|
|
| Alternative Name : |
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, PRKAR1A PKR1, PRKAR1, CAR, CNC, CNC1, PKR1, ADOHR, PPNAD1, ACRDYS1. |
| Amount : |
25 µg |
Source : Escherichia Coli.
PKA regulatory subunit I a Human Recombinant is a dimeric 86kDa protein (the monomer is 381 aa 43kDa). PKAR-I alpha is purified by proprietary chromatographic techniques.
The Regulatory (R) subunit of Protein Kinase A (PKA) inhibits its kinase activity by shielding the Catalytic (C) subunit from physiological substrates. This inhibition is reversed in response to extra-cellular signals that increase cAMP levels in the cytoplasm. Upon cAMP binding to R, C is allosterically released from R, activating a spectrum of downstream signaling cascades. Crystallographic data indicated that a series of distinct conformational changes within CBD-A must occur to relay the cAMP signal from the cAMP binding site to the R:C interaction interface. One critical cAMP relay site within the CBD-A of R has been identified as Asp170 because the D170A mutation selectively reduces the negative cooperativity between the cAMP- and C-recognition sites (i.e. the KD for the R:C complex in the presence of cAMP is reduced by more than 12-fold), without significantly compromising the high affinity of R for both binding partners.
