cDNA cloning of a novel testis-specific calcineurin B-like protein
H Mukai, CD Chang, H Tanaka, A Ito, T Kuno… - Biochemical and …, 1991 - Elsevier
H Mukai, CD Chang, H Tanaka, A Ito, T Kuno, C Tanaka
Biochemical and biophysical research communications, 1991•ElsevierA cDNA clone encoding a novel calcineurin B-like protein (CBLP) was isolated from a rat
testis cDNA library by cross-hybridization with a calcineurin B cDNA probe. CBLP is
composed of 176 amino acids and contains four putative Ca 2+-binding domains. The
overall predicted amino acid sequence homology between CBLP and calcineurin B is 82%.
Northern blots showed that trancripts for CBLP are specifically and highly expressed in the
testis.
testis cDNA library by cross-hybridization with a calcineurin B cDNA probe. CBLP is
composed of 176 amino acids and contains four putative Ca 2+-binding domains. The
overall predicted amino acid sequence homology between CBLP and calcineurin B is 82%.
Northern blots showed that trancripts for CBLP are specifically and highly expressed in the
testis.
Summary
A cDNA clone encoding a novel calcineurin B-like protein (CBLP) was isolated from a rat testis cDNA library by cross-hybridization with a calcineurin B cDNA probe. CBLP is composed of 176 amino acids and contains four putative Ca2+-binding domains. The overall predicted amino acid sequence homology between CBLP and calcineurin B is 82%. Northern blots showed that trancripts for CBLP are specifically and highly expressed in the testis.
Elsevier