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Sialic Acids

Sialic Acids are a family of nine-carbon monosaccarides that are commonly found as terminal residues of glycan chains on cell surface glycoproteins and glycolipids.
They play crucial roles in diverse biological processes, including cell-cell recognition, adhesion, and signaling.
Sialic Acids exhibit structural diversity and can undergo various modifications, influencing their functional properties.
Reserarch into Sialic Acid biology and their applications in areas such as cancer, immunology, and neurodegeeration continues to be an active field of study.

Most cited protocols related to «Sialic Acids»

1
Sandwich ELISA for Gd-IgA1 Quantification
Cited 9 times
A sandwich ELISA for Gd-IgA1 was constructed using KM55. KM55 was immobilized at 7.5 µg/mL on 96-well ELISA plates (NUNC MaxiSorp; Thermo Fisher Scientific, MA) for 18 h at room temperature. This was followed by blocking with phosphate-buffered saline (PBS) containing 1% bovine serum albumin (BSA) for 2 h at room temperature. Serum samples were diluted in proportions of 1:50 with sodium acetate buffer (pH5.0) and desialylated by treatment with neuraminidase for 3 h at 37°C. After washing five times with PBS containing 0.05% Tween-20 (PBST), desialylated serum samples diluted with fetal bovine serum (1:5 dilution) were incubated on KM55-coated plates for 2 h at room temperature. Plates were washed and incubated in 1:1000 dilution with HRP-conjugated mouse anti-human IgA1 α1 chain-specific monoclonal antibody (SouthernBiotech, AL) for 2 h at room temperature. After washing, plates were eventually colored by SIGMAFAST O-phenylenediamine (OPD) solution (Sigma-Aldrich Japan) and stopped by 1 mol/L sulfuric acid (Wako, Osaka, Japan). The levels of each serum Gd-IgA1 were extrapolated by referring to a standard curve (4-parameter logistic curve fitting) of optical density (OD) (492 nm) and expressed as units. Enzymatically generated Gd-IgA1 from human plasma IgA1 was serially diluted (1.37–1000 ng/mL) and used as standards. In this study, 1 unit was defined as 1 µg/mL of enzymatically generated Gd-IgA1.
In the present study, serum samples were desialylated by treatment with neuraminidase, similar to the serum sample preparation in HAA lectin-based assay. Neuraminidase treatment has been conventionally performed because of the following reasons: (i) the existence of sialic acids on GalNAc might affect the recognition of serum Gd-IgA1 by HAA lectin and (ii) the pattern and number of sialic acids on the hinge region of IgA1 possibly vary among individuals. Unlike HAA lectin-based assay, neuraminidase treatment of serum samples was performed before adding to KM55 pre-coated plates to avoid detachment of KM55 due to the acidic condition.
Yasutake J., Suzuki Y., Suzuki H., Hiura N., Yanagawa H., Makita Y., Kaneko E, & Tomino Y. (2015). Novel lectin-independent approach to detect galactose-deficient IgA1 in IgA nephropathy. Nephrology Dialysis Transplantation, 30(8), 1315-1321.
Publication 2015
1,2-diaminobenzene Acids Antibodies, Anti-Idiotypic Biological Assay Enzyme-Linked Immunosorbent Assay Fetal Bovine Serum galactosyl-deficient IgA1 Homo sapiens IgA1 Lectin Mice, House Neuraminidase Phosphates Plasma Saline Solution Serum Serum Albumin, Bovine Sialic Acids Sodium Acetate Specimen Handling Sulfuric Acids Technique, Dilution Tween 20
2
IgG Glycan Analysis by Fluorescent Labeling
Cited 8 times

