Active • Host: E. coli • AA: 1-286 • Tag: C-terminal His • MW: 33.4 kDa
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Lipopolysaccharide α-1,4-galactosyltransferase (N. meningitidis)

Item No. 44170

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • LgtC Glycosyltransferase
  • Lipopolysaccharyl α-galactosyltransferase
  • Lipopolysaccharyl-1,4-galactosyltransferase
Purity
≥90% estimated by SDS-PAGE
Source
Active recombinant C-terminal His-tagged LgtC expressed in E. coli
Amino Acids
1-286
MW
33.4 kDa
Formulation (Request formulation change)
50 mM Tris HCl, pH 7.4, with 50 mM sodium chloride and 3 mM DTT
UniProt Accession №
Q93EK7
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    5 mg

    $435

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    Cayman Chemical
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    Product Description

    Lipopolysaccharide α-1,4-galactosyltransferase (LgtC) is a retaining glycosyltransferase and member of glycosyltransferase family 8 (GT8) that is found in N. meningitidis, an opportunistic bacterium that can cause meningitis.1 It is composed of an N-terminal mixed α/β domain, which contains the active site, and a C-terminal helical domain, which is responsible for attachment to cell membranes.2,3 LgtC transfers a galactosyl moiety from UDP-galactose (UDP-Gal) to the terminal lactose moiety on lipooligosaccharides (LOSs) while retaining the configuration of the donor sugar glycosidic bond.3 Isolated LgtC has been used in the analysis of newborn dried blood spots as a potential screening assay for galactosemia, an inborn error of metabolism characterized by a deficiency in galactose-1-phosphate uridylyltransferase (GALT), the enzyme that converts UDP-glucose to UDP-galactose.4 Cayman’s LgtC (N. meningitidis) protein can be used for biocatalysis and enzyme activity assay applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Ly, H.D., Lougheed, B., Wakarchuk, W.W., et al. Mechanistic studies of a retaining α-galactosyltransferase from Neisseria meningitidis. Biochemistry 41(16), 5075-5085 (2002).

    2. Chan, P.H.W., Weissbach, S., Okon, M., et al. Nuclear magnetic resonance spectral assignments of α-1,4-galactosyltransferase LgtC from Neisseria meningitidis: Substrate binding and multiple conformational states. Biochemistry 51(41), 8278-8292 (2012).

    3. Persson, K., Ly, H.D., Dieckelmann, M., et al. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat. Struct. Biol. 8(2), 166-175 (2001).

    4. Hong, X., Kumar, A.B., Scott, C.R., et al. Multiplex tandem mass spectrometry assay for newborn screening of X-linked adrenoleukodystrophy, biotinidase deficiency, and galactosemia with flexibility to assay other enzyme assays and biomarkers. Mol. Genet. Metab. 124(2), 101-108 (2018).