DAD1 / Unconjugated /
Product Details
Description | Defender of cell death 1 (DAD1) was initially discovered in BHK21 cells as a negative regulator of programmed cell death1, a process important for normal organism development and tissue homeostasis.2 DAD1 was later shown to be a subunit of the mammalian oligosaccharyltransferase complex and is required for its function and structural integrity.3,4 Mice lacking DAD1 express abnormal N-linked glycoproteins and undergo increased apoptotic-associated embryonic death.5,6 Furthermore, overexpression of DAD1 mRNA is seen in some human hepatocellular carcinomas7, indicating it may also play a role in carcinogenesis. It should be noted that DAD1 is not related to the inhibitor of apoptosis proteins (IAP) family and does not contain any baculoviral IAP repeat (BIR) domains. | |
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Conjugate | Unconjugated | |
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Target Species | Human | |
Applications | IHC FFPE, WB | |
Supplier | Leinco | |
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About DAD1
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, Jul 2008]
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, Jul 2008]
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