Analytical Data
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Gene name
aac
- Application
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Alternative Names
Aculeacin-A acylase small subunit Aculeacin-A acylase large subunit
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Species
Actinoplanes utahensis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29958
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Expression Region
35-214aa
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Molecular Weight
35.1 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
AAC (amino acid transporters) recombination proteins play a significant role in cellular metabolism and nutrient uptake, making them a focal point in research on cellular physiology and disease mechanisms. These proteins facilitate the transport of amino acids across cell membranes, which is crucial for protein synthesis, cell signaling, and metabolic pathways. Recent studies have highlighted their involvement in various pathologies, including cancer, metabolic disorders, and neurodegenerative diseases, as dysregulation of amino acid transport can lead to altered cellular functions and tumor progression. The development of AAC recombinant proteins through techniques such as gene cloning and protein engineering has allowed researchers to better understand their structure, function, and regulation. Investigating these proteins not only provides insights into their biological roles but also opens avenues for therapeutic interventions, including targeted drug delivery systems and metabolic modulation strategies. The ongoing research aims to elucidate the intricate mechanisms governing amino acid transport and to leverage this knowledge for biomedical applications.
