Recombinant Human Serine--Pyruvate Aminotransferase (AGXT) Protein (His)

Name: Recombinant Human Serine--Pyruvate Aminotransferase (AGXT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10196P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Serine--Pyruvate Aminotransferase (AGXT) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P21549
Target Symbol	AGXT
Synonyms	AGT; AGT1; Agxt; AGXT1; Alanine glyoxylate aminotransferase; Alanine glyoxylate aminotransferase3; Alanine--glyoxylate aminotransferase; EC 2.6.1.44; EC 2.6.1.51; Hepatic peroxisomal alanine glyoxylate aminotransferase; Hepatic peroxisomal alanine:glyoxylate aminotransferase; L alanine glyoxylate aminotransferase 1; MS773; PH1; Serine pyruvate aminotransferase; Serine--pyruvate aminotransferase; Serine--pyruvate aminotransferase, mitochondrial; Serine:pyruvate aminotransferase; SPAT; SPT; SPYA_HUMAN; TLH6
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL
Expression Range	1-392aa
Protein Length	Full Length
Mol. Weight	47.0kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Subcellular Location	Peroxisome. Mitochondrion.
Protein Families	Class-V pyridoxal-phosphate-dependent aminotransferase family
Database References	HGNC: 341 OMIM: 259900 KEGG: hsa:189 STRING: 9606.ENSP00000302620 UniGene: Hs.144567
Associated Diseases	Hyperoxaluria primary 1 (HP1)
Tissue Specificity	Liver.

