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|Title:||Isolation and characterization of cDNA clones for Humly9: the human homologue of mouse Ly9.|
|Authors:||Sandrin, Mauro S;Henning, M M;Lo, M F;Baker, E;Sutherland, G R;McKenzie, Ian F C|
|Affiliation:||Molecular Immunogenetics Laboratory, Austin Research Institute, Austin Hospital, Heidelberg, Vic, Australia.|
|Citation:||Immunogenetics; 43(1-2): 13-9|
|Abstract:||Ly9 is a mouse cell membrane antigen found on all lymphocytes and coded for by a gene that maps to chromosome 1. We previously described the isolation and characterization of a full-length cDNA clone for mouse Ly9. Using cross-species hybridization we isolated cDNA clones encoding the human homologue Humly9. Analysis of the predicted protein sequence suggests that the extra-cellular portion of the Humly9 molecules is composed of four Ig-like domains: a V domain (V) without disulphide bonds and a truncated C2 domain (tC2) with two disulphide bonds, a second V domain without disulphide bonds and a second tC2 with two disulphide bonds, i.e., as V-tC2-V-tC2. The gene encoding Humly9 was mapped to chromosome 1 by analysis of human/hamster hybrids, and more specifically to the 1q22 region by in situ hybridization. The protein sequence data support the view that Humly9 belongs to the immunoglobulin-superfamily subgroup which includes CD48, CD2, and LFA-3.|
|Internal ID Number:||8537117|
|Subjects:||Amino Acid Sequence|
Chromosomes, Human, Pair 1
In Situ Hybridization, Fluorescence
Molecular Sequence Data
Sequence Homology, Amino Acid
|Appears in Collections:||Journal articles|
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