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The cloning expression and tissue distribution of human PP2Cβ 1
Author(s) -
Marley Anna E.,
Kline Adam,
Crabtree Garry,
Sullivan Jane E.,
Beri Raj K.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00708-x
Subject(s) - cloning (programming) , recombinant dna , okadaic acid , cdna library , complementary dna , northern blot , gene isoform , western blot , microbiology and biotechnology , biochemistry , chemistry , biology , gene , enzyme , phosphatase , computer science , programming language
We have cloned a novel PP2Cβ isoform from a human liver cDNA library which codes for a protein homologous to other mammalian PP2Cβs at the N‐terminus but with an extended C‐terminus that is unique amongst the PP2Cs. The protein expressed in E. coli is indistinguishable from human recombinant PP2Cα in its cation dependence and insensitivity to okadaic acid. Northern blot analysis of PP2Cβ along with that of PP2Cα shows that human PP2Cs are widely expressed and are most abundant in heart and skeletal muscle.

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