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Publication 2014
Acrylamide APT Electrophoresis Exoglycosidases Homo sapiens Mannose Polysaccharides Sialic Acids
3
N-Glycan Structural Characterization by Mass Spectrometry
Cited 4 times
After MS data acquisition, spectra were imported to SCiLS Lab 2017a and 2020a imaging software for analysis of the mass range m/z 500 to 4000. SCiLS-generated N-glycan spectra were normalized to the total ion count (ICR Noise Reduction Threshold = 0.95), which were then matched within ±5 ppm against an in-house database of known N-glycans generated using GlycoWorkbench and GlycoMod for annotation (22 ). N-glycan structures annotated in this article are compositionally accurate as determined by accurate mass and through prior structural characterizations by both MALDI–TOF–MS/MS and reversed-phase liquid chromatography-coupled tandem mass spectrometry (23 ). Annotated collision-induced dissociation spectra for 23 common core N-glycan structures in this report are included in Supplemental Materials. Additional isomeric configurations were confirmed by complementary analyses with core fucose-specific Endo F3 and stabilization of sialic acids by amidation. A list of all N-glycans reported in this analysis along with mass error calculations and representative structures can be found in supplemental Tables S2 and S3.
McDowell C.T., Klamer Z., Hall J., West C.A., Wisniewski L., Powers T.W., Angel P.M., Mehta A.S., Lewin D.N., Haab B.B, & Drake R.R. (2020). Imaging Mass Spectrometry and Lectin Analysis of N-Linked Glycans in Carbohydrate Antigen–Defined Pancreatic Cancer Tissues. Molecular & Cellular Proteomics : MCP, 20, 100012.
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Publication 2020
Chromatography, Reversed-Phase Liquid Endometriosis Fucose Isomerism Polysaccharides Sialic Acids Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tandem Mass Spectrometry
4
Sialic Acid Linkage-Specific Derivatization
Cited 4 times
Sialic acid linkage-specific derivatization by ethyl esterification was performed as described previously12 (link). Briefly, 1 µL of released plasma N-glycans (containing the released glycans from 0.2 µL of plasma) was added to 20 µL ethyl esterification reagent (250 mM EDC and 250 mM HOBt in EtOH) and incubated for 1 h at 37 °C. Subsequently, 20 µL MeCN was added and N-glycans were purified by cotton HILIC SPE as described before12 (link),29 (link). Samples were eluted in 10 µL MQ. In addition, an amidation step was introduced in the protocol, for the robust stabilization of the α2,3-linked sialic acids, by adding 4, 6 or 8 µL of 28% NH4OH to the reaction mixture after 1 h incubation. The addition of the ammonia was followed by an incubation step of 2 h at 37 °C. After incubation, 24, 26 or 28 µL MeCN was added to the mixture and the N-glycans were purified by cotton HILIC SPE, with an elution in 10 µL MQ. The optimized ethyl esterification protocol with amidation step (EEA) used 4 µL of 28% NH4OH solution. Furthermore, another option for the linkage-specific derivatization of