PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.
PPP2R4 Polyclonal Antibody, Biotin Conjugated. Biotin. Raised in: Rabbit.
Liquid. 0.03% Proclin 300, 50% Glycerol, 0.01M PBS, PH 7.4.
>95%, Protein G purified
Recombinant Human Serine/threonine-protein phosphatase 2A activator protein (1-250AA)
Shipped at 4°C. Upon delivery aliquot and store at -20°C (short-term) or -80°C (long-term). Avoid repeated freeze.
Serine/threonine-protein phosphatase 2A activator (EC:126.96.36.199), PPP2R4, PTPA, PP2A, subunit B', PR53 isoform, Phosphotyrosyl phosphatase activator, PTPA, Serine/threonine-protein phosphatase 2A regulatory subunit 4, Serine/threonine-protein phosphatase 2A regulatory subunit B'