Analytical Data
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基因名
Transferrin
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简介
Transferrin proteins, iron-binding transporters, bind two Fe(3+) ions and an anion, usually bicarbonate. They transport iron from absorption and heme degradation sites to storage and utilization locations. Serum transferrin may impact cell proliferation. In microbial infection, Neisseria species utilize transferrin as an iron source, capturing and extracting iron for their metabolic needs. Transferrin Protein, Human (HEK293, His) is the recombinant human-derived Transferrin protein, expressed by HEK293 , with C-His labeled tag.
- Application
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生物活性
1.Measured by its binding ability in a functional ELISA. Immobilized Human Transferrin at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R. The ED50 for this effect is 10.21 ng/mL. 2. Measured in a cell proliferation assay using HepG2 Human Hepatocellular Carcinoma Cells. The ED50 for this effect is 21.49 μg/mL, corresponding to a spec ific activity is 46.533 U/mg. 3.Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. The ED50 for this effect is 0.1817 μg/mL, corresponding to a specific activity is 5503.58 units/mg. Measured by its binding ability in a functional ELISA. Immobilized Human Transferrin at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R,The ED50 for this effect is 10.21 ng/mL
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别名
Serotransferrin; Transferrin; Beta-1 metal-binding globulin; Siderophilin; TF; TRF
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种属
Human
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表达系统
HEK293
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标签
C-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P02787/AAA61140.1
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表达区间
V20-P698
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氨基酸序列
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
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蛋白长度
Full Length of Mature Protein
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分子量
68-87 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
Transferrin is a key glycoprotein involved in iron transport and homeostasis in the human body. It plays a critical role in cellular iron uptake by binding ferric iron (Fe^3+) and facilitating its delivery to various tissues through receptor-mediated endocytosis. The study of recombinant transferrin has gained significant attention in recent years due to its potential applications in medicine and biotechnology. Recombinant technology allows for the production of modified versions of transferrin that may enhance its iron-binding capacity, stability, and specificity. These engineered proteins can be explored for therapeutic uses, such as in the treatment of iron deficiency anemia or as carriers for targeted drug delivery—leveraging the natural uptake mechanisms of transferrin to target specific cells, thereby improving treatment efficacy and reducing side effects. Furthermore, understanding the structure-function relationship of transferrin through recombinant studies can provide insights into the mechanisms of iron metabolism and its dysregulation in various diseases, including cancer and neurodegenerative disorders. Overall, the research on recombinant transferrin not only contributes to our fundamental understanding of iron biology but also holds promise for innovative therapeutic strategies.
