|Application ||WB, E|
|Other Accession||P61805, Q29036, P61804, Q5E9C2, NP_001335.1|
|Predicted||Bovine, Mouse, Pig, Rat|
|Calculated MW||12497 Da|
|Antigen Region||64-92 aa|
|Other Names||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1, Oligosaccharyl transferase subunit DAD1, Defender against cell death 1, DAD-1, DAD1|
|Target/Specificity||This DAD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 64-92 amino acids from the C-terminal region of human DAD1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||DAD1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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. 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). Loss of the DAD1 protein triggers apoptosis (By similarity).|
|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.
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. [provided by RefSeq].
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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