Background: Protein phosphatase 5 (PP5) is a novel human protein serine/threonine phosphatase of molecular weight of 58 kDa. It is made up of a C-terminal phosphatase catalytic domain and an N-terminal domain, which has four repeats of 34 amino acids, three of which are tandemly arranged. The phosphatase domain contains all of the invariant motifs of the PP1/PP2A/PP2B gene family. However, it is not closely related to any other known member of this family of phosphatases. Thus it makes up a new subfamily of phosphatases. PP5 expressed in bacteria has been shown to dephosphorylate serine residues in proteins and is more sensitive than PP1 to the tumor promoter okadaic acid. PP5 appears to be localized to the nucleus suggesting that, like other nuclear tetratricopeptide (TPR)-containing proteins, it may playa role in the regulation of RNA biogenesis and mitosis.
Positive Control: A549 and MCF-7 cell lysates.
Purification Method: Ammonium Sulfate Precipitation.
Source: Rabbits were immunized with a Synthetic peptide derived from the human protein phosphatase 5 proteins.
References: 1. Chen, MX, et al. 'A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repear motifs and locaizes to the nucleus.' EMBO J. 1994, 13, 4278-4290.
2. Zuo, Z., et al. 'Ser/Thr protein phosphatase type 5 (PP5) is a negative regulator of glucocoricoid receptor-mediated growth arrest.' Biochemistry 1999, 38, 8849-8857
3. Chinkers, M., et al. 'Protein phosphatase 5 in signal transduction.' Trends Endocrinol. Metab. 2001, 12, 28-32.
UniProt: P53041 (Human).
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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