Analytical Data
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Gene name
FLJ10292
- Application
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Alternative Names
FLJ10292; MAGO; Mago nashi homolog 2; Mago nashi homolog B; MAGOH; MAGOH2; MAGOHB; MGN2; MGN2_HUMAN; Protein mago nashi homolog 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96A72
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Expression Region
1-148aa
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AA Sequence
MAVASDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI
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Molecular Weight
43.7 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
FLJ10292, a recombinant protein, has garnered significant interest in biomedical research due to its potential roles in cellular signaling and disease mechanisms. Initially identified from gene expression profiling studies, FLJ10292 is believed to be implicated in various physiological processes, including cell proliferation, differentiation, and apoptosis. Recent studies have suggested that aberrations in FLJ10292 expression may be linked to certain cancers and metabolic disorders, thus positioning it as a candidate biomarker for diagnostic or therapeutic applications. The protein's structure and function have yet to be fully elucidated, making it an intriguing focus for further investigation. Researchers are employing recombinant DNA technology to produce FLJ10292 for in vitro studies aimed at understanding its interactions with other cellular proteins and pathways. This research could potentially lead to novel insights into its role in disease states, as well as explore its efficacy as a target for drug development. Given the increasing recognition of the importance of protein interactions in cellular function, studying FLJ10292 not only enhances our understanding of its individual contributions but also sheds light on broader biological processes, offering potential avenues for innovative treatments in conditions where these pathways are dysregulated.
