关键信息
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基因名
GALNT7
- 应用
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别名
GALNT7；N-acetylgalactosaminyltransferase 7
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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
Q86SF2
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表达区间
30-657aa
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氨基酸序列
PRPDDPSPLSRMREDRDVNDPMPNRGGNGLAPGEDRFKPVVPWPHVEGVE VDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTFTYHDPVLRP GILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVA SDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHS VIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREG LIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPL IDVINGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTPQEKRLRKTKT EPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGK LLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDY FYASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPP KNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQL MQYDQCLTKGADGSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRS EVLHQVFISNCDSSKTTQKWEMNNIHSVVDHHHHHH
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分子量
73 kDa
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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.
质检流程
相关产品
背景信息
GALNT7, a member of the glycosyltransferase family, plays a crucial role in the biosynthesis of mucin-type O-glycans. These glycans are essential for various biological processes, including cell signaling, adhesion, and immune response. Recent studies have highlighted the significance of GALNT7 in various diseases, including cancer, where it has been implicated in tumor progression and metastasis. The enzyme catalyzes the first step in the O-glycosylation process by transferring N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins. Understanding the structural and functional characteristics of GALNT7 has become increasingly important for elucidating its role in health and disease. Recombinant GALNT7 protein production has emerged as a vital approach to investigate its enzymatic activity, substrate specificity, and interaction with other cellular components. The characterization of GALNT7 through recombinant technology not only enhances our understanding of O-glycosylation mechanisms but also opens avenues for potential therapeutic applications, particularly in targeting glycosylation patterns in cancer treatment. As researchers continue to explore the complexities of glycosylation, GALNT7 stands out as a key enzyme that could provide insights into novel biomarker development and drug design, emphasizing the need for continued investigation into its biology and clinical significance.