the sialic acids was investigated, in which the sialic acids were differentially modified by double amidation (DA), as described previously11 (link). Briefly, 1 µL of released plasma N-glycans was added to 20 µL dimethylamidation reagent (250 mM dimethylamine, 250 mM EDC and 500 mM HOBt and in DMSO) and incubated for 1 h at 60 °C. An additional incubation followed of 2 h at 60 °C after the addition of 8 µL 28% NH4OH. Eighty microlitres of MeCN was added to the samples and the derivatized N-glycans were purified by cotton HILIC SPE, with elution in 10 µL MQ.
Lageveen-Kammeijer G.S., de Haan N., Mohaupt P., Wagt S., Filius M., Nouta J., Falck D, & Wuhrer M. (2019). Highly sensitive CE-ESI-MS analysis of N-glycans from complex biological samples. Nature Communications, 10, 2137.
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Publication 2019
1-hydroxybenzotriazole Ammonia dimethylamine Esterification Ethanol Gossypium N-Acetylneuraminic Acid Plasma Polysaccharides Sialic Acids Sulfoxide, Dimethyl
5
Optimized N-Glycan Methylamidation and Purification
Cited 4 times
N-Glycans were enzymatically cleaved from standard and serum glycoproteins with PNGase F and purified.35 (link) For methylamidation of sialic acids on N-glycans,49 (link) we modified the protocol to minimize sample loss and maximize purity. Dried samples of sialyllactose (0.5 μg) and N-glycans derived from serum and standard glycoproteins were dissolved in 5 μL of dimethyl sulfoxide (DMSO) containing 2 M methylamine hydrochloride and 1 M 4-methylmorpholine. Subsequently, 5 μL of 100 mM (7-azabenzotriazol-1-yloxy)tripyrrolidinophosphonium hexafluorophosphate (PyAOP) in DMSO was added to these samples. The reaction proceeded for 60 min under ambient conditions and was quenched with 240 μL of an 85:15 acetonitrile (ACN)/H2O solution, and the N-glycans were purified with amino (NH2) micro-spin columns. Briefly, micro-spin columns were conditioned with three 300-μL aliquots of a solution composed of H2O/ACN/TFA (95:5:0.1) and equilibrated with three 300-μL aliquots of the 85:15 ACN/H2O solution. The samples were loaded onto the columns, the columns were centrifuged, the sample solution was collected in microcentrifuge tubes and reloaded onto the columns, and the entire process was repeated. The samples were washed with two 200-μL aliquots of the 85:15 ACN/H2O solution and finally eluted with 300-μL of a 20:80 ACN/H2O solution. Samples requiring no further treatment or derivatization were labeled with APTS48 by established procedures29 (link) to impart a negative charge for electrophoresis and a fluorescent tag for detection.
Mitra I., Snyder C.M., Zhou X., Campos M.I., Alley WR J.r., Novotny M.V, & Jacobson S.C. (2016). Structural Characterization of Serum N-Glycans by Methylamidation, Fluorescent Labeling, and Analysis by Microchip Electrophoresis. Analytical chemistry, 88(18), 8965-8971.
Publication 2016
acetonitrile Electrophoresis Glycopeptidase F Glycoproteins methylamine hydrochloride N-acetylneuraminoyllactose Polysaccharides Serum Sialic Acids Sulfoxide, Dimethyl

