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Merck
모든 사진(2)

주요 문서

S2076

Sigma-Aldrich

α-2,6-Sialyltransferase from Photobacterium damsela

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

동의어(들):

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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1 UNIT
₩842,653

₩842,653


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1 UNIT
₩842,653

About This Item

효소 위원회 번호:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

₩842,653


구입 가능 여부는 고객센터에 문의하십시오.

재조합

expressed in E. coli BL21

Quality Level

양식

lyophilized powder

특이 활성도

≥5 units/mg protein

분자량

56.8 kDa

배송 상태

dry ice

저장 온도

−20°C

관련 카테고리

일반 설명

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

애플리케이션

α-2,6-Sialyltransferase from Photobacterium damsela has been used in resialylation and restoration of sialic acids (SAs) in HRT-18G cells.[2]
Highly active α2-6 sialyltransferase has been used to prepare high levels of disialylated fragment crystals. [3]

생화학적/생리학적 작용

Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
The terminal step of complex N-glycan biosynthesis is catalysed by α-2,6-sialyltransferase (STs).[1] Bacterial α(2,6)-STs possesses broader acceptor substrate specificity when compared to eukaryotic α(2,6)-STs.[4]

단위 정의

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.

물리적 형태

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

분석 메모

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

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
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
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
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)
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)

문서

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.

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