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S2076

Sigma-Aldrich

α-2,6-Sialyltransferase from Photobacterium damsela

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

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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
Enzyme Commission number:
MDL number:

recombinant

expressed in E. coli BL21

Quality Level

form

lyophilized powder

specific activity

≥5 units/mg protein

mol wt

56.8 kDa

shipped in

dry ice

storage temp.

−20°C

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This Item
S1951G7163A1031
α-Amylase from human saliva Type XIII-A, lyophilized powder, 300-1,500 units/mg protein

A1031

α-Amylase from human saliva

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous solution

form

lyophilized powder

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli

recombinant

-

mol wt

56.8 kDa

mol wt

46.4 kDa

mol wt

80 kDa

mol wt

-

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

shipped in

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

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


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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)
Nageswari Yarravarapu et al.
Bioconjugate chemistry, 33(5), 781-787 (2022-04-20)
Glycan binding often mediates extracellular macromolecular recognition events. Accurate characterization of these binding interactions can be difficult because of dissociation and scrambling that occur during purification and analysis steps. Use of photocrosslinking methods has been pursued to covalently capture glycan-dependent
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

Articles

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.

Review article and products for sialic acid synthesis and signaling.

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