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DAD1 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P61803 |
|---|---|
| Clone Names | 100712271 |
| Gene ID | 1603 |
|---|---|
| Other Names | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1, Oligosaccharyl transferase subunit DAD1, Defender against cell death 1, DAD-1, DAD1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | DAD1 (HGNC:2664) |
|---|---|
| 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 (PubMed:22467853, 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. Loss of the DAD1 protein triggers apoptosis (PubMed:22467853). |
| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
DAD1, the defender against apoptotic cell death, wasinitially identified as a negative regulator of programmed celldeath in the temperature sensitive tsBN7 cell line. The DAD1protein disappeared in temperature-sensitive cells following ashift to the nonpermissive temperature, suggesting that loss of theDAD1 protein triggered apoptosis. DAD1 is believed to be a tightlyassociated subunit of oligosaccharyltransferase both in the intactmembrane and in the purified enzyme, thus reflecting the essentialnature of N-linked glycosylation in eukaryotes. [provided byRefSeq].
References
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)Liu, C.Y., et al. Carcinogenesis 31(7):1259-1263(2010)Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Kulke, M.H., et al. Genes Chromosomes Cancer 47(7):591-603(2008)Shibatani, T., et al. Biochemistry 44(16):5982-5992(2005)
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