Analytical Data
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Gene name
YJEFN3
- Application
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Alternative Names
YJEFN3；AIBP2；YjeF N-terminal domain-containing Protein 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A6XGL0
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Expression Region
1-299aa
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AA Sequence
MSSAAGPDPSEAPEERHFLRALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQSWLEQIWNAGPVCQSTAEAAALERELLEDYRFGRQQLVELCGHASAVAVTKAFPLPALSRKQRTVLVVCGPEQNGAVGLVCARHLRVFEYEPTIFYPTRSLDLLHRDLTTQCEKMDIPFLSYLPTEVQLINEAYGLVVDAVLGPGVEPGEVGGPCTRALATLKLLSIPLVSLDIPSGWDAETGSDSEDGLRPDVLVSLAAPKRCAGRFSGRHHFVAGRFVPDDVRRKFALRLPGYTGTDCVAAL
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Molecular Weight
32.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
