Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. Protein phosphatase 2A (PP2A) holozyme consists of a catalytic subunit (C), a structural subunit (A) and a regulatory subunit (B). The subunit B dictates the substrate specificity and is coded by at least 13 genes resulting in 3 distinct classes of subunits - α, β and γ. The B α subunit is targeted to the microtubules, renders substrate specificty and dephosphorylates cyclin-dependent kinase sites. The PP2A holoenzyme has been implicated in various functions such as cell cycle progression, oncogenic transformation and is subjected to tight regulation at the translational level, by post translational modifications and by protein-protein interations. Anti-Serine/Threonine Protein Phosphatase 2A/Bα recognizes protein phosphatase 2A/Bα?isoforms of 55 kDa.
Immunogen
synthetic peptide (FSQVKGAVDDDVAE) corresponding to the N-terminus (amino acids 14-27) of the protein phosphatase 2A/Bα subunit.
Application
Anti-Serine/Threonine Protein Phosphatase 2A/B α may be used for detection at working concentration of 5-10 μg/mL in total rat brain homogenate. The antibody is also suitable for immunocytochemistry at a working concentration of 5-10 μg/mL.
Physical form
Provided as a 0.2 μm filtered solution in phosphate buffered saline containing 0.08% sodium azide.
Molecular and cellular biology, 14(7), 4616-4623 (1994-07-01)
The ability of simian virus 40 (SV40) large T antigen to catalyze the initiation of viral DNA replication is regulated by its phosphorylation state. Previous studies have identified the free catalytic subunit of protein phosphatase 2A (PP2Ac) as the cellular
Trends in cell biology, 4(8), 287-291 (1994-08-01)
Protein phosphorylation is probably the major regulatory mechanism employed by eukaryotic cells. Much work has been devoted to the role of protein kinases and their modulation by hormones, growth factors and neurotransmitters. It is now appreciated that protein phosphatases are
The Biochemical journal, 353(Pt 3), 417-439 (2001-02-15)
Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate
Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine- and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.