PP2A alpha + beta Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of PP2A alpha + beta on different lysates using anti-PP2A alpha + beta antibody at 1/1,000 dilution.
Lane 1: A431
Lane 2: NIH/3T3
Lane 3: 293T
Fig2: ICC staining PP2A alpha + beta in PANC-1 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Fig3: ICC staining PP2A alpha + beta in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Host Species; Species ReactivityRabbit; Human, Mouse, Rat, Zebrafish
Application SummaryWB, ICC, IHC, IP
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesSerine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, Replication protein C, Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
BackgroundThe catalytic subunit of protein phosphatase 2A (PP2A) is inactivated by in vitro phosphorylation of Tyr-307 by receptor and nonreceptor protein tyrosine kinases. The catalytic subunit of PP2A is phosphorylated by tyrosine-specific protein kinases and associates with a variety of regulatory subunits. Phosphorylation is enhanced in the presence of the phosphatase inhibitor okadaic acid, consistent with an autodephosphorylation reaction. Phosphorylation is catalyzed by p60v-src, p56lck, epidermal growth factor receptors, and insulin receptors. Transient deactivation of PP2A might enhance transmission of cellular signals through kinase cascades within cells. In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases.(ET1611-54)