Analytical Data
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Gene name
AFP
- Application
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Alternative Names
AFP；HPAFP；Alpha-fetoProtein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02771
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Expression Region
1-198aa
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AA Sequence
MTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVK DALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSE EGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIAR RHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESS GGSNIEF AAQIRSQVMTHLRVIYER
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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
The study of AFP (Alpha-Fetoprotein) recombinant proteins has gained significant importance in biomedical research due to their potential applications in diagnostics and therapeutics. AFP is a glycoprotein produced primarily by the fetal liver, with key roles in fetal development. Its levels are elevated in certain conditions, including hepatocellular carcinoma and germ cell tumors, making it a valuable biomarker for cancer diagnosis and monitoring. Research has focused on the recombinant production of AFP to ensure a reliable supply of the protein for further studies, including the investigation of its roles in tumorigenesis and immune modulation. Advances in synthetic biology and genetic engineering have enabled scientists to produce AFP in various expression systems, facilitating the study of its structure-function relationships and the development of AFP-based cancer vaccines or targeted therapies. Additionally, the expression and purification of recombinant AFP allow for enhanced understanding of its interactions with other cellular components, paving the way for novel diagnostic tools and therapeutic strategies in oncology. Overall, the investigation of AFP recombinant proteins represents a critical intersection of cancer biology and therapeutic innovation, driving forward the development of more effective diagnostic and treatment options for AFP-related diseases.
