Analytical Data
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基因名
ST6GALNAC2
- Application
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别名
ST6GALNAC2；SIAT7B；Alpha-N-acetylgalactosaminide alpha-2.6-sialyltransferase 2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UJ37
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表达区间
1-374aa
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氨基酸序列
MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAF FQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPA LWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIR CAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFT VNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVP EGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDL YMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYAN HDLSLEAALWRDLHKAGILQLYQR
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
ST6GALNAC2 is a member of the sialyltransferase family, playing a critical role in the biosynthesis of glycan structures on glycoproteins and glycolipids. Sialylation, the addition of sialic acid to these glycoconjugates, is pivotal for various biological processes, including cell-cell recognition, immune response modulation, and tumor progression. Dysfunctional sialylation has been implicated in several diseases, particularly cancer, where altered glycosylation patterns can influence tumor aggressiveness and metastasis. Research on the recombinant protein ST6GALNAC2 is increasingly relevant due to its potential applications in therapeutic strategies aimed at targeting aberrant sialylation in tumors. By producing ST6GALNAC2 as a recombinant protein, scientists can study its enzymatic activity, substrate specificity, and role in pathological conditions. This knowledge could pave the way for the development of novel biomarker assays and therapeutics that manipulate sialylation patterns for improved cancer diagnosis and treatment. Additionally, understanding the molecular mechanisms regulated by ST6GALNAC2 may provide insights into its functional significance in both normal physiology and disease states. Ongoing studies are likely to uncover the diverse roles of this enzyme, highlighting its importance in glycomics and its potential as a target in precision medicine. As research advancements continue, ST6GALNAC2 could offer new avenues for innovative approaches to combat diseases associated with aberrant glycosylation.
