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Literature summary for 2.4.2.26 extracted from

  • Casanova, J.C.; Ambrosius, M.; Kuhn, J.; Kleesiek, K.; Goetting, C.
    Analysis of xylosyltransferase II binding to the anticoagulant heparin (2009), Biochem. Biophys. Res. Commun., 383, 4-10.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
into pGEX-6P-1, ligated into the multiple cloning site of the BamHI-digested and shrimp alkaline phosphatase-dephosphorylated pMAL-c4E expression vector, in frame with the N-terminal located maltose binding protein, expressed in Escherichia coli strain BL21(DE3) under the control of the IPTG inducible tac promoter. MBP/XylT-II fusion protein expressed in ER2507 that contains prolonged XylT-II fragments (MBP/XylT-IIF1-3 and MBP/XylT-IIF4-6) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Purification (Commentary)

Purification (Comment) Organism
full-length XylT-II purified to homogeneity as inclusion bodies, by maltose binding protein affinity chromatography and heparin affinity chromatography Homo sapiens

Synonyms

Synonyms Comment Organism
xylosyltransferase II
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Homo sapiens
XylT-II
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Homo sapiens

General Information

General Information Comment Organism
physiological function XylT-II fragments bind with low affinity to heparin. Prolonging of XylT-II fragments does not account for a cooperative effect of multiple heparin-binding motifs and in turn for a stronger heparin-binding. Two high polarity surface regions in the stem region with the sequence [-K-G-R-Q-R-K-P-R-P-] and [-G-R-R-H-G-R-W-], both representing Cardin-Weintraub motifs Homo sapiens