Analytical Data
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Gene name
Intrinsic Factor/GIF
- Application
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Alternative Names
TCN3; IF; IFMH; INF; Transcobalamin III; Vitamin B Synthesis
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Species
Rat
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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
P17267
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Expression Region
Arg196~Phe414
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Molecular Weight
28kDa
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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
Intrinsic Factor (IF), also known as Gastric Intrinsic Factor (GIF), is a glycoprotein produced by parietal cells in the stomach, essential for the absorption of vitamin B12 in the intestines. Its primary role is to bind vitamin B12, protecting it from degradation in the gastrointestinal tract and facilitating its transport across the intestinal barrier. Deficiencies in Intrinsic Factor can lead to malabsorption of vitamin B12, resulting in pernicious anemia, neuropathy, and other serious health issues. Given the critical role of IF in human health, researchers have increasingly focused on the structural and functional characterization of IF to understand its mechanism of action and potential therapeutic applications. Transgenic techniques have enabled the production of recombinant forms of Intrinsic Factor, facilitating studies on its interactions with vitamin B12 and its receptor, as well as its implications in clinical settings. Furthermore, advancements in protein engineering have opened avenues for optimizing the stability and efficacy of recombinant Intrinsic Factor, potentially leading to novel treatments for vitamin B12 deficiency and related disorders. Understanding the molecular structure and function of Intrinsic Factor is crucial for developing innovative strategies to combat nutritional deficiencies and improve patient outcomes in clinical therapies.
