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Mouse Anti-DPAGT1 Recombinant Antibody (1G1) (CBMAB-D1539-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase 1 (DPAGT1). The antibody can be used for immunoassay techniques, such as ELISA.
See all DPAGT1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
1G1
Antibody Isotype
IgG2a, κ
Application
ELISA

Basic Information

Immunogen
Partial recombinant corresponding to a.a.296-377 from human DPAGT1 (NP_001373) with GST tag.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)
Introduction
DPAGT1 is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4. This protein is an integral membrane protein of the endoplasmic reticulum. The congenital disorder of glycosylation type Ij is caused by mutation in the gene encoding this enzyme.
Entrez Gene ID
1798
UniProt ID
Q9H3H5
Alternative Names
Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase 1; Dolichyl-Phosphate (UDP-N-Acetylglucosamine) N-Acetylglucosaminephosphotransferase 1 (GlcNAc-1-P Transferase); UDP-N-Acetylglucosamine--Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase 1; N-Acetylglucosamine-1-Phosphate Transferase; GlcNAc-1-P Transferase 1; EC 2.7.8.15; DPAGT2; G1PT; GPT; Dolichyl-Phosphate (UDP-N-Acetylglucosamine) N-Acetylglucosaminephosphotransferase 1 (GlcNAc-1-P Tra; UDP-N-Acetylglucosamine--Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase; UDP-GlcNAc:Dolichyl-Phosphate N-Acetylglucosaminephosphotransferase; Dolichyl-Phosphate Alpha-N-Acetylglucosaminyltransferase;
Function
Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Biological Process
Dolichol-linked oligosaccharide biosynthetic process Source: UniProtKB
Dolichol metabolic process Source: Ensembl
Dolichyl diphosphate biosynthetic process Source: GO_Central
Protein N-linked glycosylation Source: UniProtKB
UDP-N-acetylglucosamine metabolic process Source: Ensembl
Cellular Location
Endoplasmic reticulum membrane
Involvement in disease
Congenital disorder of glycosylation 1J (CDG1J):
A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Myasthenic syndrome, congenital, 13 (CMS13):
A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS13 is characterized by muscle weakness mostly affecting proximal limb muscles, minimal involvement of facial, ocular and bulbar muscles, and tubular aggregates present on muscle biopsy. Symptoms include difficulty walking and frequent falls. Younger patients show hypotonia and poor head control. Neurophysiological features indicate a disorder of neuromuscular transmission on electromyography.
Topology
Lumenal: 1-10
Helical: 11-38
Cytoplasmic: 39-58
Helical: 59-78
Lumenal: 79-91
Helical: 92-118
Cytoplasmic: 119-121
Helical: 122-143
Lumenal: 144-166
Helical: 167-186
Cytoplasmic: 187-192
Helical: 193-213
Lumenal: 214-218
Helical: 219-242
Cytoplasmic: 243-250
Helical: 251-269
Lumenal: 270-271
Helical: 272-293
Cytoplasmic: 294-375
Helical: 376-400
Lumenal: 401-408

Mitachi, K., Mingle, D., Effah, W., Sánchez-Ruiz, A., Hevener, K. E., Narayanan, R., ... & Kurosu, M. (2022). Concise Synthesis of Tunicamycin V and Discovery of a Cytostatic DPAGT1 Inhibitor. Angewandte Chemie.

Liu, Z., Yang, S., Chen, X., Dong, S., Zhou, S., & Xu, S. (2021). LncRNA LINC00467 acted as an oncogene in esophageal squamous cell carcinoma by accelerating cell proliferation and preventing cell apoptosis via the miR‐485‐5p/DPAGT1 axis. Journal of Gastroenterology and Hepatology, 36(3), 721-730.

Mitachi, K., Kansal, R. G., Hevener, K. E., Gillman, C. D., Hussain, S. M., Yun, H. G., ... & Kurosu, M. (2020). DPAGT1 inhibitors of capuramycin analogues and their antimigratory activities of solid tumors. Journal of medicinal chemistry, 63(19), 10855-10878.

Li, H., You, L., Tian, Y., Guo, J., Fang, X., Zhou, C., ... & Su, Y. Q. (2020). DPAGT1‐Mediated Protein N‐Glycosylation Is Indispensable for Oocyte and Follicle Development in Mice. Advanced Science, 7(14), 2000531.

Mitachi, K., Kurosu, S. M., Eslamimehr, S., Lemieux, M. R., Ishizaki, Y., Clemons Jr, W. M., & Kurosu, M. (2019). Semisynthesis of an anticancer DPAGT1 inhibitor from a muraymycin biosynthetic intermediate. Organic letters, 21(4), 876-879.

Li, R., Xu, T., Wang, H., Wu, N., Liu, F., Jia, X., ... & Gao, H. (2019). Dysregulation of the miR-325–3p/DPAGT1 axis supports HBV-positive HCC chemoresistance. Biochemical and biophysical research communications, 519(2), 358-365.

Mitachi, K., Kurosu, S. M., Gillman, C. D., Yun, H. G., Clemons Jr, W. M., & Kurosu, M. (2019). A practical synthesis of a novel DPAGT1 inhibitor, aminouridyl phenoxypiperidinbenzyl butanamide (APPB) for in vivo studies. MethodsX, 6, 2305-2321.

Dong, Y. Y., Wang, H., Pike, A. C., Cochrane, S. A., Hamedzadeh, S., Wyszyński, F. J., ... & Carpenter, E. P. (2018). Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design. Cell, 175(4), 1045-1058.

Ng, B. G., Underhill, H. R., Palm, L., Bengtson, P., Rozet, J. M., Gerber, S., ... & University of Washington Center for Mendelian Genomics. (2018). DPAGT1 deficiency with encephalopathy (DPAGT1-CDG): clinical and genetic description of 11 new patients. In JIMD Reports, Volume 44 (pp. 85-92). Springer, Berlin, Heidelberg.

Yuste-Checa, P., Vega, A. I., Martín-Higueras, C., Medrano, C., Gámez, A., Desviat, L. R., ... & Pérez, B. (2017). DPAGT1-CDG: Functional analysis of disease-causing pathogenic mutations and role of endoplasmic reticulum stress. PLoS One, 12(6), e0179456.

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For research use only. Not intended for any clinical use.

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