Analytical Data
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Gene name
ME3
- Application
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Alternative Names
ME3；NADP-dependent malic enzyme. 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
Q16798-1
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Expression Region
24-590aa
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AA Sequence
RWTPTAPAQGCHSKPGPARPVPLKKRGYDVTRNPHLNKGMAFTLEERLQL GIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYR VLTSDVEKFMPIVYTPTVGLACQHYGLTFRRPRGLFITIHDKGHLATMLN SWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQC LPVLLDVGTNNEELLRDPLYIGLKHQRVHGKAYDDLLDEFMQAVTDKFGI NCLIQFEDFANANAFRLLNKYRNKYCMFNDDIQGTASVAVAGILAALRIT KNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKG LIVKGRSHLNHEKEMFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGAFTE QILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTEGRGIFASGSPFKS VTLEDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQE VSEQHLSQGRLYPPLSTIRDVSLRIAIKVLDYAYKHNLASYYPEPKDKEA FVRSLVYTPDYDSFTLD
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Molecular Weight
67 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
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Protein Description
ME3 (malic enzyme 3) is a crucial enzyme involved in metabolic processes, particularly in the regulation of energy production and signaling pathways. It catalyzes the oxidative decarboxylation of malate to pyruvate, a reaction that plays a significant role in both mitochondrial metabolism and cytosolic pathways, influencing cellular respiration and anabolic processes. Research into ME3 has gained momentum due to its potential implications in various physiological and pathological conditions, including cancer metabolism, obesity, and neurodegenerative diseases. Dysregulation of ME3 expression and activity has been linked to altered metabolic states, highlighting its importance as a metabolic regulator. Recent studies have focused on the structural and functional characterization of ME3, utilizing recombinant protein techniques to produce and analyze the enzyme. Understanding the mechanisms by which ME3 operates at a molecular level could pave the way for novel therapeutic strategies aimed at correcting metabolic imbalances in diseases. Additionally, exploring the role of ME3 in different tissues may reveal its versatility and necessity in maintaining cellular homeostasis. Thus, the investigation of ME3 as a recombinant protein is not only crucial for basic biochemical research but also offers significant insights into its potential as a target for therapeutic intervention in metabolic disorders.
