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Glycobiology

Background

Glycobiology

Glycobiology, also known as glycan, is the study of the structure, biosynthesis, biology, and evolution of saccharides that are widely distributed in nature in all living forms. Glycobiology is a rapidly expanding field of study that is critical for both cellular biology and studies of carbohydrate-based drugs and therapeutics:

  • Glycans play a role in communication between cells and their external environment.
  • Glycosylation is important for protein folding and quality control and defines the adhesive properties of proteins and cells.
  • Glycans play an important role in the development of multicellular organisms and their functions are determined by their unique structures.
  • Glycosylation is an important determinant of the efficacy of biologics such as therapeutic antibodies.

Research Area of Glycobiology in Different Species

  • Yeasts

As biopharmaceuticals with humanized N-linked oligosaccharides, the suppression of yeast-specific O-mannosylation is important to reduce immune response and to improve heterologous protein productivity in the production of biopharmaceuticals. Present study demonstrated that Saccharomyces cerevisiae strain is capable of producing a glycoprotein with humanized Man5GlcNAc2 N-linked oligosaccharides, an intermediate of mammalian hybrid- and complex-type oligosaccharides while suppressing O-mannosylation. This strain was generated by firstly introducing msdS encoding α-1,2-mannosidase into a strain synthesizing Man8GlcNAc2 N-linked oligosaccharides, then disrupting PMT1 and PMT2, using a mutagenesis technique that is based on the disparity theory of evolution and finally disrupting vacuolar proteases PEP4 and PRB1.

  • Rice

Although the differences in protein glycosylation between sexes have already been observed in the rice pest insect Nilaparvata lugens (N. lugens), the functionality of differential N-glycosylation between sexes is yet unknown. Recent study indicated that comparison of N-glycopeptides sites from the adult stages of N. lugens revealed striking differences in protein N-glycosylation between sexes. Additionally, differential glycan composition between males and females was observed for proteins shared across sexes.

  • Arabidopsis thaliana (Arabidopsis)

N-glycosylation plays multiple roles in regulating stress tolerance of plants. Study has shown that an obvious decrease in photosynthetic capacity and dry mass were detected in alg3-3 and cgl1-1, two typical mutants in N-glycosylation process of Arabidopsis. The maximal photochemical efficiency of PSII, which reflected the photochemical of plant, decreased significantly in cgl1-1. Also, a similar tendency was observed in alg3-3. Besides, N-glycosylation was also required to maintain the stability of a chloroplast-located protein CAH1, which was closely related to photosynthesis.

Creative Biolabs offers a comprehensive range of monoclonal, polyclonal, and secondary antibodies. All our antibodies provide high levels of specificity and affinity to target antigens. We also provide a range of cell line controls for reliable antibody validation. For further details, please feel free to contact us.

Reference

  1. Lakshminarayanan, Abirami.; et al. Studying glycobiology at the single-molecule level. Nature Reviews Chemistry. 2018.

Our provided featured target antibody products including but not limited to:

Cat# Product Name Host species Species Reactivity Application Size Conjugate Alternative Names Protein
CBMOAB-00431HCB Mouse Anti-C. elegans AGL1 Antibody (CBMOAB-00431HCB) Mouse C. elegans (Caenorhabditis elegans) WB, ELISA 0.5mg, 1mg, 200µg Alexa Fluor 350, AP, APC, Biotin, Consult us more, Cy3, Cy5, Cy5.5, Cy7, FITC, HRP, NONE, PE, PerCP AGL (Amylo-1,6-GLucosidase, 4-alpha-glucanotransferase) glycogen debranching enzyme, agl-1 4-alpha-glucanotransferase
CBMOAB-04249HCB Mouse Anti-C. elegans GALT1 Antibody (CBMOAB-04249HCB) Mouse C. elegans (Caenorhabditis elegans) WB, ELISA 0.5mg, 1mg, 200µg Alexa Fluor 350, AP, APC, Biotin, Consult us more, Cy3, Cy5, Cy5.5, Cy7, FITC, HRP, NONE, PE, PerCP Protein GALT-1, galt-1 Beta-1,4-galactosyltransferase galt-1
MORAB-011F Anti-ALG6 Antibody (Cat MORAB-011F), Human IgG Human Saccharomyces cerevisiae IA 0.5mg, 1mg, 10mg None ALG6, YOR002W, UNA544 Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
MOFAB-008W Rabbit Anti-PPP1R3G Antibody (MOFAB-008W) Rabbit Zebrafish ELISA, WB, IP Inquiry None PPP1R3G, PPP1R3G PPP1R3G
MOFAB-030W mouse Anti-Rubisco Antibody (MOFAB-030W) mouse Rice IA Inquiry None Ribulose-1, 5-bisphosphate carboxylase/oxygenase, Rubisco Ribulose-1, 5-bisphosphate carboxylase/oxygenase
MOFAB-184W Rabbit Anti-UGPase Antibody (MOFAB-184W) Rabbit Arabidopsis, Canola, Brassica Oleracea WB, IF Inquiry None Probable UTP--glucose-1-phosphate uridylyltransferase 2, EC 2.7.7.9, UDP-glucose pyrophosphorylase 2, UDPGP 2, UGPase 2, At3g03250, UGPase, UGPase Probable UTP--glucose-1-phosphate uridylyltransferase 2
MOF032922W82 Rabbit Anti-Gliadin Antibody (MOF032922W82) Rabbit Wheat gliadin ELISA, IHC-P, IHC-Fr, ICC, IF 100µL, 200µL, 50µL NONE Celiac disease, gliadin - wheat ergot protein
For Research Use Only | Not For Clinical Use.