Analytical Data
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Gene name
Ces1d
- Application
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Alternative Names
Ces1d;Ces1;Ces3;Carboxylesterase 1D
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Species
Mouse
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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
Q8VCT4
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Expression Region
19-565aa
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AA Sequence
YP SSPPVVNTVK GKVLGKYVNL EGFTQPVAVF LGVPFAKPPL GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD AVGGQVLSEL FTNRKENIPL QFSEDCLYLN IYTPADLTKN SRLPVMVWIH GGGLVVGGAS TYDGLALSAH ENVVVVTIQY RLGIWGFFST GDEHSRGNWG HLDQVAALRW VQDNIANFGG NPGSVTIFGE SAGGFSVSVL VLSPLAKNLF HRAISESGVS LTAALITTDV KPIAGLVATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL NLFKLDLLGN PKESYPFLPT VIDGVVLPKA PEEILAEKSF STVPYIVGIN KQEFGWIIPT LMGYPLAEGK LDQKTANSLL WKSYPTLKIS ENMIPVVAEK YLGGTDDLTK KKDLFQDLMA DVVFGVPSVI VSRSHRDAGA STYMYEFEYR PSFVSAMRPK AVIGDHGDEI FSVFGSPFLK DGASEEETNL SKMVMKFWAN FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK EVSFWAELRA KESAQRPSHR EHVEL
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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
Ces1d, a member of the Carboxylesterase family, has garnered research interest due to its significant role in various biochemical processes, including lipid metabolism and the detoxification of xenobiotics. This enzyme is particularly relevant in the context of agriculture and pharmaceuticals, as it can influence the metabolism of pesticide compounds and drug metabolism, affecting efficacy and toxicity. The ability of Ces1d to hydrolyze esters has implications in the development of biocatalysts for industrial applications, including in the synthesis of biofuels and biopolymers. Recent advancements in recombinant protein technology have enabled detailed studies of Ces1d’s structure-function relationships, facilitating insights into its catalytic mechanisms and substrate specificity. Furthermore, understanding the regulatory mechanisms that govern Ces1d expression and activity may provide novel strategies for enhancing its functionality in biotechnological applications. Overall, researching Ces1d and its recombinant protein forms is essential for harnessing its potential in environmental sustainability, toxicological research, and therapeutic developments.