Most recents protocols related to «Sialic Acids»

1
Antibody Purity and Identity Analysis
Not available on PMC !

Example 5

Non-reducing and reducing SDS-PAGE is used to analyze purity and identity of an antibody. The band pattern in non-reducing gels shows the major band at about 160 kDa and methodical artefacts of heavy and light chains and combinations thereof (˜25, 50-55, 75, 110, 135 kDa). Reducing gels show distinct light and heavy chain bands at and 50-55 kDa. Due to lack of the Fab glycosylation PM-N54Q has a smaller heavy chain, as expected (see FIG. 4, right).

The charge profile is clearly different, as shown by isoelectric focusing (IEF; see FIG. 5). The Fab glycosylation is considerably sialylated, whereas the Fc glycosylation is only minimally sialylated. Thus PankoMab-GEX® has more charged isoforms than PM-N54Q, reflecting its higher level of negatively charged sialic acids in the Fab part.

US11872289B2. Anti-MUC1 antibody-drug conjugate (2024-01-16). DAIICHI SANKYO CO., LTD. [JP]. Inventors: Johanna Gellert [DE], Anke Flechner [DE], Doreen Weigelt [DE], Antje Danielczyk [DE], Akiko Nagase [JP].
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Patent 2024
Gels Glycosylation Immunoglobulins Light PankoMab-GEX Protein Isoforms SDS-PAGE Sialic Acids
2
Comprehensive Analysis of IgG N-Glycopeptides
The database search was performed with Byonic v4.5.2 (Protein Metrics, Cupertino, California, USA), a search engine specialized in the identification of glycopeptides. Considering the high apparent purity of the captured IgG samples based on the SDS-PAGE results (Supplementary Fig. S13), the samples were searched against a simplified database containing only the immunoglobulin sequences from IMGT RefSeq as described above. Decoys were added to the protein database. The N-glycan database used was based on the Byonic built-in database of 309 mammalian N-glycans. The default database was expanded to include complex and hybrid glycan antennae of N, N′-diacetyllactosamine (LacdiNAc) and all combinations of LacdiNAc and N-acetyllactosamine (LacNAc). To confirm which types of sialic acid to include into the glycan database, we verified MS2 chromatographic traces and spectra of relevant 0.5 d colostrum and 28 d mature milk samples from raw files resulting from methods employing higher-energy collisional dissociation. Supplementary Fig. S15 shows oxonium ion evidence for various sialic acids, including unmodified and acetylated N-acetylneuraminic acid (NeuAc), unmodified and acetylated N-glycolylneuraminic acid (NeuGc), and unmodified deaminated neuraminic acid (Kdn). The occurrence of NeuAc and NeuGc was undeniably confirmed, and they were found to overlap with oxonium ions derived from HexNAc residues. Acetylated residues and Kdn, however, could not be detected above noise levels. Based on this information, the database was expanded to include sialylation with both NeuAc and the non-human NeuGc, as well as all combinations thereof. The resulting database containing a total of 2440 N-glycan compositions that were used for identifying the IgG N-glycopeptides, is shown in Supplementary Table S3. Default search parameters were used, unless otherwise specified. Tryptic cleavage sites were defined C-terminal of arginine and lysine residues with two missed cleavages, but digestion specificity was set to non-specific. Fragmentation type was set either to HCD for the samples analyzed with HCD or product ion-triggered stepping HCD, or to both HCD & EThcD for the samples analyzed with product ion-triggered EThcD. Cysteine carbamidomethylation was set as a fixed modification. Methionine and tryptophan oxidation, and N-terminal cyclization of glutamine and glutamic acid to pyroglutamic acid were all searched as rare variable modifications, whereas N-glycosylation was searched as a common variable modification. A maximum of one rare and one common variable modifications were allowed per peptide. Protein false discovery rate (FDR) was set to 1 percent or 20 reverse counts. Further post-processing included filtering of the data based on |Log Prob| ≥ 1 and score ≥ 150. Based on the identified glycan composition, proposed glycan structures were built using GlycoWorkBench 2.1 build 146, according to the symbol nomenclature for glycan representation of the Consortium for Functional Glycomics (Varki et al. 2009 (link)).
