-function relationships. Moreover, insights into its interaction with receptors and iron metabolism can aid in the design of novel treatments targeting iron-related diseases. Recent advances in genetic engineering and expression systems, including bacteria, yeast, and mammalian cells, have improved the efficiency of recombinant serotransferrin production, providing researchers with valuable tools to explore its biological functions and optimize its therapeutic potential. Understanding the molecular mechanisms underlying serotransferrin's role in iron transport and metabolism is critical not only for basic science but also for developing innovative strategies to address global health challenges associated with iron deficiency and overload conditions.
