Analytical Data
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Gene name
MOCS2
- Application
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Alternative Names
MOCS2;MOCO1;Molybdopterin synthase sulfur carrier subunit
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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
O96007
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Expression Region
1-188aa
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AA Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMSSLEISSSCFSLE TKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVI SPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKW PVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPI WKKEIYEESSTWKGNKECFWASNS
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Molecular Weight
25 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
MOCS2 (Molybdopterin Synthase 2) is a key enzyme involved in the biosynthesis of molybdenum cofactor in humans, which is essential for various biological processes, including the metabolism of sulfur-containing amino acids. Deficiencies in MOCS2 can lead to severe metabolic disorders, such as molybdenum cofactor deficiency, characterized by neurological impairments and sulfite toxicity. The study of recombinant MOCS2 proteins has gained significant attention as it provides insights into the enzyme's structure, function, and its role in enzymatic pathways. By expressing MOCS2 in heterologous systems, researchers can generate sufficient quantities of the enzyme for detailed biochemical characterization and to investigate its interactions with substrates and other associated proteins. This knowledge is crucial for understanding the molecular basis of MOCS2-related disorders and for developing potential therapeutic strategies. Furthermore, recombinant MOCS2 can be used in various applications, including enzyme engineering and biotechnological processes. Advances in recombinant DNA technology have made it feasible to produce MOCS2 in large scales, paving the way for in-depth studies concerning its mechanism of action and potential drug development for MOCS2-related diseases. Overall, research on recombinant MOCS2 not only enhances our understanding of fundamental biochemical processes but also holds promise for clinical applications in treating metabolic disorders associated with molybdenum cofactor deficiencies.
