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CMP-C9-azido-Sialic Acid (ammonium salt)

Name: CMP-C9-azido-Sialic Acid (ammonium salt)
Brand: eversyn®

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Synonyms: Cytidine-5'-monophospho-N-acetyl-9-azido-9-deoxy-neuraminic acid; CMP-N-acetyl-9-azidoneuraminic acid; CMP-Neu5Ac9Az; CMP-C9AzNeu5Ac; CMP-9Az-Neu5Ac; CMP-9´-Az-Neu5Ac, CMP-Neu5Ac9N3 (ammonium salt)

CAS No.: N/A

Related CAS No: 112037-53-3 (free acid)

Formula: C20H29N7O15PNH4

Molecular weight: 656.51 g/mol

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Technical Product Information

Other identifiers	Canonical SMILES: [N-]=[N+]=NCC(O)C(O)C1OC(OP(=O)(O)OCC2OC(N3C=CC(=NC3=O)N)C(O)C2O)(C(=O)O) CC(O)C1NC(=O)C Isomeric SMILES: O(P(OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N2C(=O)N=C(N)C=C2)(=O)O)[C@]3(C(O)=O)O[C@@]([C@@H]([C@@H](CN=[N+]=[N-])O)O)([C@H](NC(C)=O)[C@@H](O)C3)[H] InChI Key: YZOBTNNKILRMMB-BILDWYJOSA-N
Description	CMP-Neu5Ac9N3 is an advanced sialic acid nucleotide sugar analog featuring an azide group at the C9 position. The product is designed for research use in bioorthogonal, click-chemistry-based glycoengineering, and selective labeling of glycans. Key features: Enables highly selective enzymatic transfer by different sialyltransferases (e.g., ST6Gal1, bacterial 2,6SiaT, 2,3SiaT), allowing flexible application on diverse glycans. Incorporates a bioorthogonal azide handle for click chemistry reactions (e.g., conjugation of fluorophores, toxins, imaging agents, or affinity probes), without disrupting native glycan function. Applicable in both cell-based and in vitro glycoengineering settings. The product is for research use only, not for use in diagnostic procedures.
Appearance	Lyophilized white powder
Purity	≥ 95% (HPLC-UV). Product has not been tested for endotoxins.
Storage	At -20°C.

Applications (Research Use Only)

Biotherapeutics & Drug Conjugation

Development of site-specific antibody-drug conjugate (ADC), peptide-drug conjugate (PDC), and glycoconjugate vaccine via selective glycan remodeling, enabling homogeneous drug attachment and optimized pharmacokinetics

Generation of novel bioconjugates including labeled antibodies, engineered glycoproteins, or functionalized exosomes for targeted delivery or imaging studies.

Cellular and Molecular Biology

Live cell glycan labeling for imaging, proteomics, and flow cytometry using click chemistry with alkyne-modified probes.

Mechanistic studies of glycosylation, glycan-protein interactions including Siglecs (Sialic acid-binding Immunoglobulin-like Lectins), and cell-surface glycan mapping.

Antimicrobial Prophylaxis

Investigational use as a topical agent for reducing pathogenic colonization (e.g., N. gonorrhoeae), with efficacy shown in preclinical mouse models.

Analytical Research

Exo-enzymatic glycan engineering of exosomes and nanoparticles for functionalization and delivery research.

Sialoglycan spin labeling for structural biology and electron paramagnetic resonance (EPR) spectroscopy studies.

All applications listed above are intended exclusively for research use only and are not for use in diagnostic procedures.

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References

1. Thames, A. H.; Moons, S. J.; Wong, D. A.; Boltje, T. J.; Bochner, B. S.; Jewett, M. C., GlycoCAP: A Cell-Free, Bacterial Glycosylation Platform for Building Clickable Azido-Sialoglycoproteins. ACS Synth Biol 2023, 12 (4), 1264-1274.

2. Yang, G.-Y.; Li, C.; Fischer, M.; Cairo, C. W.; Feng, Y.; Withers, S. G., A FRET Probe for Cell-Based Imaging of Ganglioside-Processing Enzyme Activity and High-Throughput Screening. Angew Chem Int Ed 2015, 54 (18), 5389-5393.

3. Mbua, N. E.; Li, X.; Flanagan-Steet, H. R.; Meng, L.; Aoki, K.; Moremen, K. W.; Wolfert, M. A.; Steet, R.; Boons, G.-J., Selective Exo-Enzymatic Labeling of N-Glycans on the Surface of Living Cells by Recombinant ST6Gal I. Angew Chem Int Ed 2013, 52 (49), 13012-13015.

4. Hosoguchi, K.; Maeda, T.; Furukawa, J.; Shinohara, Y.; Hinou, H.; Sekiguchi, M.; Togame, H.; Takemoto, H.; Kondo, H.; Nishimura, S., An efficient approach to the discovery of potent inhibitors against glycosyltransferases. J Med Chem 2010, 53 (15), 5607-19.