Analytical Data
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基因名
Igfl
- Application
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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-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6B9Z0
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表达区间
25-140aa
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分子量
26.1 kDa
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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
IgFL (Immunoglobulin-like fold protein) recombinant proteins have garnered significant attention in the field of biomedicine due to their potential applications in immunotherapy and diagnostics. These proteins, characterized by their immunoglobulin-like domains, exhibit unique structural and functional properties that make them appealing for various therapeutic applications. Research indicates that IgFL proteins can modulate immune responses, making them candidates for developing novel treatments for autoimmune diseases, cancer, and infectious diseases. The use of recombinant DNA technology allows for the production of these proteins in a controlled environment, ensuring reproducibility and purity for experimental studies. Scientists are exploring the mechanisms by which IgFL proteins interact with immune cells, as well as their ability to enhance or inhibit specific immune pathways. Furthermore, the engineering of IgFL proteins to improve their stability and binding affinity is a focus of ongoing research, with the aim of creating more effective therapeutics. As a result, understanding the biology of IgFL proteins not only advances our knowledge of immune regulation but also paves the way for innovative approaches to combat various diseases. The collaborative efforts in structural biology, molecular engineering, and clinical research continue to expand the potential of IgFL recombinant proteins in modern medicine.
