Recombinant Human Serine/threonine-protein phosphatase 2A activator (PTPA)

• Product Name Alternative:

  PP2A, subunit B', PR53 isoform Phosphotyrosyl phosphatase activator

• Abbreviation:

  Recombinant Human PTPA protein

• Gene Name:

  PTPA

• UniProt:

  Q15257

• Expression Region:

  2-358aa

• Organism:

  Homo sapiens (Human)

• Target Sequence:

  AEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEMWNEVHEEKEQAAKQSVSCDECIPLPRAGHCAPSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG

• Tag:

  N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged

• Type:

  Developed Protein

• Source:

  E.coli

• Field of Research:

  Others

• 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.

• Endotoxin:

  Not test

• Purity:

  Greater than 90% as determined by SDS-PAGE.

• Activity:

  Not Test

• 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.

• 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)

• Molecular Weight:

  60.5 kDa

• References & Citations:

  "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)

• Storage Conditions:

  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.

• Protein Length:

  Full Length of Mature Protein