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

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A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation. / Steentoft, Catharina; Yang, Zhang; Wang, Shengjun; Ju, Tongzhong; Vester-Christensen, Malene Bech; Festari, María Florencia; King-Smith, Sarah Louise; Moremen, Kelley; Larsen, Ida Signe Bohse; Goth, Christoffer Knak; Schjoldager, Katrine Ter-Borch Gram; Hansen, Lars; Bennett, Eric Paul; Mandel, Ulla; Narimatsu, Yoshiki.

I: Glycobiology, Bind 29, Nr. 9, 2019, s. 645–656.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Steentoft, C, Yang, Z, Wang, S, Ju, T, Vester-Christensen, MB, Festari, MF, King-Smith, SL, Moremen, K, Larsen, ISB, Goth, CK, Schjoldager, KT-BG, Hansen, L, Bennett, EP, Mandel, U & Narimatsu, Y 2019, 'A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.', Glycobiology, bind 29, nr. 9, s. 645–656. https://doi.org/10.1093/glycob/cwz041

APA

Steentoft, C., Yang, Z., Wang, S., Ju, T., Vester-Christensen, M. B., Festari, M. F., ... Narimatsu, Y. (2019). A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation. Glycobiology, 29(9), 645–656. https://doi.org/10.1093/glycob/cwz041

Vancouver

Steentoft C, Yang Z, Wang S, Ju T, Vester-Christensen MB, Festari MF o.a. A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation. Glycobiology. 2019;29(9):645–656. https://doi.org/10.1093/glycob/cwz041

Author

Steentoft, Catharina ; Yang, Zhang ; Wang, Shengjun ; Ju, Tongzhong ; Vester-Christensen, Malene Bech ; Festari, María Florencia ; King-Smith, Sarah Louise ; Moremen, Kelley ; Larsen, Ida Signe Bohse ; Goth, Christoffer Knak ; Schjoldager, Katrine Ter-Borch Gram ; Hansen, Lars ; Bennett, Eric Paul ; Mandel, Ulla ; Narimatsu, Yoshiki. / A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation. I: Glycobiology. 2019 ; Bind 29, Nr. 9. s. 645–656.

Bibtex

@article{23718aaeeb59441aa08aca8c79b94ebe,
title = "A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.",
abstract = "Complex carbohydrates serve a wide range of biological functions in cells and tissues, and their biosynthesis involves more than 200 distinct glycosyltransferases (GTfs) in human cells. The kinetic properties, cellular expression patterns and subcellular topology of the GTfs direct the glycosylation capacity of a cell. Most GTfs are ER or Golgi resident enzymes, and their specific subcellular localization is believed to be distributed in the secretory pathway according to their sequential role in the glycosylation process, although detailed knowledge for individual enzymes is still highly fragmented. Progress in quantitative transcriptome and proteome analyses has greatly advanced our understanding of the cellular expression of this class of enzymes, but availability of appropriate antibodies for in situ monitoring of expression and subcellular topology have generally been limited. We have previously used catalytically active GTfs produced as recombinant truncated secreted proteins in insect cells for generation of mouse monoclonal antibodies (mAbs) to human enzymes primarily involved in mucin-type O-glycosylation. These mAbs can be used to probe subcellular topology of active GTfs in cells and tissues as well as their presence in body fluids. Here, we present several new mAbs to human GTfs and provide a summary of our entire collection of mAbs, available to the community. Moreover, we present validation of specificity for many of our mAbs using human cell lines with CRISPR/Cas9 or zinc finger nuclease (ZFN) knockout and knockin of relevant GTfs.",
author = "Catharina Steentoft and Zhang Yang and Shengjun Wang and Tongzhong Ju and Vester-Christensen, {Malene Bech} and Festari, {Mar{\'i}a Florencia} and King-Smith, {Sarah Louise} and Kelley Moremen and Larsen, {Ida Signe Bohse} and Goth, {Christoffer Knak} and Schjoldager, {Katrine Ter-Borch Gram} and Lars Hansen and Bennett, {Eric Paul} and Ulla Mandel and Yoshiki Narimatsu",
year = "2019",
doi = "10.1093/glycob/cwz041",
language = "English",
volume = "29",
pages = "645–656",
journal = "Glycobiology",
issn = "0959-6658",
publisher = "Oxford University Press",
number = "9",

}

RIS

TY - JOUR

T1 - A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.

AU - Steentoft, Catharina

AU - Yang, Zhang

AU - Wang, Shengjun

AU - Ju, Tongzhong

AU - Vester-Christensen, Malene Bech

AU - Festari, María Florencia

AU - King-Smith, Sarah Louise

AU - Moremen, Kelley

AU - Larsen, Ida Signe Bohse

AU - Goth, Christoffer Knak

AU - Schjoldager, Katrine Ter-Borch Gram

AU - Hansen, Lars

AU - Bennett, Eric Paul

AU - Mandel, Ulla

AU - Narimatsu, Yoshiki

PY - 2019

Y1 - 2019

N2 - Complex carbohydrates serve a wide range of biological functions in cells and tissues, and their biosynthesis involves more than 200 distinct glycosyltransferases (GTfs) in human cells. The kinetic properties, cellular expression patterns and subcellular topology of the GTfs direct the glycosylation capacity of a cell. Most GTfs are ER or Golgi resident enzymes, and their specific subcellular localization is believed to be distributed in the secretory pathway according to their sequential role in the glycosylation process, although detailed knowledge for individual enzymes is still highly fragmented. Progress in quantitative transcriptome and proteome analyses has greatly advanced our understanding of the cellular expression of this class of enzymes, but availability of appropriate antibodies for in situ monitoring of expression and subcellular topology have generally been limited. We have previously used catalytically active GTfs produced as recombinant truncated secreted proteins in insect cells for generation of mouse monoclonal antibodies (mAbs) to human enzymes primarily involved in mucin-type O-glycosylation. These mAbs can be used to probe subcellular topology of active GTfs in cells and tissues as well as their presence in body fluids. Here, we present several new mAbs to human GTfs and provide a summary of our entire collection of mAbs, available to the community. Moreover, we present validation of specificity for many of our mAbs using human cell lines with CRISPR/Cas9 or zinc finger nuclease (ZFN) knockout and knockin of relevant GTfs.

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

U2 - 10.1093/glycob/cwz041

DO - 10.1093/glycob/cwz041

M3 - Journal article

C2 - 31172184

VL - 29

SP - 645

EP - 656

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

IS - 9

ER -

ID: 231905122