Recombinant Human Serine/threonine-protein phosphatase 2A activator (PTPA)
Product Specifications
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
Available Sizes
Curated Selection
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