Analytical Data
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Gene name
AGA
- Application
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Alternative Names
AGA；N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
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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
P20933
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Expression Region
24-346aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSSSPLPLVVNTWPFKNATEAAWRALASG GSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVG AVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTA SQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGILKQDIPIHKETED DRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDT AGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEF FGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
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Molecular Weight
37 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
AGA (Adenylate Glycolytic Enzyme) recombinant protein research has gained significant interest due to its potential applications in biotechnology and medicine. AGA plays a crucial role in purine metabolism, and its dysfunction is associated with various metabolic disorders, highlighting its importance in understanding and treating such conditions. The ability to produce AGA in recombinant form allows for in-depth studies on its structure and function, enabling researchers to elucidate its biochemical pathways and interactions within cellular systems. The development of AGA recombinant proteins also paves the way for innovative therapeutic approaches, including enzyme replacement therapies for patients with enzymatic deficiencies. Furthermore, the generation of large quantities of pure AGA can facilitate drug discovery processes, as these proteins serve as vital tools in high-throughput screening and assay development. The advancement of techniques like CRISPR and synthetic biology also enhances the capacity for engineering AGA to improve its efficacy or to create novel variants with tailored properties, further expanding its utility in various scientific domains. Overall, AGA recombinant protein research not only contributes to our fundamental understanding of metabolic processes but also holds promise for developing targeted treatments for metabolic disorders, making it a vital area of interest in contemporary biological research.