Gazi I., Reiding K.R., Groeneveld A., Bastiaans J., Huppertz T, & Heck A.J. (2023). Key changes in bovine milk immunoglobulin G during lactation: NeuAc sialylation is a hallmark of colostrum immunoglobulin G N-glycosylation. Glycobiology, 33(2), 115-125.
Publication 2023
Acids Arginine Chromatography Colostrum Cyclization Cysteine Cytokinesis Digestion Glutamic Acid Glutamine Glycopeptides Homo sapiens Hybrids hydronium ion Immunoglobulins Lysine Mammals Methionine Milk, Cow's N-acetylgalactosaminyl-1-4-N-acetylglucosamine N-acetyllactosamine N-Acetylneuraminic Acid Peptides Polysaccharides Protein Glycosylation Proteins Pyrrolidonecarboxylic Acid SDS-PAGE Sialic Acids Strains Trypsin Tryptophan
3
Screening Glucoside Hydrolases for Glycan Digestion
Ten glucoside hydrolases were screened regarding their ability to digest APTS-labeled maltodextrins and dextrans under different reaction conditions, i.e., buffers. Tested glucoside hydrolases were: α-amylase II-A (0.15 U/μL), α-amylase IX-A (1 U/μL), α-amylase XIII-A (1 U/μL), α-glucosidase (1 U/μL), β-amylase (1 U/μL), oligo-1,6-glucosidase (1 U/μL), oligo-α-(1,4-1,6)-glucosidase (1 U/μL), GAP (0.17 U/μL and 0.017 U/μL), DxPsp (0.5 U/μL), and DxChe (activity unknown). Overall, the pH ranges and optima for the tested enzymes’ activities varied from acidic (pH 3) to neutral (pH 6.9) conditions according to the manufacturer’s information. To exclude the loss of acid labile sialic acids from N-glycans, we tested six digestion buffers in less acidic to neutral range: WS0049 (pH 6.6), WS0095 (pH 5), WS0122 (pH 6), disodium phosphate-citrate buffer at pH 5 and 7, and potassium phosphate buffer at pH 6.
The reaction setup was as follows: All ten glucoside hydrolases were tested in time series from 10 min up to overnight incubation. For each sampling time point, APTS-labeled maltodextrins or dextrans were formulated in 9 μL 1X digestion buffer. To each sampling time point, 1 μL of glucoside hydrolase solution was added and thoroughly mixed. The reaction mixture was incubated at 37 °C for 10 min, 30 min, 1 h, 4 h, or overnight (18 h). The reaction was stopped by the addition of 90 μL 89% ACNaq (v/v) and drying in a vacuum centrifuge. Samples were subsequently stored at −20 °C and formulated in Washing Solution I (part of the glyXprepCE™ kit) for sample purification. As a negative control, 9 μL of buffered APTS-labeled sample were treated similar without addition of glucoside hydrolase solution.
To deplete the enzymes and salts from the reaction mixture before xCGE-LIF analysis, an adapted sample purification using the glyXprepCE™ kit was performed. After application of the APTS-labeled sample, washing was performed four times with Washing Solution I before elution. The result of the enzyme reaction was monitored by xCGE-LIF on a glyXboxCE™ system.
Burock R., Cajic S., Hennig R., Buettner F.F., Reichl U, & Rapp E. (2023). Reliable N-Glycan Analysis–Removal of Frequently Occurring Oligosaccharide Impurities by Enzymatic Degradation. Molecules, 28(4), 1843.
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Publication 2023
Acids Adjustment Disorders alpha Glucosidase Amylase APT Citrate Dextrans Digestion enzyme activity Enzymes Glucosidase Glucosides Hydrolase maltodextrin Oligonucleotides Polysaccharides potassium phosphate Salts Sialic Acids sodium phosphate, dibasic Vacuum
4
O-Glycopeptide Enrichment and Sialidase Digestion
Intact O-glycopeptides were prepared by a combination of enrichment methods using acetone (35 (link)) and GlycOCATCH (Genovis, Lund, Sweden) enrichment resin for affinity purification of mucin-type O-glycopeptides. O-glycoproteins that were consecutively affinity-purified with the three types of lectins as described in section 2.3, were precipitated by adding a three-fold volume of cold acetone and incubating for 16 h at -30°C, followed by centrifugation at 12,000 × g for 10 min at 4°C. The precipitate was reduced with 10 mM dithiothreitol at 56°C for 30 min, and alkylated with 20 mM iodoacetamide at 25°C in dark for 40 min. Subsequently, O-glycoproteins were digested with 1.8 µg of trypsin/Lys-C mix (Promega, WI, USA) for 16 h at 37°C, in a thermomixer under continuous shaking at 800 rpm. O-glycopeptides were