Analytical Data
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基因名
Intrinsic Factor/GIF
- Application
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别名
TCN3; IF; IFMH; INF; Transcobalamin III; Vitamin B Synthesis
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P52787
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表达区间
Asp31~Cys288
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分子量
32kDa
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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
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.
