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Literature summary for 3.1.4.39 extracted from

  • Song, Y.; Dilger, E.; Bell, J.; Barton, W.A.; Fang, X.
    Large scale purification and characterization of recombinant human autotaxin/lysophospholipase D from mammalian cells (2010), BMB Rep., 43, 541-546.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.39

Application

Application Comment Organism
analysis the purified ATX protein is enzymatically active and biologically functional, offering a useful tool for further biological and structural studies of this important enzyme Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
functional expression of the ATX-Fc fusion protein in HEK-293 cells with secretion of the enzyme to the medium Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant ATX-Fc fusion protein from HEK-293 cells cell medium by affinity chromatography with protein A sepharose followed by cleavage with thrombin. Detagged ATX protein is further purified to essential homogeneity by gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
ATX
-
 Homo sapiens
autotaxin
-
 Homo sapiens
lysophospholipase D
-
 Homo sapiens

General Information

General Information Comment Organism
additional information the ability of ATX to drive cell migration is enhanced by the presence of the ATX substrate lysophosphocholine Homo sapiens
physiological function autotaxin is an enzyme present in the blood and responsible for biosynthesis of lysophosphatidic acid Homo sapiens