Analytical Data
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Gene name
Transferrin
- Application
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Alternative Names
TRF; Siderophilin; Serotransferrin; Beta-1 metal-binding globulin
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Species
Dog
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02787
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Expression Region
Val26~Glu350
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Molecular Weight
56kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
