Analytical Data
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基因名
JUN
- Application
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别名
(Activator protein 1)(AP1)(Proto-oncogene c-Jun)(Transcription factor AP-1 subunit Jun)(V-jun avian sarcoma virus 17 oncogene homolog)(p39)
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种属
Human
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P05412
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表达区间
1-331aa
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分子量
43.1 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
Research on JUN recombinant proteins focuses on understanding the role of the JUN proto-oncogene, a vital component of the AP-1 transcription factor complex, which is crucial in regulating gene expression, cell proliferation, differentiation, and apoptosis. The JUN protein, particularly in its phosphorylated form, is implicated in various cellular processes and is associated with numerous pathological conditions, including cancer, inflammation, and tissue repair. Studies often investigate how overexpression or mutation of the JUN gene can lead to oncogenic transformations, making it a significant target for therapeutic intervention. The ability to produce JUN recombinant proteins enables researchers to explore the protein's biochemical properties, interaction with other cellular factors, and its involvement in signaling pathways. By utilizing techniques such as molecular cloning, expression in suitable host systems, and purification processes, scientists can delve into the functions and mechanisms of JUN in greater detail. Furthermore, understanding its dynamics can offer insights into potential drug development aimed at modulating JUN activity for treating diseases where its dysregulation is a contributing factor. As such, examining JUN recombinant proteins is a critical aspect of cancer research and regenerative medicine, providing a foundation for innovations in targeted therapies and biologic treatments.
