Analytical Data
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Gene name
AMN
- Application
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
D3ZFK9
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Expression Region
Ala20~Glu268
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Molecular Weight
30kDa
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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
Related Products
Protein Description
The study of AMN (Amnionless) recombinant proteins has gained significant attention due to their crucial role in various physiological processes and potential implications in disease mechanisms. AMN is a membrane protein that plays an essential part in the development of the embryonic hematopoietic system and is involved in the uptake of nutrients and signaling pathways in the vertebrate embryo. Disruptions in AMN function have been linked to abnormalities in cell signaling and tissue development, making it a key candidate for research related to developmental disorders and cancers. Recent advancements in recombinant protein technology have enabled researchers to produce AMN proteins in vitro, allowing for detailed studies of their structure, function, and interactions with other cellular components. This research not only enhances our understanding of AMN's biological roles but also paves the way for potential therapeutic applications, including drug design and regenerative medicine. As scientists continue to explore the mechanisms by which AMN influences cellular dynamics, the insights gained could lead to the development of innovative approaches to address various health challenges.
