Protein Phosphatase 2A (PP2A) is a protein that belongs to serine/threonine-specific protein phosphatases family. It has a pivotal role in several cellular processes like DNA replication, transcription, RNA splicing, translation, cellular metabolism, cell-cycle progression, morphogenesis, development and transformation. Anti-serine/threonine protein phosphatase 2 A/A antibody can be used for detecting protein phosphatase 2A/A isoforms by using immunoprecipitation. It can also be used in immunocytochemistry. Rabbit anti-serine/threonine protein phosphatase 2 A/A antibody reacts specifically with protein phosphatase 2A/A isoforms (65kD) from mouse, bovine, rat and human.
Immunogène
synthetic peptide corresponding to the N-terminus (amino acids 7-19) of the protein phosphatase 2A structural subunit.
Application
Anti-serine/threonine protein phosphatase 2 A/A antibody can be used in western blotting using total rat brain homogenate. It can also be used in microarray.
Forme physique
Solution in phosphate buffered saline containing 0.08% sodium azide.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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
Serine/threonine protein phosphatases.
S Wera et al.
The Biochemical journal, 311 ( Pt 1), 17-29 (1995-10-01)
Polish journal of veterinary sciences, 16(4), 663-669 (2013-01-01)
Changes in the level of cellular proteins in cells inoculated with equine influenza virus H7N7 and H3N8 were studied with microarray technique. H3N8 induced pro-apoptotic proteins while H7N7 induced both pro- as well as anti-apoptotic factors. The higher level of
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