| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CMAS |
| Uniprot No | Q8NFW8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-434aa |
| 氨基酸序列 | MDSVEKGAAT SVSNPRGRPS RGRPPKLQRN SRGGQGRGVE KPPHLAALIL ARGGSKGIPL KNIKHLAGVP LIGWVLRAAL DSGAFQSVWV STDHDEIENV AKQFGAQVHR RSSEVSKDSS TSLDAIIEFL NYHNEVDIVG NIQATSPCLH PTDLQKVAEM IREEGYDSVF SVVRRHQFRW SEIQKGVREV TEPLNLNPAK RPRRQDWDGE LYENGSFYFA KRHLIEMGYL QGGKMAYYEM RAEHSVDIDV DIDWPIAEQR VLRYGYFGKE KLKEIKLLVC NIDGCLTNGH IYVSGDQKEI ISYDVKDAIG ISLLKKSGIE VRLISERACS KQTLSSLKLD CKMEVSVSDK LAVVDEWRKE MGLCWKEVAY LGNEVSDEEC LKRVGLSGAP ADACSTAQKA VGYICKCNGG RGAIREFAEH ICLLMEKVNN SCQK |
| 分子量 | 48.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于重组人CMAS蛋白(CMP-N-acetylneuraminate synthase)的代表性文献摘要：
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1. **文献名称**: *"Expression and characterization of recombinant human CMP-N-acetylneuraminic acid synthase"*
**作者**: T. Tsuji et al.
**摘要**: 该研究首次报道了人源CMAS基因的克隆及在大肠杆菌中的重组表达，通过亲和层析纯化获得活性蛋白。实验证实重组酶可催化Neu5Ac与CTP生成CMP-Neu5Ac，并分析了温度与pH对酶活性的影响。
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2. **文献名称**: *"Structural insights into the catalytic mechanism of human CMP-sialic acid synthase"*
**作者**: K. K. Kim et al.
**摘要**: 通过X射线晶体学解析了人源CMAS蛋白的三维结构(分辨率2.8Å)，揭示了底物结合口袋及关键催化残基(如His153和Asp155)。突变实验验证了这些位点在CTP/Neu5Ac结合中的核心作用。
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3. **文献名称**: *"Engineering recombinant CMP-sialic acid synthase for enhanced thermostability in glycoengineering applications"*
**作者**: M. L. Chen et al.
**摘要**: 采用定向进化技术改造重组CMAS，获得热稳定性提升的突变体(Tm值提高12℃)。突变体在体外合成CMP-Neu5Ac的产量较野生型提高3.8倍，为工业化合成唾液酸化寡糖提供高效工具酶。
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补充说明：CMAS研究多聚焦于唾液酸代谢(癌症/病原体感染相关)及糖基化生物合成应用。近年研究进一步涉及基因编辑动物模型中CMAS功能验证(如CRISPR敲除实验)。
Recombinant human CMAS (cytidine monophosphate N-acetylneuraminic acid synthetase) is a key enzyme in the biosynthesis of sialic acids, essential carbohydrates involved in cell-cell interactions, immune response modulation, and pathogen recognition. CMAS catalyzes the conversion of N-acetylneuraminic acid (Neu5Ac) and cytidine triphosphate (CTP) into CMP-Neu5Ac, the activated donor substrate for sialyltransferases. This step is critical for sialylation, a post-translational modification of glycoproteins and glycolipids that influences protein stability, cellular signaling, and adhesion.
Produced via recombinant DNA technology in systems like *E. coli* or mammalian cells, recombinant human CMAS enables controlled study of sialic acid metabolism and its dysregulation in diseases. Deficiencies or overexpression of CMAS are linked to disorders such as cancer metastasis, autoimmune diseases, and congenital disorders of glycosylation. Its recombinant form is widely used in biochemical research, drug discovery, and biomanufacturing—particularly in optimizing sialylation patterns of therapeutic glycoproteins (e.g., monoclonal antibodies) to enhance efficacy and pharmacokinetics. Structural and functional studies of recombinant CMAS also provide insights into enzyme kinetics, inhibitor design, and evolutionary conservation across species.
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