|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:100|
|Western Blot (WB)||1:500-1:1000|
|Tested Species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic non-phosphopeptide derived from human PPP1R2 around the phosphorylation site of Ser120 and Ser121 (Q-E-SP-SP-G-E)|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 150mM NaCl, 50% glycerol|
|Contains||0.02% sodium azide|
Inhibitor-2 (I-2) exists as a heterodimer with protein phosphatase type-1 (PP1), termed MgATP-dependent phosphatase. I-2 binds and forms an inactive complex with PP1 in its unphosphorylated state. This complex is activated through a series of phosphorylations on serine and threonine residues in I-2 that increases phosphatase activity. Multiple kinases have been implicated in phosphorylation of I-2 at threonine 72, namely GSK-3, cdc2 and ERK1. Casein kinase II phosphorylates I-2 at serine residues, which in turn enhances threonine phosphorylation by GSK-3. Recent evidence has shown that phosphorylation at threonine 72 peaks during prophase of the cell cycle and is localized in the centrosomes. The I-2/PP1 complex also binds neurabin and the kinases Nek2, KPI-2, and Aurora-A. Regulation of I-2/PP1 has been shown to be important in cell cycle, gene expression, ion gating, and neuromodulation.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: IPP-2; IPP2; phosphatase inhibitor 2; phosphoprotein phosphatase; PPP1R2; protein phosphatase 1, regulatory (inhibitor) subunit 2; protein phosphatase 1, regulatory subunit 2; Protein phosphatase inhibitor 2
Gene Aliases: 0610025N14Rik; 2310007G06Rik; 4930440J04Rik; 5430408E15Rik; D16Ertd248e; IPP-2; IPP2; PPP1R2
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