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Merck
CN

S2076

α-2,6-唾液酸转移酶 来源于美人鱼发光杆菌

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

别名:

β-半乳糖苷-α-2,6-唾液酸转移酶, CMP-N-乙酰神经氨酸酯：β-D-半乳糖基-1,4-N-乙酰基-β-D-葡糖胺-α-2,6-N-乙酰神经氨酸转移酶

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关于此项目

UNSPSC Code:
12352204
NACRES:
NA.54
EC 号:
2.4.99.1 (BRENDA, IUBMB)
MDL number:
MFCD00132245

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产品名称

α-2,6-唾液酸转移酶 来源于美人鱼发光杆菌, recombinant, expressed in E. coli BL21, ≥5 units/mg protein

recombinant

expressed in E. coli BL21

form

lyophilized powder

specific activity

≥5 units/mg protein

mol wt

56.8 kDa

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

相关类别

Other Notes

在37℃，pH8.0条件下，一个单位每分钟可催化由CMP-Neu-5-Ac和Lac-β-OMU形成1 μmol Neu-5-Ac-α -2,6-LacMU。

Analysis Note

酶活性测定在含有CMP-Neu-5-Ac（1 mM）和Lac-β−OMU（1 mM）的Tris-HCl缓冲液（100 mM，pH 8.0）中于37°C进行30分钟，并使用带有荧光检测器（激发波长325nm，发射波长372nm）的HPLC进行分析。

Application

α来自美人鱼发光杆菌（Photobacterium damsela） 的-2,6-唾液酸转移酶已被用于HRT-18G细胞中唾液酸（SA）的再唾液酸化（resialylation）和恢复。
高活性α 2-6唾液酸转移酶已用于制备高级别的的二唾液酸化片段晶体。

Biochem/physiol Actions

α复杂的N-聚糖生物合成的最终步骤是由-2,6-唾液酸转移酶（ST）催化。与真核生物α（2,6）-ST相比，细菌α（2,6）-ST具有更广泛的受体底物特异性。
唾液酸转移酶可将Neu5Ac从CMP-Neu5Ac转移至受体分子（包括糖蛋白、糖脂和寡糖）的半乳糖基末端。

General description

人ST6Gal-1（β半乳糖苷α-2,6-唾液酸转移酶1）是CAZy家族GT29的成员。

Physical form

以含有Tris-HCl和NaCl的冻干粉末形式提供。

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
0000415709
0000415709
0000356578
0000318578
0000356578

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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
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)
Masayoshi Onitsuka et al.
Applied microbiology and biotechnology, 94(1), 69-80 (2011-12-30)
Improvement of glycosylation is one of the most important topics in the industrial production of therapeutic antibodies. We have focused on terminal sialylation with alpha-2,6 linkage, which is crucial for anti-inflammatory activity. In the present study, we have successfully cloned
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