precipitated with a five-fold volume of cold acetone, incubated for 16 h at -30°C, and then centrifuged at 12,000 × g for 10 min. The supernatant was collected in a new tube, dried using a speed vacuum concentrator, and subjected to GlycOCATCH affinity purification. O-Glycopeptide enrichment was performed according to the manufacturer’s instructions. The resin was washed three times with TBS, and the supernatant fraction of acetone reconstituted O-glycopeptides in TBS-Tx, was rotated with a resin containing 10 units of sialidase mix (SialEXO, Genovis) at 25°C for 2 h. Sialidase mix catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked sialic acid residues from O-glycopeptide. This enzymatic treatment is required for complete removal of sialic acids, the presence of which reduce the affinity of the O-glycopeptides for the resin. The unbound peptides were removed by centrifugation at 1,000 × g for 1 min and washed three times with TBS containing 0.5 M NaCl. Resin-bound peptides were recovered by shaking with 8 M urea for 5 min. It was combined with the glycopeptide precipitate using the acetone enrichment method and purified with GL-Tip SDB (GL Science, Tokyo Japan).
Takakura D., Ohashi S., Kobayashi N., Tokuhisa M., Ichikawa Y, & Kawasaki N. (2023). Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer. Frontiers in Oncology, 13, 1104936.
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Publication 2023
Acetone Centrifugation Chromatography, Affinity Common Cold Dithiothreitol Enzymes Glycopeptides Glycoproteins Hydrolysis Iodoacetamide Lectin Mucins N-Acetylneuraminic Acid Neuraminidase Peptides Promega PRSS1 protein, human Resins, Plant Sialic Acids Sodium Chloride Urea Vacuum
5
Quantifying NA protein expression on MDCK-II cells
The expression of NA protein on MDCK-II cells was quantified by flow cytometry using FACS analysis as previously described with few modifications [65 (link)]. Briefly, MDCK-II cells in 24-well plates were infected with MOI 1 of different viruses in three replicates. At 8 and 24 h, the supernatant (0.5mL) were firstly collected then cell sheets were dissociated by trypsin (0.250 mL) and anti-N1 polyclonal antibodies were added at a ratio 1:1000 for 1 h to ~5x106 non-permeabilized single cells. After washing, secondary anti-rabbit antibodies were added 1:20000 and the cells were subjected to immuno-staining for flow cytometry analysis using a BD FACSCanto flow cytometer (BD Biosciences). The mean fluorescence intensity (MFI) of non-infected cells was subtracted from infected cells and the results were shown as ΔMFI and standard deviation of all replicates. For the detection of SA moieties, MDCK-II and MDCK-SIAT cells were infected at an MOI of 1 with rg-AL or rg-HL-16. After 2 hour incubation at 37°C cells were detached with trypsin and washed once with staining buffer. Fluorescein-labelled Sambucus nigra lectin (SNA; Vector Laboratories) and biotin-labelled Maackia amurensis lectin II (MAL II; Vector Laboratories) were used for the detection of (α-2,6) or (α-2,3) linked sialic acids, respectively, in infected and non-infected cells. After washing, MAL II binding was detected using PE-Cy7-labelled streptavidin (Biolegend). All incubation steps were carried out at 4°C in the dark. Stained infected and non-infected cells were treated with fixation buffer according to the manufacturer’s protocol (Biolegend). Reading was done using a BD FACSCanto flow cytometer (BD Biosciences). The results are the average and standard deviation of a triplicate experiment.
Scheibner D., Salaheldin A.H., Bagato O., Zaeck L.M., Mostafa A., Blohm U., Müller C., Eweas A.F., Franzke K., Karger A., Schäfer A., Gischke M., Hoffmann D., Lerolle S., Li X., Abd El-Hamid H.S., Veits J., Breithaupt A., Boons G.J., Matrosovich M., Finke S., Pleschka S., Mettenleiter T.C., de Vries R.P, & Abdelwhab E.M. (2023). Phenotypic effects of mutations observed in the neuraminidase of human origin H5N1 influenza A viruses. PLOS Pathogens, 19(2), e1011135.
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Publication 2023
Anti-Antibodies Biotin Buffers Cells Cloning Vectors Flow Cytometry Fluorescein Fluorescence Lectin Maackia amurensis Madin Darby Canine Kidney Cells Proteins Rabbits Sambucus nigra Sialic Acids Streptavidin Trypsin Virus

