Analytical Data
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Gene name
MLYCD
- Application
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Alternative Names
MLYCD；Malonyl-CoA decarboxylase. mitochondrial
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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
O95822
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Expression Region
40-493aa
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AA Sequence
MDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL
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Molecular Weight
55.9kDa
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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
MLYCD, or malonyl-CoA decarboxylase, is an enzyme that plays a crucial role in fatty acid metabolism by catalyzing the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide. This process is essential for maintaining energy homeostasis and regulating lipid biosynthesis in various organisms. Research into MLYCD has gained momentum due to its potential implications in metabolic disorders, including obesity, diabetes, and cardiovascular diseases. Understanding the structure and function of MLYCD at a molecular level can provide insights into its regulatory mechanisms and its significance in cellular metabolism. Recent studies have focused on the recombinant expression of MLYCD to facilitate detailed biochemical characterization and structural analysis. These investigations can lead to the identification of the enzyme’s active sites and developmental pathways, paving the way for potential therapeutic targets to address metabolic diseases. Advancements in recombinant DNA technology have enabled the production of MLYCD in various expression systems, enhancing our ability to study its enzymatic properties and interactions with other metabolic pathways. Overall, research on the recombinant MLYCD protein is crucial for elucidating its biological functions and exploring its potential as a target for drug development aimed at treating metabolic conditions characterized by dysregulated fatty acid metabolism.
