Analytical Data
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Gene name
Alpha-Fetoprotein
- Application
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Alternative Names
aFP; A-FP; FETA; HPAFP; Alpha-Fetoglobulin; Alpha-1-fetoprotein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P02771
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Expression Region
Ile31~Pro171
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Molecular Weight
18kDa
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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
Alpha-fetoprotein (AFP) is a glycoprotein produced predominantly in the fetal liver, yolk sac, and gastrointestinal tract. It serves various biological functions, including acting as a transport protein for fatty acids and playing a role in immune modulation. Beyond its physiological roles in development, AFP levels are also clinically significant, as they are used as a tumor marker, particularly in hepatocellular carcinoma (HCC) and germ cell tumors. Research has increasingly focused on the recombinant production of AFP, driven by the need for standardized quantities of the protein for diagnostics and therapeutic applications. The development of recombinant AFP not only facilitates improved understanding of its structure-function relationships but also aids in the creation of novel cancer immunotherapies and vaccine formulations. Moreover, the ability to engineer AFP allows scientists to explore its potential role in drug delivery systems and peptide-based imaging agents. Achieving high-yield expression systems, coupled with effective purification methods, remains a critical area of study to ensure the availability of this biomarker for clinical and research purposes. Thus, the investigation into the recombinant production of AFP embodies a multidisciplinary approach, bridging molecular biology, biochemistry, and clinical applications, emphasizing its significance in advancing cancer research and improving patient outcomes.
