Analytical Data
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基因名
JN
- Application
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别名
JN；KIAA1189；Ermin
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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
Q8TAM6
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表达区间
1-284aa
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氨基酸序列
MTDVPATFTQ AECNGDKPPE NGQQTITKIS EELTDVDSPL PHYRVEPSLE GALTKGSQEE RRKLQGNMLL NSSMEDKMLK ENPEEKLFIV HKAITDLSLQ ETSADEMTFR EGHQWEKIPL SGSNQEIRRQ KERITEQPLK EEEDEDRKNK GHQAAEIEWL GFRKPSQADM LHSKHDEEQK VWDEEIDDDD DDNCNNDEDE VRVIEFKKKH EEVSQFKEEG DASEDSPLSS ASSQAVTPDE QPTLGKKSDI SRNAYSRYNT ISYRKIRKGN TKQRIDEFES MMHL
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分子量
32.7 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
The study of JN recombinant proteins has emerged as a pivotal area in biomedical research, particularly due to their potential applications in therapeutic development and disease modeling. JN proteins are known for their unique structural and functional properties, which make them suitable candidates for a variety of biotechnological applications. These proteins can be engineered to exhibit enhanced stability, binding affinity, and specificity, thereby improving their utility in drug delivery systems, vaccines, and diagnostic tools. Recent advancements in genetic engineering and protein expression techniques have facilitated the high-yield production of JN recombinant proteins, allowing researchers to investigate their biochemical properties and interactions with other biomolecules in detail. As a result, they have garnered significant attention for their role in addressing complex challenges such as vaccine development for emerging infectious diseases, targeted cancer therapies, and the study of protein interactions in cellular pathways. Furthermore, the elucidation of their mechanisms of action could lead to novel insights into pathophysiological processes and contribute to the development of innovative therapeutic strategies. Overall, ongoing research into JN recombinant proteins holds promise for advancing our understanding of molecular biology and enhancing the efficacy of current medical interventions.