Gene Functions References

Mutations at the dimer interface of alanine-glyoxylate aminotransferase alter enzyme structure/activity, leading to primary hyperoxaluria type I and determine the cellular response to vitamin B6. PMID: 29110180
two novel AGXT missense mutations (p.M49L and p.N72I), which will enrich the AGXT mutation database and provide a better comprehension of PH1 pathogenesis, were identified in a big Chinese PH1 family. Significant morphological and structural difference of kidney stones from two siblings with the same genotype observed in this study displays the heterogeneity of genotype-phenotype correlation PMID: 27644547
AGXT mutational analysis was performed to confirm the diagnosis of PH1. PMID: 28161266
this study identifies a novel AGXT gene mutation in primary hyperoxaluria after kidney transplantation failure in Tunisian patient PMID: 27568336
AGXT gene sequencing is now the choice of diagnosis of Primary hyperoxaluria type 1 (PH1)due to its non-invasive nature compared to liver enzyme assay. Early diagnosis and accurate treatment in PH1 is important for better patient outcomes. PMID: 27915025
Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1. PMID: 27179589
Novel AGXT mutations in a Tunisian population with primary hyperoxaluria type 1. PMID: 27935012
The novel p.Gln137Hisfs*19 AGXT mutation detected in this study extends the spectrum of known primary hyperoxaluria type I AGXT gene mutations in Tunisia. PMID: 27659337
Data show that onomeric minor allele of human alanine glyoxylate aminotransferase (AGT-Mi) binds pyridoxal 5-phosphate (PLP) but does not display catalytic activity. PMID: 27720751
Letter/Case Report: novel missense AGXT gene mutation in a Sri Lankan family with primary hyperoxaluria type 1. PMID: 26693850
Primary hyperoxaluria type 1 (PH1) is due to a defect in the AGXT gene. The aim of our study was to analyze the mutations causing PH1 in the Moroccan population PMID: 26383609
In conclusion, this study of an unprecedented number of primary hyperoxaluria type 1 patients showed geno-phenotype associations that have not been previously reported. PMID: 24988064
The pathogenic mutation G47R causes misfolding of alanine:glyoxylate aminotransferase. PMID: 26149463
A review of the current knowledge of the biochemical properties of liver peroxisomal alanine:glyoxylate aminotransferase and of the molecular defects caused by single point mutations associated with Primary Hyperoxaluria Type 1. PMID: 25620715
S81L and G170R mutations of AGT is associated with Primary Hyperoxaluria type I in homozygosis and heterozygosis. PMID: 24990153
AGT missense mutations associated with Primary Hyperoxaluria Type 1, were characterized. PMID: 24718375
Data suggest that dequalinium chloride (DECA) may be a pharmacologic strategy to treat primary hyperoxaluria 1 (PH1) patients with mutations in alanine:glyoxylate aminotransferase (AGT). PMID: 25237136
These are the first cases of primary hyperoxaluria type 1 to be diagnosed by clinical manifestations and AGXT gene mutations in mainland China. PMID: 24934730
data imply that the AGT Pro11Leu polymorphism is not directly responsible for the low incidence of stone formation in black South Africans. PMID: 24344980
Modeling of the mutations on a 1.9 A crystal structure suggests that Primary hyperoxaluria type I causing mutants perturb locally the native structure of AGT. PMID: 24205397
The view presented has important implications for the development of new therapeutic strategies based on targeting specific elements of alanine-glyoxylate aminotransferase homeostasis PMID: 23956997
Gly161 mutations in alanine:glyoxylate aminotransferase is associated with Primary Hyperoxaluria Type I. PMID: 24055001
Solved is the X-ray crystal structure of the S187F variant of AGT to a resolution of 2.9 A. PMID: 23589421
Identification of a double mutation c.32C>T (Pro11Leu) and c.731T>C (p.Ile244Thr) in AGXT gene in five unrelated Tunisian families with primary hyperoxaluria type 1 disease. PMID: 24012869
Three novel mutations detected in the AGXT gene associated with primary hyperoxaluria type 1 in a Tunisian patient population. PMID: 23810941
Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele PMID: 23229545
The molecular mechanism of recognition by the peroxisomal receptor Pex5p, in complex with alanine-glyoxylate aminotransferase revealed by X-ray crystallography. PMID: 22529745
These results suggest that the N-terminal extension plays an essential role in allowing AGT to attain its correct conformation and functional activity. PMID: 22198249
A side-by-side comparison was performed between normal AGT and nine purified recombinant pathogenic variants in terms of catalytic activity, coenzyme binding mode and affinity, spectroscopic features, oligomerization, and thermal stability. PMID: 22018727
selected aspects of the biochemical properties of the two allelic forms of AGXT and of some primary hyperoxaluria type 1-causing variants (review) PMID: 22201765
Partially unfolded states of AGXT strongly interact with Hsc70 and Hsp90 chaperones. PMID: 21103899
Selected AGXT gene mutations analysis provides a genetic diagnosis in 28% of Tunisian patients with primary hyperoxaluria. PMID: 21612638
Data show that P11L mutation is responsible for the urea sensitivity of AGT-Mi. PMID: 20713123
mutation of the AGXT gene, showing the patient to be compound heterozygous for the c.33_34InsC and c.508G > A mutations PMID: 20020206
Genotype-phenotype correlation in primary hypoxaluria type 1: the p. Gly170Arg AGXT mutation is associated with a better outcome. PMID: 20016466
Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I. PMID: 20133649
investigated occurrence of Pro11Leu polymorphism in both herder & agriculturalist populations from Central Asia; findings show distribution of variation observed in the AGXT gene could be due to demographic history, rather than local adaptation to diet PMID: 20059472
crystal structure of AGT consists of an intimate dimer in which an extended N-terminal segment of 21 amino acids from one subunit wraps as an elongated irregular coil around the outside of the crystallographic symmetry-related subunit. PMID: 20208150
3D picture of an in vivo early ATP-dependent step of the folding reaction cycle of the chaperonin and supports a GroEL functional model in which the chaperonin promotes folding of the AGXT-LTM mutant protein through forced unfolding mechanism PMID: 20056599
serine:pyruvate aminotransferase expression is regulated by Sp1, AP-2 and PKA PMID: 12169688
crystal structure of normal human AGT complexed to the competitive inhibitor amino-oxyacetic acid to 2.5A PMID: 12899834
Early detection of Gly170Arg and Phe152Ile mutations in PH1 has important clinical implications because of their association with pyridoxine responsiveness and clinical outcome PMID: 15253729
report describing 3 AGXT gene mutations in Chinese patients with primary hyperoxaluria type 1 PMID: 15365967
mutations with serious consequences in vivo may not be inherently catalytically inactive and may be rescuable PMID: 15802217
human AGT interacts with human Pex5p in mammalian cells, but not yeast cells; type 1 peroxisomal targeting sequence(PTS1)is located entirely within the smaller C-terminal structural domain of 110 amino acids PMID: 15911627
Determination of crystal structure of AGT has enabled effects of some of most important missense mutations in AGXT gene to be rationalised in terms of AGT folding, dimerization and stability. New possibilities for design of pharmacological agents. PMID: 15961951
Presentation and role of transplantation [kidney and/or liver] in adult patients with type 1 primary hyperoxaluria and the 1244T AGXT mutation in a university hospital in Spain are presented. PMID: 16912707
The effects of missense mutations on enzyme activity, dimerization, aggregation, and turnover were investigated. PMID: 16971151
expressed wild-type human AGT1 was predominantly localized in mouse hepatocellular peroxisomes, whereas the most common mutant form of AGT1 (G170R) was localized predominantly in the mitochondria PMID: 17110443
AGXT is even more variable than formerly believed in the diagnosis of primary hyperoxaluria PMID: 17460142

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