A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation

• DOI: 10.1093/glycob/cwz041
• Publication Date: 2019-06-04T11:39:42Z
• Authors: Catharina Steentoft; Zhang Yang; Shengjun Wang; Tongzhong Ju; Malene B Vester-C...; María F Festari; Sarah L King; Kelley Moremen; Ida S B Larsen; Christoffer K Goth; Katrine T Schjold...; Lars Hansen; Eric P Bennett; Ulla Mandel; Yoshiki Narimatsu
• Keywords: 0301 basic medicine; Glycosylation; Mucins; Antibodies, Monoclonal; Glycosyltransferases; Reproducibility of Results; 3. Good health; Mice; 03 medical and health sciences; HEK293 Cells; Antibody Specificity; Animals; Humans

Complex carbohydrates serve a wide range of biological functions in cells and tissues, their biosynthesis involves more than 200 distinct glycosyltransferases (GTfs) human cells. The kinetic properties, cellular expression patterns subcellular topology the GTfs direct glycosylation capacity cell. Most are ER or Golgi resident enzymes, specific localization is believed to be distributed secretory pathway according sequential role process, although detailed knowledge for individual enzymes still highly fragmented. Progress quantitative transcriptome proteome analyses has greatly advanced our understanding this class but availability appropriate antibodies situ monitoring have generally been limited. We previously used catalytically active produced as recombinant truncated secreted proteins insect generation mouse monoclonal (mAbs) primarily involved mucin-type O-glycosylation. These mAbs can probe tissues well presence body fluids. Here, we present several new provide summary entire collection mAbs, available community. Moreover, validation specificity many using cell lines with CRISPR/Cas9 zinc finger nuclease (ZFN) knockout knockin relevant GTfs.