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| Cat.No | ACP20444 | Target Name | DAD1 |
|---|---|---|---|
| Target Synonyms | DAD1; Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1; Oligosaccharyl transferase subunit DAD1; Defender against cell death 1; DAD-1 | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Expression Range | 2-113aa |
| Mol Weight | 39.8kD | Protein Length | Full Length of Mature Protein |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P61803 |
|---|
Uniprot Id
P61803
Target Species
Human
Target Name
DAD1
Target Full Name
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
Target Function
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. 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. Required for the assembly of both SST3A- and SS3B-containing OST complexes. Loss of the DAD1 protein triggers apoptosis.
Target Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Target Protein Families
DAD/OST2 family
Target Research Area
Apoptosis
Target Synonyms
DAD1; Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1; Oligosaccharyl transferase subunit DAD1; Defender against cell death 1; DAD-1
Target Background
DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes.
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