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Updated: Aug 2, 2026

Functional Cloning Using a Xenopus Oocyte Expression System
Published on: January 30, 2016
Cloning and characterization of SOB1, a new testis-specific cDNA encoding a human sperm protein probably involved in
A Lefevre1, C Duquenne, M F Rousseau-Merck
1INSERM U 355, Maturation Gamétique et Fécondation, IPSC, 32 rue des Carnets, Clamart, 92140, France. annick.lefevre@inserm.ipsc.u-psud.fr
Abstract:
A human sperm-oocyte binding protein, SOB1, was purified by two dimensional gel electrophoresis and sequenced. This protein was selected because it was recognized by a monoclonal antibody that inhibited the binding of human sperm to zona-free hamster oocytes. The sequences of the tryptic peptides were used to design degenerate primers. These were used to amplify a specific fragment from human testis cDNA by the polymerase chain reaction. This 1233 bp fragment was extended in 3' and 5' by RACE to obtain the 3 kb full length SOB1 cDNA. Sequence analysis indicated that the deduced open reading frame encodes a 853 amino acid protein, with a molecular mass of 94. 7 kDa. This is a new testis-specific cDNA. It is 27, 32.8 and 34.4% homologous to three sperm proteins, HI, Fsc1 and AKAP82 respectively. A single 3kb transcript was demonstrated only in the testis by northern blot analysis. It is a single copy gene, well conserved among mammals and located on human chromosome 12 at band p13.
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