DDOST Antibodies

AND DDOST ELISA kits, DDOST Proteins

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

We validate the specificity of these antibodies to DDOST by testing them on tissues known to express DDOST positively and negatively. Browse below to find the DDOST 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.

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DDOST Infographic by Boster Bio

All DDOST Products

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Anti-DDOST Mouse Monoclonal Antibody [Clone ID: OTI2B4]

HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY DDOST (Right lane) cDNA for 48 hrs and lysed

Immunohistochemical staining of paraffin-embedded Human pancreas tissue within the normal limits using anti-DDOST mouse monoclonal antibody

Immunohistochemical staining of paraffin-embedded Human prostate tissue within the normal limits using anti-DDOST mouse monoclonal antibody

+11

Human, Mouse, Rat

IHC, WB

$523
Cat # M10511
100 µl

Anti-DDOST Antibody Picoband®

Western blot analysis of DDOST using anti-DDOST antibody (A10511-1)

IHC analysis of DDOST using anti-DDOST antibody (A10511-1)

Human, Mouse, Rat

ELISA, Flow Cytometry, IP, IHC, WB

$370
Cat # A10511-1
100 μg/vial

DDOST Overview

Facts about Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit.

DDOST 3D structure. Source: alphafold

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (DDOST)

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Required for the assembly of both SST3A- and SS3B-containing OST complexes.

Required for efficient N-glycosylation. .

Gene Information

Human
Gene Name:	DDOST
Uniprot:	P39656
Entrez:	1650

Family

Belongs to:

DDOST 48 kDa subunit family

Alternative Names

advanced glycation endproduct receptor 1; DDOST 48 kDa subunit; dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit; dolichyl-diphosphooligosaccharide-protein glycosyltransferase; dolichyl-diphosphooligosaccharide--protein glycosyltransferase; dolichyl-diphosphooligosaccharide-protein glycotransferase; EC 2.4.1.119; KIAA0115MGC2191; Oligosaccharyl transferase 48 kDa subunit; oligosaccharyltransferase 48 kDa subunit; OST48AGER1; OSTOKSWcl45; WBP1

Molecular Weight

Mass (kDA):
50.801 kDA

Genomic Context


Human

Location:	1p36.12
Sequence:	1; NC_000001.11 (20651777..20661369, complement)

Subcellular Localizations

Endoplasmic reticulum membrane; Single-pass type I membrane protein.

Diseases

Diabetic Nephropathy
Complications Of Diabetes Mellitus
Myeloid Leukemia, Chronic
Atherosclerosis
Diabetes Mellitus
Gastritis
Parkinson Disease
Congenital Disorders Of Glycosylation
Congenital Disorders
Diabetic Angiopathies
Cardiovascular Diseases
Malignant Neoplasms

Diabetes Mellitus, Insulin-dependent
Persistent Superficial Gastritis
Kidney Diseases
Hematological Disease
Vascular Diseases
Alzheimer's Disease

Interacting Proteins

TMEM173

Pathways

Pathogenesis
Transport
Dna Replication
Aging
Glycosylation
Oxidative Phosphorylation
Autolysis

Localization

PTMs

Phosphorylation

Glycosylation

Ubiquitination

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

References

PMID: 9367678 by Yamagata T., et al. Genome organization of human 48-kDa oligosaccharyltransferase (DDOST).

PMID: 22467853 by Roboti P., et al. The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation.