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  4. Recombinant Human Serine--pyruvate aminotransferase (AGXT)

Recombinant Human Serine--pyruvate aminotransferase (AGXT)

  • 中文名稱：
    Recombinant Human Serine--pyruvate aminotransferase(AGXT)
  • 貨號：
    CSB-EP001468HU
  • 規格：
    ￥1344
  • 圖片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

產品詳情

  • 純度：
    Greater than 90% as determined by SDS-PAGE.
  • 基因名：
    AGXT
  • Uniprot No.：
  • 別名：
    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
  • 種屬：
    Homo sapiens (Human)
  • 蛋白長度：
    Full Length
  • 來源：
    E.coli
  • 分子量：
    47.0kDa
  • 表達區域：
    1-392aa
  • 氨基酸序列
    MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL
    Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
    If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
  • 蛋白標簽：
    N-terminal 6xHis-tagged
  • 產品提供形式：
    Liquid or Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 緩沖液：
    If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
    Note: If you have any special requirement for the glycerol content, please remark when you place the order.
    If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
  • 儲存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 貨期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事項：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA：
    Please contact us to get it.

產品評價

靶點詳情

  • 基因功能參考文獻：
    1. 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
    2. 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
    3. AGXT mutational analysis was performed to confirm the diagnosis of PH1. PMID: 28161266
    4. this study identifies a novel AGXT gene mutation in primary hyperoxaluria after kidney transplantation failure in Tunisian patient PMID: 27568336
    5. 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
    6. Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1. PMID: 27179589
    7. Novel AGXT mutations in a Tunisian population with primary hyperoxaluria type 1. PMID: 27935012
    8. 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
    9. 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
    10. Letter/Case Report: novel missense AGXT gene mutation in a Sri Lankan family with primary hyperoxaluria type 1. PMID: 26693850
    11. 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
    12. 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
    13. The pathogenic mutation G47R causes misfolding of alanine:glyoxylate aminotransferase. PMID: 26149463
    14. 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
    15. S81L and G170R mutations of AGT is associated with Primary Hyperoxaluria type I in homozygosis and heterozygosis. PMID: 24990153
    16. AGT missense mutations associated with Primary Hyperoxaluria Type 1, were characterized. PMID: 24718375
    17. 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
    18. 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
    19. data imply that the AGT Pro11Leu polymorphism is not directly responsible for the low incidence of stone formation in black South Africans. PMID: 24344980
    20. 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
    21. 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
    22. Gly161 mutations in alanine:glyoxylate aminotransferase is associated with Primary Hyperoxaluria Type I. PMID: 24055001
    23. Solved is the X-ray crystal structure of the S187F variant of AGT to a resolution of 2.9 A. PMID: 23589421
    24. 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
    25. Three novel mutations detected in the AGXT gene associated with primary hyperoxaluria type 1 in a Tunisian patient population. PMID: 23810941
    26. 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
    27. The molecular mechanism of recognition by the peroxisomal receptor Pex5p, in complex with alanine-glyoxylate aminotransferase revealed by X-ray crystallography. PMID: 22529745
    28. 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
    29. 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
    30. 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
    31. Partially unfolded states of AGXT strongly interact with Hsc70 and Hsp90 chaperones. PMID: 21103899
    32. Selected AGXT gene mutations analysis provides a genetic diagnosis in 28% of Tunisian patients with primary hyperoxaluria. PMID: 21612638
    33. Data show that P11L mutation is responsible for the urea sensitivity of AGT-Mi. PMID: 20713123
    34. mutation of the AGXT gene, showing the patient to be compound heterozygous for the c.33_34InsC and c.508G > A mutations PMID: 20020206
    35. Genotype-phenotype correlation in primary hypoxaluria type 1: the p. Gly170Arg AGXT mutation is associated with a better outcome. PMID: 20016466
    36. Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I. PMID: 20133649
    37. 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
    38. 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
    39. 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
    40. serine:pyruvate aminotransferase expression is regulated by Sp1, AP-2 and PKA PMID: 12169688
    41. crystal structure of normal human AGT complexed to the competitive inhibitor amino-oxyacetic acid to 2.5A PMID: 12899834
    42. 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
    43. report describing 3 AGXT gene mutations in Chinese patients with primary hyperoxaluria type 1 PMID: 15365967
    44. mutations with serious consequences in vivo may not be inherently catalytically inactive and may be rescuable PMID: 15802217
    45. 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
    46. 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
    47. 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
    48. The effects of missense mutations on enzyme activity, dimerization, aggregation, and turnover were investigated. PMID: 16971151
    49. 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
    50. AGXT is even more variable than formerly believed in the diagnosis of primary hyperoxaluria PMID: 17460142

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  • 相關疾?。?/div>
    Hyperoxaluria primary 1 (HP1)
  • 亞細胞定位：
    Peroxisome. Mitochondrion.
  • 蛋白家族：
    Class-V pyridoxal-phosphate-dependent aminotransferase family
  • 組織特異性：
    Liver.
  • 數據庫鏈接：

    HGNC: 341

    OMIM: 259900

    KEGG: hsa:189

    STRING: 9606.ENSP00000302620

    UniGene: Hs.144567



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