Skip to Content

Dear Customer:

The current international situation is complex and volatile, and uncertain tariff policies may potentially impact our product prices. Given these uncertainties, we value your understanding regarding order-related matters.

If you decide to place an order during this period, we reserve the right to adjust the price based on the evolving situation. We understand that market changes may cause inconvenience. We will negotiate with you if there’s a significant price fluctuation due to tariff policy changes before the order’s actual delivery, and in such cases we may adjust or cancel the order as necessary.

Merck
CN
All Photos(2)

Key Documents

Safety Information

S1951

Sigma-Aldrich

α-2,3-Sialyltransferase from Pasteurella multocida

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

Synonym(s):

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

Sign Into View Organizational & Contract Pricing

Select a Size

20 G
CN¥1,672.57
100 G
CN¥6,760.74

CN¥1,672.57


Please contact Customer Service for Availability


Select a Size

Change View
20 G
CN¥1,672.57
100 G
CN¥6,760.74

About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

CN¥1,672.57


Please contact Customer Service for Availability

recombinant

expressed in E. coli BL21

Quality Level

form

lyophilized powder

specific activity

≥2 units/mg protein

mol wt

46.4 kDa

shipped in

dry ice

storage temp.

−20°C

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
S2076S1826C1999
specific activity

≥2 units/mg protein

specific activity

≥5 units/mg protein

specific activity

≥3.0 units/mg protein

specific activity

≥10 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized solid

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

mol wt

46.4 kDa

mol wt

56.8 kDa

mol wt

33.4 kDa

mol wt

26.0 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

General description

Sialyltransferases belongs to the glycosyltransferases family with the capability of catalyzing the transfer of N-acetylneuraminic acid residues.[1] It is a multifunctional enzyme with α-2,3-sialyltransferase activity, α-2,6-sialyltransferase activity, sialidase activity, and trans-sialidase activity.[2] It has a molar mass of 46.4 kDa, with pI, pH being 5.94 and 7.5-8.5 respectively.

Biochem/physiol Actions

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.[1]
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 1.0 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.

Physical form

Lyophilized powder containing Tris-HCl and NaCl

Preparation Note

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).

Analysis Note

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).

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Lisheng Ni et al.
Biochemistry, 45(7), 2139-2148 (2006-02-16)
Sialyltransferases catalyze reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated with galactose, N-acetylgalactosamine, or sialic acid). They are key enzymes that catalyze the synthesis of sialic acid-containing oligosaccharides, polysaccharides, and glycoconjugates that play
Vishwanath B Chachadi et al.
The international journal of biochemistry & cell biology, 43(4), 586-593 (2010-12-21)
Sialyl Lewis X is a tumor-associated antigen frequently found in the advanced cancers. However, the mechanism for the production of this cancer antigen is not entirely clear. The objective of this study is to examine whether epigenetics is involved in
Kevin M Schilling et al.
The Journal of organic chemistry, 85(3), 1687-1690 (2019-11-07)
Bacterially expressed proteins used in NMR studies lack glycans, and proteins from other organisms are neither 15N labeled nor glycosylated homogeneously. Here, we add two artificial glycans to uniformly 15N labeled prion protein using a buffer system that evolves over
Markus Sperandio
Annals of the New York Academy of Sciences, 1253, 201-205 (2012-01-20)
The ability of leukocytes to navigate through the different body compartments is an essential component for functioning immune defense and surveillance systems. In order to exit the blood circulation, leukocytes follow distinct recruitment steps, including capture of free-flowing leukocytes to
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

Articles

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

Enzymatic glycosyltransferase specificity challenges the one enzyme-one linkage concept.

Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service