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AB204314

Anti-DDOST antibody

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(2 Publications)

Rabbit Polyclonal DDOST antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human DDOST aa 250-450.

View Alternative Names

KIAA0115, OST48, OK/SW-cl.45, DDOST, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit, DDOST 48 kDa subunit, Oligosaccharyl transferase 48 kDa subunit

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DDOST antibody (AB204314)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DDOST antibody (AB204314)

Immunohistochemical analysis of paraffin-embedded Human duodenum tissue, labeling DDOST using ab204314 at a 1/500 dilution.

Immunocytochemistry/ Immunofluorescence - Anti-DDOST antibody (AB204314)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-DDOST antibody (AB204314)

Immunofluorescence analysis of paraformaldehyde-fixed U-2 OS cells labeling DDOST using ab204314 at 4 μg/ml (green).

Western blot - Anti-DDOST antibody (AB204314)
  • WB

Supplier Data

Western blot - Anti-DDOST antibody (AB204314)

All lanes:

Western blot - Anti-DDOST antibody (ab204314) at 1/100 dilution

Lane 1:

RT-4 cell lysate

Lane 2:

U-251 MG cell lysate

Predicted band size: 51 kDa

true

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, ICC/IF, WB

applications

Immunogen

Recombinant Fragment Protein within Human DDOST aa 250-450. The exact immunogen used to generate this antibody is proprietary information.

P39656

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit (DDOST) also known as oligosaccharyltransferase 48 kDa subunit weighs approximately 48 kDa. It is part of the oligosaccharyltransferase (OST) complex which is found mostly in the endoplasmic reticulum (ER). This protein functions to transfer glycan chains to nascent proteins during N-linked glycosylation an important post-translational modification. DDOST expresses widely across different tissues reflecting its importance in protein synthesis and folding.
Biological function summary

The DDOST protein plays a big role in the process of protein glycosylation. As part of the OST complex it facilitates the attachment of oligosaccharides to specific asparagine residues of target proteins in the ER. This glycosylation process helps with protein folding and stability and is important for the functionality and longevity of the proteins. Alterations in this system can affect protein structure and function illustrating DDOST's critical role in ensuring protein integrity and cellular homeostasis.

Pathways

DDOST participates rigorously in the N-glycosylation pathway. It interacts with key enzymes involved in the transfer of glycan moieties to nascent polypeptides which is necessary for proper cellular function. The protein also works closely with ribophorin and other subunits of the OST complex. While directly part of this glycosylation pathway its activity indirectly impacts various cellular signaling pathways due to its role in modifying and folding membrane-bound and secreted proteins.

Defects in DDOST relate to congenital disorders of glycosylation. Mutations in this protein can lead to improper glycosylation causing a range of symptoms from developmental delays to neurological issues. Also changes in glycosylation patterns have associations with cancer progression. Beyond DDOST itself glycosylation often affects other key proteins contributing to these conditions such as integrins and cadherins especially in the context of cell adhesion and signaling.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed : 31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed : 22467853).
See full target information DDOST

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Discover oncology 15:69 PubMed38460058

2024

DDOST is associated with tumor immunosuppressive microenvironment in cervical cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Jie Mei,Liuliu Pan,Min Huang,Dandan Bao,Hui Gao,Danhan Wang

Genetics in medicine open 2:100841 PubMed39669623

2023

Clinical study of ferredoxin-reductase-related mitochondriopathy: Genotype-phenotype correlation and proposal of ancestry-based carrier screening in the Mexican population.

Applications

Unspecified application

Species

Unspecified reactive species

Teresa Campbell,Jesse Slone,Hallie Metzger,Wensheng Liu,Stephanie Sacharow,Amy Yang,Mariya Moosajee,Chiara La Morgia,Valerio Carelli,Flavia Palombo,Matthew A Lines,A Micheil Innes,Rebecca J Levy,Derek Neilson,Nicola Longo,Taosheng Huang
View all publications

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