Background

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.
Reference
- 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 |