Top products related to «Sialic Acids»

1
α2 3 6 8 neuraminidase by New England Biolabs
Sourced in United States, United Kingdom
α2-3,6,8 neuraminidase is an enzyme that cleaves α-2,3, α-2,6, and α-2,8 linked sialic acid residues from glycoproteins and glycolipids. It is commonly used in glycobiology research for the removal of sialic acids from carbohydrate structures.
2
Bovine serum albumin (bsa) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico
Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
3
Maackia amurensis lectin 2 mal 2 by Vector Laboratories
Sourced in United States
Maackia amurensis lectin II (MAL-II) is a carbohydrate-binding protein purified from the bark of the Maackia amurensis tree. MAL-II specifically binds to sialic acid-containing glycoconjugates. This property makes it a useful tool for the study of sialic acid-mediated biological processes.
4
Pngase f by New England Biolabs
Sourced in United States, United Kingdom, Germany, Japan, Canada, France, China, Morocco, Italy
PNGase F is an enzyme that cleaves the bond between the asparagine residue and the N-acetylglucosamine residue in N-linked glycoproteins. It is commonly used in the analysis and characterization of glycoproteins.
5
Neuraminidase by Merck Group
Sourced in United States, Germany, United Kingdom, Canada
Neuraminidase is a lab equipment product manufactured by Merck Group. It is an enzyme that cleaves the glycosidic linkages of neuraminic acids (sialic acids) from glycoproteins, glycolipids, and oligosaccharides. This enzymatic function is essential for various biological processes and research applications.
6
Neuraminidase a by New England Biolabs
Sourced in United States
Neuraminidase A is an enzyme that cleaves the glycosidic linkages of sialic acid residues on the surface of cells. It serves as a core component in various biochemical applications and research techniques.
7
Biotinylated sambucus nigra lectin sna by Vector Laboratories
Sourced in United States
Biotinylated Sambucus nigra lectin (SNA) is a plant-derived lectin that binds to sialic acid residues. It is commonly used in glycobiology research to detect and visualize sialic acid-containing glycans.
8
N acetylneuraminic acid by Merck Group
Sourced in United States, China, United Kingdom
N-acetylneuraminic acid is a chemical compound used in laboratory settings. It is a naturally occurring sialic acid that plays a role in various biological processes. The primary function of N-acetylneuraminic acid is to serve as a building block for the synthesis of glycoproteins and glycolipids, which are important components of cell membranes and cell surface structures.
9
Orbitrap fusion tribrid mass spectrometer by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom
The Orbitrap Fusion Tribrid mass spectrometer is a high-performance analytical instrument designed for advanced proteomics and metabolomics research. It combines a powerful Orbitrap mass analyzer with a suite of ion manipulation and detection technologies to provide high-resolution, accurate-mass measurements of complex molecular samples.
10
Ultraflextreme by Bruker
Sourced in Germany, United States, France
The UltrafleXtreme is a high-performance mass spectrometry system designed for advanced proteomics and metabolomics research. It features a flexible architecture that allows for the integration of various ion sources and mass analyzers, enabling precise and reliable analysis of complex biological samples.

More about "Sialic Acids"

Sialic acids, also known as N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid (Neu5Gc), are a family of nine-carbon monosaccharides that play crucial roles in diverse biological processes.
These terminal residues of glycan chains on cell surface glycoproteins and glycolipids are involved in cell-cell recognition, adhesion, and signaling.
Sialic acids exhibit structural diversity and can undergo various modifications, influencing their functional properties.
Reserach into sialic acid biology and their applications in areas such as cancer, immunology, and neurodegeneration continues to be an active field of study.
Researchers often utilize tools like α2-3,6,8 neuraminidase, Bovine serum albumin, Maackia amurensis lectin II (MAL-II), and PNGase F to study sialic acid structure and function.
Neuraminidase and Neuraminidase A are also commonly used to cleave sialic acids from glycoprotein and glycolipid surfaces.
Biotinylated Sambucus nigra lectin (SNA) is a valuable tool for detecting and analyzing sialic acid residues, particularly N-acetylneuraminic acid (Neu5Ac).
Mass spectrometry techniques, such as the Orbitrap Fusion Tribrid mass spectrometer and UltrafleXtreme, have been instrumental in advancing the understanding of sialic acid structures and their roles in various biological processes.