Analytical Data
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Gene name
CarE
- Application
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Alternative Names
CarE；CARMA2；Caspase recruitment domain-containing Protein 14
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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
E5FQV0
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Expression Region
1-547aa
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AA Sequence
MALKLAVINLVWSVVLIFPNFSASHNTAPVVHDTASGDVTGKWWTIAPNRTIEAYLGIPYAKPPVGPRRFKDPEPFGKWIGVYDGTKEPTRCLQINAFLPEKTVEGSEDCLYLNVYTPSHSSPAGYPVMVFIHGGGFVDGSATSDIYGPEKLLIKDIILVTLHYRLGFLGFASLDDKDFAGNYGLKDQSLALKWVKNNIAKFGGDANKITLVGESAGAASAHYQVLSKHSQDLFQQAILMSGTADCPWAVSKPHQNGNLTAKMANFVNCSVDDSTTELLECLRKVDATEFLKHNKKFQTVWNGSFVPIVIFRPVLESSFDNSFMTYEAHRAPAPKPMMIGVTSAEGALVLELLKSDKTKRVGEALSELDKRFLEIIPVEGDFYEEQFPEKKAASIREKYFGNLTISNETMPQLIKLYSDIYFLNGTKETIKRHRGVKYLYKFGYEGSFSISQLISGDLTSKNGACHADDLLYLFPMKPFVAKRVGNETDKDKEISAKMVDLVTNYVIEGNPNSKSKPNIWTTSTEDMDFLSISPEGNFEMKKHFPDA
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Molecular Weight
61.5 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
CarE (carboxylesterase) proteins are a class of enzymes that play a crucial role in the hydrolysis of ester bonds found in various substrates, including drugs, toxins, and natural compounds. Their significance in pharmacokinetics, particularly in drug metabolism and detoxification processes, has garnered substantial attention in biomedical research. With the increasing use of ester-containing drugs and the burgeoning field of biopharmaceuticals, understanding the structure, function, and regulation of CarE proteins has become imperative. Additionally, studies indicate that CarE enzymes exhibit diverse isoforms across different species, each with unique catalytic efficiencies and substrate specificities, further emphasizing their complexity and potential applications. Advances in genomic and proteomic technologies have facilitated the exploration of CarE gene families, leading to the identification of novel isoforms and their roles in metabolism and disease. Furthermore, the relationship between CarE activity and various pathophysiological conditions highlights the importance of this enzyme family in personalized medicine. Recent studies have focused on engineering CarE proteins for enhanced activity or novel functionalities, aiming to improve drug delivery systems and bioremediation strategies. Overall, the intricate role of CarE in both human health and environmental applications underlines the necessity for continued research to fully exploit their biological potential and address relevant issues in therapeutic contexts and ecological sustainability.
