Analytical Data
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基因名
YJEFN3
- Application
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别名
YJEFN3；AIBP2；YjeF N-terminal domain-containing Protein 3
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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
A6XGL0
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表达区间
1-299aa
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氨基酸序列
MSSAAGPDPSEAPEERHFLRALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQSWLEQIWNAGPVCQSTAEAAALERELLEDYRFGRQQLVELCGHASAVAVTKAFPLPALSRKQRTVLVVCGPEQNGAVGLVCARHLRVFEYEPTIFYPTRSLDLLHRDLTTQCEKMDIPFLSYLPTEVQLINEAYGLVVDAVLGPGVEPGEVGGPCTRALATLKLLSIPLVSLDIPSGWDAETGSDSEDGLRPDVLVSLAAPKRCAGRFSGRHHFVAGRFVPDDVRRKFALRLPGYTGTDCVAAL
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分子量
32.6 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
YJEFN3 is a novel protein that has garnered attention in recent years due to its potential roles in cellular processes and disease mechanisms. Initial studies have suggested that YJEFN3 may be involved in cell signaling pathways, contributing to both normal cellular functions and pathological conditions such as cancer and neurodegenerative diseases. Its unique structural characteristics, particularly its domain organization, suggest that it may interact with other proteins and play a critical role in protein-protein interactions within various biological contexts. Research involving the recombinant production of YJEFN3 has facilitated the investigation of its functional properties and interactions, enabling scientists to elucidate its role within the cell. Additionally, understanding YJEFN3's mechanisms may provide insights into therapeutic targets for diseases where it is implicated. The study of YJEFN3 is critical as it not only contributes to our fundamental understanding of cellular biology but also opens avenues for the development of new interventions in health and disease. As research progresses, the detailed characterization of YJEFN3 could lead to pivotal advancements in molecular biology and medicine.
