Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/7377
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Type: Journal article
Title: Isolation and characterization of cDNA clones for Humly9: the human homologue of mouse Ly9
Author: Sandrin, M.
Henning, M.
Lo, M.
Baker, E.
Sutherland, G.
McKenzie, I.
Citation: Immunogenetics, 1996; 43(1-2):13-19
Issue Date: 1996
ISSN: 0093-7711
1432-1211
Statement of
Responsibility: 
Mauro S. Sandrin, Margaret M. Henning, Michael F. Lo, Elizabeth Baker, Grant R. Sutherland, Ian F. C. McKenzie
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.
Keywords: Hybrid Cells; Chromosomes, Human, Pair 1; Animals; Humans; Mice; DNA, Complementary; Antigens, Ly; In Situ Hybridization, Fluorescence; Chromosome Mapping; Sequence Alignment; Species Specificity; Amino Acid Sequence; Base Sequence; Sequence Homology, Amino Acid; Gene Library; Genes; Multigene Family; Molecular Sequence Data; Cricetinae
RMID: 0030005590
DOI: 10.1007/BF00186599
Appears in Collections:Paediatrics publications

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