Protein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate -based phosphatases.

Protein phosphatase 1 (PP1) catalyzes more than half of all phosphoserine/threonine dephosphorylation reactions in mammalian cells. In vivo PP1 does not exist as a free catalytic subunit but is always associated with at least one regulatory ...

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Jan 15, 2002 · Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits.

PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription.

Antibodies that detect PP1 beta can be used in several scientific applications, including Western Blot, Immunohistochemistry, Immunocytochemistry, Immunoprecipitation and ELISA. These antibodies target PP1 beta in Human, Rat, Mouse, Bovine and Non-human primate samples.

Protein phosphatase type 1 (PP1) forms a wide range of Ser/Thr-specific phosphatase holoenzymes which contain one catalytic subunit (PP1c), present in all eukaryotic cells, associated with variable subunits known as regulatory proteins.

Protein phosphatase 1 belongs to the PPP family of phosphatases and is involved in the regulation of a wide variety of cellular processes ranging from intermediary metabolism to apoptosis.

Invitrogen Anti-PP1 alpha Polyclonal, Catalog # PA5-83841. Tested in Western Blot (WB), Immunocytochemistry (ICC/IF) and Immunohistochemistry (Paraffin) (IHC (P)) applications. This antibody reacts with Human samples. Supplied as 100 µL purified antibody (0.3 mg/mL).

Rat cDNAs encoding neuronal isoforms of protein phosphatase 1 (PP1) were isolated and their primary structures elucidated. The derived amino acid sequences allowed us to design synthetic C-terminal peptides that were used to raise antibodies.