Serine/threonine-protein phosphatase 2A activator (PTPA), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 2-358aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged. Target Protein Sequence: AEGERQPPPD SSEEAPPATQ NFIIPKKEIH TVPDMGKWKR SQAYADYIGF ILTLNEGVKG KKLTFEYRVS EMWNEVHEEK EQAAKQSVSC DECIPLPRAG HCAPSEAIEK LVALLNTLDR WIDETPPVDQ PSRFGNKAYR TWYAKLDEEA ENLVATVVPT HLAAAVPEVA VYLKESVGNS TRIDYGTGHE AAFAAFLCCL CKIGVLRVDD QIAIVFKVFN RYLEVMRKLQ KTYRMEPAGS QGVWGLDDFQ FLPFIWGSSQ LIDHPYLEPR HFVDEKAVNE NHKDYMFLEC ILFITEMKTG PFAEHSNQLW NISAVPSWSK VNQGLIRMYK AECLEKFPVI QHFKFGSLLP IHPVTSG. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg2+. Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg2+ (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis, the function appears to be independent from PP2A. Reference: "Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A." Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J., Merlevede W., Goris J. Genomics 28:261-272(1995). Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D)