Analytical Data
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Gene name
AEA
- Application
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Alternative Names
AEA；CB2A；CB2B；Cannabinoid receptor 2
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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
P34972
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Expression Region
1-360aa
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AA Sequence
MEECWVTEIANGSKDGLDSNPMKDYMILSGPQKTAVAVLCTLLGLLSALENVAVLYLILSSHQLRRKPSYLFIGSLAGADFLASVVFACSFVNFHVFHGVDSKAVFLLKIGSVTMTFTASVGSLLLTAIDRYLCLRYPPSYKALLTRGRALVTLGIMWVLSALVSYLPLMGWTCCPRPCSELFPLIPNDYLLSWLLFIAFLFSGIIYTYGHVLWKAHQHVASLSGHQDRQVPGMARMRLDVRLAKTLGLVLAVLLICWFPVLALMAHSLATTLSDQVKKAFAFCSMLCLINSMVNPVIYALRSGEIRSSAHHCLAHWKKCVRGLGSEAKEEAPRSSVTETEADGKITPWPDSRDLDLSDC
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Molecular Weight
39.6 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
Related Products
Protein Description
AEA (Amylopectin Exonuclease A) recombinant proteins have emerged as a significant focus of research due to their critical role in understanding the biochemical processes involved in starch metabolism and its implications for various biological and industrial applications. Starch, a major energy source for plants and many organisms, is composed of amylose and amylopectin, the latter being a highly branched polymer. AEA proteins specifically target and degrade amylopectin, providing insight into the mechanisms of polysaccharide breakdown and energy release. The recombinant expression of AEA proteins allows for the production of large quantities of these enzymes, facilitating detailed studies on their enzymatic activity, substrate specificity, and structural properties. Additionally, AEA proteins are of considerable interest in the agricultural and food industries, where manipulating starch degradation can lead to improved crop yields, enhanced food texture, and more efficient biofuel production. As the demand for sustainable energy sources continues to escalate, understanding AEA and similar enzymes could contribute to the development of novel bioconversion processes. Overall, ongoing research into AEA recombinant proteins promises to advance our knowledge in biochemistry, agriculture, and industrial biotechnology, paving the way for innovations that leverage starch metabolism for various beneficial applications.
