Recombinant Full Length Human AGXT, Flag-tagged

• Cat.No.: AGXT-6061HFL
• Product Overview: Recombinant Full Length Human AGXT, fused with C-terminal Flag tag, was expressed in mamanlian cells.

Specification

• Source: Mamanlian cells
• Species: Human
• Tag: Flag
• Molecular Mass: 42.8 kDa
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Storage: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol.
• Concentration: >50 ug/mL as determined by microplate BCA method
• Shipping: The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.

Gene Information

• Gene Name: AGXT alanine-glyoxylate aminotransferase [ Homo sapiens (human) ]
• Official Symbol: AGXT
• Synonyms: AGXT; AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1; alanine-glyoxylate aminotransferase; serine--pyruvate aminotransferase; serine-pyruvate aminotransferase; serine:pyruvate aminotransferase; alanine--glyoxylate aminotransferase; L-alanine: glyoxylate aminotransferase 1; hepatic peroxisomal alanine:glyoxylate aminotransferase; NP_000021.1; EC 2.6.1.44; EC 2.6.1.51
• Gene ID: 189
• mRNA Refseq: NM_000030
• Protein Refseq: NP_000021
• MIM: 604285
• UniProt ID: P21549

Reviews

03/07/2022

The customer service was fantastic—helpful, friendly, and made the ordering process a breeze!

02/10/2022

The efficiency of this protein is outstanding. Saved me a lot of time!

07/30/2021

I never knew how much easier my work could be until I tried this protein.

11/16/2019

I'm so grateful for this protein – it's a game-changer for my studies!

08/02/2018

I can confidently say that this product is worth every penny.

Q&As

Are there any known structural motifs in AGXT essential for its enzymatic activity?

AGXT contains a PLP-binding domain, characteristic of aminotransferases, which is critical for its enzymatic activity and substrate specificity.

Can mutations in the AGXT gene lead to any hereditary disorders?

Yes, mutations in the AGXT gene can cause primary hyperoxaluria type 1 (PH1), a rare autosomal recessive disorder characterized by the overproduction and accumulation of oxalate, resulting in severe kidney and urinary tract complications.

Can AGXT be targeted therapeutically for the treatment of kidney stones in non-PH1 patients?

Targeting AGXT enzymatic activity may hold promise for developing therapies to prevent kidney stone formation in non-PH1 patients; however, further research is needed to validate this approach.

Which cellular compartment is AGXT predominantly localized in?

AGXT is primarily localized in the peroxisomes, a subcellular organelle responsible for various metabolic processes, including lipid metabolism and detoxification.

Can AGXT activity be influenced by epigenetic modifications?

Epigenetic modifications, such as DNA methylation or histone acetylation, could potentially regulate AGXT gene expression and activity, affecting oxalate metabolism.

How is AGXT activity regulated at the post-translational level?

AGXT activity can be regulated by phosphorylation, allosteric modulation, and interaction with other proteins involved in peroxisomal metabolism.

What is the primary function of AGXT in the human body?

AGXT plays a crucial role in the peroxisomal glyoxylate pathway, converting glyoxylate to glycine to prevent the accumulation of harmful oxalate, which can lead to kidney stone formation.

How does AGXT deficiency lead to hyperoxaluria in PH1 patients?

In PH1 patients, AGXT deficiency impairs the conversion of glyoxylate to glycine, leading to the accumulation of glyoxylate. Excessive glyoxylate is converted to oxalate, which can form kidney stones and cause tissue damage.

Is AGXT involved in other physiological processes beyond oxalate metabolism?

AGXT may participate in other cellular processes or metabolic pathways, and its broader functional roles warrant further exploration.

What is the reaction catalyzed by AGXT in the glyoxylate pathway?

AGXT catalyzes the conversion of glyoxylate and L-alanine to glycine and pyruvate, utilizing PLP as a cofactor.