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S1951

Sigma-Aldrich

α-2,3-Sialyltransferase from Pasteurella multocida

recombinant, expressed in E. coli BL21, ≥2 units/mg protein

Synonym(e):

CMP-N-acetylneuraminate:β-D-galactoside α-(2,3)-N-acetylneuraminyltransferase

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About This Item

EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli BL21

Qualitätsniveau

Form

lyophilized powder

Spezifische Aktivität

≥2 units/mg protein

Mol-Gew.

46.4 kDa

Versandbedingung

dry ice

Lagertemp.

−20°C

Allgemeine Beschreibung

Sialyltransferases belongs to the glycosyltransferases family with the capability of catalyzing the transfer of N-acetylneuraminic acid residues. It is a multifunctional enzyme with α-2,3-sialyltransferase activity, α-2,6-sialyltransferase activity, sialidase activity, and trans-sialidase activity. It has a molar mass of 46.4 kDa, with pI, pH being 5.94 and 7.5-8.5 respectively.

Biochem./physiol. Wirkung

Sialyltransferase catalyzes the transfer of Neu5Ac from CMP-Neu5Ac as a donor substrate to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Einheitendefinition

One unit will catalyze the formation of 1.0 μmol Neu-5-Ac-α-2,3LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Physikalische Form

Lyophilized powder containing Tris-HCl and NaCl

Angaben zur Herstellung

Reconstitute the lyophilized powder with a volume of water in the range of 0.1 mL to 1 mL, to give a concentration in the range of 1 unit/mL (1 mL volume of water) to 10 units/mL (0.1 mL volume of water).

Hinweis zur Analyse

Enzymatic activity assays performed in Tris-HCl buffer (100 mM, pH 8.0) containing CMP-Neu-5Ac (1 mM) and Lac-β−OMU (1 mM) at 37°C for 30 min and analyzed using HPLC with a fluorescence detector (excitation at 325 nm and emission at 372 nm).

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Peng Zhang et al.
Bipolar disorders, 12(8), 786-792 (2010-12-24)
Multiple linkage and association studies have suggested chromosome 8q24 as a promising candidate region for bipolar disorder (BP). We performed a detailed association analysis assessing the contribution of common genetic variation in this region to the risk of BP. We
E V Chandrasekaran et al.
Journal of proteome research, 11(4), 2609-2618 (2012-02-15)
Our previous studies suggest that the α2,3sialylated T-antigen (NeuAcα2,3Galβ1,3GalNac-) and associated glycan structures are likely to be elevated during cancer. An easy and reliable strategy to label mucinous glycans that contain such carbohydrates can enable the identification of novel glycoproteins
Yoshimitsu Kakuta et al.
Glycobiology, 18(1), 66-73 (2007-10-27)
Sialyltransferases are a family of glycosyltransferases that catalyze the transfer of N-acetylneuraminic acid residues from cytidine monophosphate N-acetylneuraminic acid (CMP-NeuAc) as a donor substrate to the carbohydrate groups of glycoproteins and glycolipids as acceptor substrates. We determined the crystal structure
Sung-Wook Son et al.
Biochemical and biophysical research communications, 414(1), 159-164 (2011-09-29)
In this study we investigated for the first time the transcriptional regulation of pig Galβ1,3GalNAc α2,3-sialyltransferase (pST3Gal I) in response to TGF-β1 in porcine kidney PK-15 cells. The pST3Gal I gene was found to span about 90kb and to be
Vireak Thon et al.
Applied microbiology and biotechnology, 94(4), 977-985 (2011-11-15)
Pasteurella multocida (Pm) strain Pm70 has three putative sialyltransferase genes including Pm0188, Pm0508, and Pm1174. A Pm0188 gene homolog in Pm strain P-1059 encodes a multifunctional α2-3-sialyltransferase, PmST1, that prefers oligosaccharide acceptors. A Pm0508 gene homolog in the same strain

Artikel

Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some nucleoside mono- or diphosphate sugar donors.

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