Analytical Data
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Gene name
AGXT
- Application
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Alternative Names
AGXT;AGT1;SPAT;Alanine--glyoxylate aminotransferase
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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
P21549
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Expression Region
293-392aa
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AA Sequence
EAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDH FDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL
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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
Related Products
Protein Description
AGXT, short for alanine-glyoxylate aminotransferase, is a crucial enzyme involved in the metabolism of glyoxylate to glycine in the liver, playing a significant role in preventing the accumulation of toxic metabolites. Mutations in the AGXT gene can lead to primary hyperoxaluria type 1 (PH1), a rare genetic disorder characterized by excessive oxalate production, resulting in kidney damage and increased risk of kidney stones. Current therapeutic strategies for PH1 include renal replacement therapies and liver transplantation, but these approaches do not address the underlying enzymatic deficiency. Consequently, the recombinant expression and purification of AGXT protein have gained attention as potential avenues for developing enzyme replacement therapies. Research efforts focus on optimizing the expression of AGXT in suitable host systems, such as bacteria or yeast, to produce functionally active enzyme with proper folding and catalytic activity. Furthermore, understanding the structure-function relationships of AGXT through techniques like X-ray crystallography and molecular dynamics simulations can enhance the design of small molecules or gene therapies aimed at correcting the malfunctioning enzyme. This research area presents a promising outlook for innovative treatments for PH1, potentially improving the quality of life for affected individuals by providing a targeted intervention that addresses the root cause of the disease.











