ADVANCE DEFT 865 DRIVER DETAILS:
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ADVANCE DEFT 865 DRIVER
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Cell survival was determined by counting the number of viable blue cells from Advance DEFT 865 random fields of view per well The nucleotide coding sequence is Structurally, the DEFT protein can be subdivided into two parts: The N-terminal third contains a stretch of amino acid sequence completely conserved between human and rat that is homologous to the DEDs of other known molecules Fig. By contrast, the amino acid sequence corresponding to the C-terminal two-thirds of DEFT shows no substantial homology to any previously identified proteins.
Figure 1. Numbers to right of sequences indicate amino acids in italics and nucleotides. Initiation codon as well as in-frame terminator codons marked by asterisks up- and downstream of ORF are depicted in boldface. Dots in rat nucleotide sequence represent identity with Advance DEFT 865 sequence. Shaded residues 25— correspond to death effector domain Advance DEFT 865 DEFT, whereas underlined tetrapeptides indicate putative caspase cleavage sites see text.
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Figure 2. Positions of residues contributing to a hydrophobic region important for protein-protein interactions asterisks in DED of FADD are marked. Also included in the analysis was Bap31, a molecule with a weak DED homology that forms a complex with procaspase-8 and Bcl-2 proteins in the endoplasmatic reticulum The putative phylogenetic relationship among the DEDs of these proteins is shown in Fig. In addition, low level expression was also detected in a variety of other adult human and rat tissues, including the ovary. In human tissues, one main transcript with a size of approximately 2.
Advance DEFT 865 3.
Numbers on left indicate kilobases and arrowheads DEFT transcripts of different sizes. Small int.
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