Analytical Data
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基因名
IFNG
- Application
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别名
IFNG;Interferon gamma
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P01579
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表达区间
24-166aa
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氨基酸序列
QDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ
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分子量
40.0 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
Interferon-gamma (IFN-γ), a cytokine primarily produced by T cells and natural killer (NK) cells, plays a crucial role in the immune response by promoting the activation of macrophages, enhancing antigen presentation, and influencing the differentiation of various immune cells. Due to its pivotal role in immunity and its immunomodulatory effects, recombinant IFN-γ has been extensively studied for therapeutic applications in various diseases, including chronic infections like tuberculosis and autoimmune disorders. The production of recombinant IFN-γ using recombinant DNA technology allows for the generation of a highly pure and biologically active form of the protein, which can be used in clinical settings. Researchers focus on optimizing expression systems, such as bacteria, yeast, or mammalian cells, to develop cost-effective and scalable production methods. Additionally, understanding the structure-function relationship of IFN-γ is vital for improving its efficacy and reducing potential side effects. Investigations into post-translational modifications, stability, and delivery methods further enhance its therapeutic potential. As research progresses, the development of IFN-γ as a treatment option continues to show promise, particularly in the context of immunotherapy and combination treatments in oncology and infectious diseases.
