Analytical Data
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Gene name
BCHE
- Application
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Alternative Names
BCHE；CHE1；Cholinesterase
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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
P06276
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Expression Region
29-602aa
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AA Sequence
EDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLT KWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIP APKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGA LGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAG AASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLT GCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLT DMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEF QEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPL ERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKY LTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRW NNYMMDWKNQFNDYTSKKESCVGLVDHHHHHH
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Molecular Weight
66 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
BCHE, or butyrylcholinesterase, is a serine hydrolase enzyme primarily found in the human plasma, playing a key role in the metabolism of choline esters and the breakdown of certain neurotoxic compounds such as organophosphates. Research into recombinant BCHE has gained significant attention due to its potential therapeutic applications in treating conditions associated with cholinergic dysfunction, including Alzheimer’s disease and myasthenia gravis. Additionally, recombinant BCHE has been explored as a bioscavenger for organophosphate detoxification, offering a promising avenue for counteracting pesticide and chemical warfare agent exposure. The ability to produce BCHE through recombinant DNA technology enables the generation of large quantities of the enzyme with enhanced stability and activity, overcoming limitations associated with human-derived enzymes. Studies have focused on optimizing expression systems, modifying the enzyme for improved properties, and investigating its interactions with various substrates. These efforts aim to facilitate the development of BCHE-based treatments and provide insights into the enzyme’s role in pharmacology and toxicology, highlighting its importance in medical research and public health.
