DPAGT1 Antibodies

AND DPAGT1 ELISA kits, DPAGT1 Proteins

Many biological assays use antibodies to detect DPAGT1, such as Western Blot (WB), ELISA, Flow Cytometry, Immunocytochemistry (IHC). These antibodies can be polyclonal or monoclonal, and react with DPAGT1 in Human, Mouse, Rat, and many other animal samples. Boster Bio use mainly mouse and rabbit to develop DPAGT1 antibodies...

We validate the specificity of these antibodies to DPAGT1 by testing them on tissues known to express DPAGT1 positively and negatively. Browse below to find the DPAGT1 antibody that suites your experiment. We have 2 of these antibodies and many publications and validation images.

If you cannot find antibodies that fit your needs, contact us for making custom antibodies. We have a full suite of custom antibody services covering from research to diagnostic and therapeutic applications.

Designing an IHC experiment for DPAGT1? The guide has the expected staining pattern, antigen retrieval and fixation, antibodies backed by real IHC images, the tissue controls to run alongside, and protocols taken from published papers.

Open the DPAGT1 IHC Guide

DPAGT1 Infographic by Boster Bio

All DPAGT1 Products

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Anti-DPAGT1 Antibody

Western blot analysis of DPAGT1 in mouse kidney tissue lysate with DPAGT1 antibody at 1 μg/mL in (A) the absence and (B) the presence of blocking peptide

Immunohistochemistry of DPAGT1 in human kidney tissue with DPAGT1 antibody at 2

Immunofluorescence of DPAGT1 in human kidney tissue with DPAGT1 antibody at 20 μg/mL

Human, Mouse

ELISA, IF, IHC-P, WB

$481
Cat # A08142
0.1 mg

DPAGT1 (NM_203316) Human Over-expression Lysate

DPAGT1 Human Over-expression Lysates NM_001382

Human

$628
Cat # LS001798
20 µg, 100 µg

DPAGT1 Overview

Facts about UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase.

DPAGT1 3D structure. Source: alphafold

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1)

Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc on the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P- dolichol. .

Gene Information

Human
Gene Name:	DPAGT1
Uniprot:	Q9H3H5
Entrez:	1798

Family

Belongs to:

glycosyltransferase 4 family

Alternative Names

ALG7; CDG1J; CDG-Ij; D11S366; DGPTDPAGT2UAGT; dolichyl-phosphate (UDP-N-acetylglucosamine)N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P tra; dolichyl-phosphate (UDP-N-acetylglucosamine)N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase); dolichyl-phosphate alpha-N-acetylglucosaminyltransferase; EC 2.7.8; EC 2.7.8.15; G1PT; GlcNAc-1-P transferase; GPTDPAGT; N-acetylglucosamine-1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate N-acetylglucosaminephosphotransferase; UDP-N-acetylglucosamine--dolichyl-phosphateN-acetylglucosaminephosphotransferase; UGAT

Molecular Weight

Mass (kDA):
46.09 kDA

Genomic Context


Human

Location:	11q23.3
Sequence:	11; NC_000011.10 (119096505..119101884, complement)

Subcellular Localizations

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Diseases

Congenital Disorders Of Glycosylation
Congenital Disorders
Malignant Neoplasms
Carcinoma
Malignant Squamous Cell Neoplasm
Muscle Hypotonia
Weakness
Myasthenic Syndromes, Congenital
Mouth Neoplasms
Malignant Neoplasm Of Mouth

Exotropia
Microcephaly
Tissue Adhesions
Muscle Weakness
Bilateral Cataracts (disorder)

Pathways

Glycosylation
Protein Glycosylation
Signal Transmission
Localization
Epithelial Cell-cell Adhesion
Chromosome Segregation

Cell-cell Adhesion

PTMs

Glycosylation

Phosphorylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/DPAGT1

References

PMID: 9451016 by Eckert V., et al. Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae.

PMID: 29459785 by Yoo J., et al. GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation.