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S2076

Sigma-Aldrich

α-2,6-Sialyltransferase from Photobacterium damsela

recombinant, expressed in E. coli BL21, ≥5 units/mg protein

Synonym(s):

β-Galactoside α-2,6-sialyltransferase, CMP-N-Acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase

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About This Item

Enzyme Commission number:
2.4.99.1 (BRENDA, IUBMB)
MDL number:
MFCD00132245
UNSPSC Code:
12352204

recombinant

expressed in E. coli BL21

Quality Level

200

form

lyophilized powder

specific activity

≥5 units/mg protein

mol wt

56.8 kDa

shipped in

dry ice

storage temp.

−20°C

Related Categories

General description

Human ST6Gal-I (β-galactoside α-2,6-sialyltransferase 1) is a member of the CAZy family GT29.

Application

α-2,6-Sialyltransferase from Photobacterium damsela has been used in resialylation and restoration of sialic acids (SAs) in HRT-18G cells.
Highly active α2-6 sialyltransferase has been used to prepare high levels of disialylated fragment crystals.

Biochem/physiol Actions

The terminal step of complex N-glycan biosynthesis is catalysed by α-2,6-sialyltransferase (STs). Bacterial α(2,6)-STs possesses broader acceptor substrate specificity when compared to eukaryotic α(2,6)-STs.
Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Unit Definition

One unit will catalyze the formation of 1 μmol Neu-5-Ac-α-2,6-LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Physical form

Supplied as a lyophilized powder containing Tris-HCl and NaCl.

Analysis Note

Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 8.0) containing CMP-Neu-5-Ac (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).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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High-quality production of human alpha-2, 6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities
Ribitsch D, et al.
Microbial cell factories, 13, 138-138 (2014)
Jung-Jin Park et al.
Biochemical pharmacology, 83(7), 849-857 (2012-01-24)
β-Galactoside α2,6-sialyltransferase (ST6Gal-I) has been shown to catalyze α2,6 sialylation of N-glycan, an action that is highly correlated with colon cancer progression and metastasis. We have recently demonstrated that ST6Gal-I-induced α2,6 sialylation is critical for adhesion and migration of colon
Tatsuya Kato et al.
Journal of bioscience and bioengineering, 113(6), 694-696 (2012-02-09)
Modified polyhedrin promoter (Ppolh) was designed by repeating burst sequences (BSs) and adopted to overexpress rat α2,6-sialyltransferase (ST6Gal I) in silkworm. Modified Ppolh of five BSs with VLF-1 coexpression yielded 2.9 U/ml ST6Gal I activity and 32.5 mU/mg specific activity
Miyako Nakano et al.
Molecular & cellular proteomics : MCP, 10(11), M111-M111 (2011-08-24)
Resistance to tubulin-binding agents used in cancer is often multifactorial and can include changes in drug accumulation and modified expression of tubulin isotypes. Glycans on cell membrane proteins play important roles in many cellular processes such as recognition and apoptosis
Enhanced Bacterial alpha (2, 6)-Sialyltransferase Reaction through an Inhibition of Its Inherent Sialidase Activity by Dephosphorylation of Cytidine-5'-Monophosphate
Kang JY, et al.
PLoS ONE, 10(7), e0133739-e0133739 (2015)
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Articles

Glycosyltransferases

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.

Sialic Acid

Review article and products for sialic acid synthesis and signaling.

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