Analytical Data
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Gene name
AMD1
- Application
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Alternative Names
SAMDC; AdoMetDC; S-Adenosylmethionine Decarboxylase 1; S-adenosylmethionine decarboxylase proenzyme
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17707
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Expression Region
Met1~Ser334
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Molecular Weight
42kDa
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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
The study of AMD1 (adenosine monophosphate deaminase 1) recombinant protein has garnered significant attention due to its crucial role in the cellular metabolism of adenine and the regulation of purine nucleotide levels. AMD1 is involved in converting adenosine monophosphate (AMP) to inosine monophosphate (IMP), a key step in the purine salvage pathway, which is essential for maintaining nucleotide pools, energy balance, and overall cellular function. Dysregulation of AMD1 has been implicated in various pathologies, including cancer and neurological disorders, highlighting its potential as a therapeutic target. The ability to produce AMD1 as a recombinant protein has enabled researchers to investigate its structural and functional properties more thoroughly. By understanding AMD1 at a molecular level, including its enzymatic mechanisms and interactions with other cellular components, scientists aim to elucidate the pathways it influences and the implications of its dysregulation. This research not only provides insights into fundamental biochemical processes but also holds promise for developing innovative therapeutic strategies to combat diseases associated with impaired purine metabolism.
