Recombinant Human Serine/Threonine-Protein Phosphatase 2A Activator (PTPA) Protein (His-SUMO&Myc)

Name: Recombinant Human Serine/Threonine-Protein Phosphatase 2A Activator (PTPA) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-08874P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Serine/Threonine-Protein Phosphatase 2A Activator (PTPA) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q15257
Target Symbol	PTPA
Synonyms	subunit B''; KIAA0044; MGC2184; Phosphotyrosyl phosphatase activator; PP2A; PP2A phosphatase activator; PP2A subunit B'; PP2A subunit B' isoform PR53; PP2A subunit B' PR53 isoform; PPP2R4; PR53; PR53 isoform; Protein phosphatase 2, regulatory subunit B-prime; Protein phosphatase 2A activator regulatory subunit 4; Protein phosphatase 2A regulatory subunit B' (PR 53); PTPA; PTPA_HUMAN; Serine/threonine protein phosphatase 2A regulatory subunit B'; Serine/threonine-protein phosphatase 2A activator; Serine/threonine-protein phosphatase 2A regulatory subunit 4; Serine/threonine-protein phosphatase 2A regulatory subunit B''
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	AEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEMWNEVHEEKEQAAKQSVSCDECIPLPRAGHCAPSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG
Expression Range	2-358aa
Protein Length	Full Length of Mature Protein
Mol. Weight	60.5kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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+). 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):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	PTPA-type PPIase family
Database References	HGNC: 9308 OMIM: 600756 KEGG: hsa:5524 UniGene: PMID: 28300193 Study reveals the mechanism controlling abscission through integration of Aurora B kinase and B56-bound PP2A phosphatase activities on the kinesin motor protein MKlp2. MKlp2 is an essential protein for promoting abscission, which may regulate tethering and stabilizing of the PM to the microtubule cytoskeleton at the intercellular bridge through its previously uncharacterized lipid association motif. PMID: 27939310 These results suggest that loss of specific PP2A regulatory subunits is functionally important in breast tumourigenesis, and support strategies to enhance PP2A activity as a therapeutic approach in breast cancer. PMID: 28744751 High expression of PP2A is associated with cisplatin resistant gastric cancer. PMID: 28534965 Study identifies Eya3 as a regulator of PP2A, a major cellular Ser/Thr phosphatase, and uncovers a mechanism of controlling the stability of a critical oncogene, c-Myc. PMID: 29535359 Authors demonstrated CFTR and PP2AA interact in the cytosol, resulting in PP2A complex inactivation and increased degradation of PP2A substrates via the lysosomal/proteasome pathway. PMID: 28445932 Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A disinhibition. PMID: 28613156 An imbalanced regulation in protein kinases and protein phosphatases is the direct cause of tau hyperphosphorylation in Alzheimer's disease; GSK-3beta and PP2A are the most implicated. (Review) PMID: 28585125 Isoliensinine suppresses NF-kappaB in hepatocellular carcinoma cells through impairing PP2A/I2PP2A interaction and stimulating PP2A-dependent p65 dephosphorylation at Ser536 PMID: 27244888 BIR domain of XIAP activated the protein phosphatase 2 (PP2A) activity by decreasing the phosphorylation of PP2A at Tyr307 in its catalytic subunit, PP2A-C. Such activated PP2A prevented the deviant phosphorylation and activation of MAPK kinases/MAPKs, their downstream effector c-Jun; and in turn inhibiting transcription of c-Jun-regulated miR-200a PMID: 28057023 T-type channel signaling is redirected towards the activation of the kinase Akt1, leading to increased expression of the anti-apoptotic protein survivin, and a decrease in the pro-apoptotic mediator FoxO3A. Finally, in iPAH cells, Akt1 is no longer able to regulate caspase 9 activation, whereas T-type channel overexpression reverses PP2A defect in iPAH cells but reinforces the deleterious effects of Akt1 activation PMID: 28655554 The present results indicate that rs959627 predicts PPP2R2 B mRNA prefrontal expression in two independent post-mortem datasets as well as lateral prefrontal activity during working memory in healthy subjects and suggest that genetic modulation of signal transduction mediated by PP2A affects complex biological phenotypes of relevance for cognitive behavior. PMID: 27591184 the present study suggested that PP2A has an important role in regulating mast cell beta2-adrenoceptors PMID: 28090813 The results of this study demonstrated that HBx of hepatitis B virus impairs interferon signaling via increased expression of SOCS3 and PP2A. PMID: 27459003 The current study describes a novel pathogenic mechanism of action for human polyomavirus 6 small tumor (sT) antigen which involves binding to protein phosphatase 2A (PP2A) via its WFG motif and zinc binding sites for activation of PP2A's downstream oncogenic pathways (MEK/ERK/c-Jun). PMID: 27632801 The aim of this review is to shed light on the role of four different phosphatases (PTEN, PP2A, CDC25 and DUSP1) in five different solid tumors (breast cancer, lung cancer, pancreatic cancer, prostate cancer and ovarian cancer), in order to better understand the most frequent and aggressive primary cancer of the central nervous system, glioblastoma. PMID: 28801478 Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 PMID: 28174209 Such effect by miR-429 was again abolished with AMPKalpha1 silence or mutation. Together, we propose that PP2A-c silence by miR-429 activates AMPK and protects osteoblastic cells from Dex. PMID: 28438603 PTPalpha is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V) and could be a factor regulating promotion of migration in breast cancer cells PMID: 27965091 This article reviews the involvement of PP2A in the regulation of three cell signaling pathways: wnt, mTOR and MAP kinase, as well as the G1-->S transition, DNA synthesis and mitotic initiation. These processes are all crucial for proper cell survival and proliferation and are often deregulated in cancer and other diseases. [review] PMID: 26906453 PP2A-B55 substrates were identified and assigned their temporal order in mitotic exit. PMID: 27551054 Our results provide a novel mechanistic insight into the activation of Myc by 27-HC via transcriptional repression of PP2A, SCP1 and FBW7 to increase Myc protein stability in breast cancer cells. PMID: 27751849 Data show that the truncation promotes glycogen synthase kinase-3beta (GSK-3beta) nuclear translocation and enhances its interaction with protein phosphatase 2A (PP2A), leading to dephosphorylation. PMID: 28267204 that KAP1 phosphorylation is decreased following recruitment of PP2A by URI. PMID: 27780869 These results provide direct evidence for the rapid response of PP2A catalytic activity to extracellular insulin stimulation, as well as insight into the complex regulation of phosphorylation levels by opposing kinase and phosphatase activities within the cell. PMID: 27805358 LPS tolerance interferes with TLR4 signaling by inhibiting Lyn and c-Src phosphorylation and their recruitment to TLR4, while increasing the phosphatase activity and expression of PP2A, PTPN22, PTP1B and MKP1. PMID: 26457672 we propose that RhoB could be responsible for early metastatic prevention by inhibiting the EMT-derived invasiveness of lung cells through the control of PP2A activity. PMID: 26148238 Cohesin complex is shown to be a target of the prophase pathway at centrosomes and protected by Sgo1-dependent PP2A recruitment. PMID: 26365192 Zinc-alpha2-glycoprotein modulates AKT-dependent insulin signaling in adipocytes by activation of the PP2A phosphatase. PMID: 26068931 these data reveal the molecular mechanisms of PP2A regulation and highlight the potential of boosting the power of endogenous phosphatases as novel anti-inflammatory strategies to combat asthmatic inflammation. PMID: 25985190 Transgenic overexpression of myocardial PP2A causes adverse remodeling which coincides with a disruption of the classical Akt/GSK3/beta-catenin pathway under baseline conditions that is restored to normal values in chronic myocardial infarction. PMID: 25662052 an increase in the phosphorylation level of PTPalphaTyr789 by its upstream activator, FAKDel33, leading to Src activation in certain breast cancer cells, which has significant implications for metastatic potential. PMID: 25625869 results suggested that PPFIA1 functioned with PP2A to promote the dephosphorylation of Kif7, triggering Kif7 localization to the tips of primary cilia and promoting Gli transcriptional activity. PMID: 25492966 The roles of protein phosphatases including MAPK phosphatase-1 (MKP-1) and protein phosphatase type 2A (PP2A) in modulating p38MAPK activation and downstream TNF-alpha expressions in primary human monocyte-derived macrophages, were examined. PMID: 23549267 The invariant C-terminal residues of the catalytic subunit can act as affinity enhancer for different PP2A interaction partners, including PTPA, and a different 'code' of posttranslational modifications can favour interactions to one subunit over others. PMID: 25003389 REDD1 may act as a targeting protein for the catalytic subunit of PP2A PMID: 25056877 We have also defined in the actin-binding protein cofilin-1 a link between PP2A, actin cytoskeleton, and necrotic death PMID: 25096578 PP2A is activated upon CK2 activation and acts as the dephosphorylating agent for pStat3S727. PMID: 24726840 we investigated whether down-regulation of PTPA affects cell viability and the underlying mechanismswe investigated whether down-regulation of PTPA affects cell viability and the underlying mechanisms PMID: 24821282 Hyperphosphorylation of PP2A is associated with colorectal cancer. PMID: 24997451 PTPA stabilizes a conformation of apo- PP2Ac that facilitates metal chelation and ATP binding and hydrolysis, whereby the precise geometry of ATP binding at the active site is important for selectively enhanced binding of proper catalytic metal ions. PMID: 24100351 These data point to PP2A-B56gamma-driven Ras signaling modulation in G2 as essential for suppressing aberrant cyclin E expression during mitosis and thereby achieving normal G0 control. PMID: 24857551 The presence of full-length SET in the neuronal cytoplasm is sufficient to impair PP2A methylation and activity, leading to tau hyperphosphorylation. PMID: 24981783 the A/Balpha/C holoenzyme form of PP2A is essential in EC barrier integrity both in micro- and macrovascular EC PMID: 23721711 Authors show that PP2Ac associates with Jak1/Tyk2/STAT1 and reduces Jak1/Tyk2/STAT1 phosphorylation resulting in an impairment of the IFNalpha-induced hepatitis C virus antiviral response. PMID: 23910645 Plant homeodomain finger protein 20 (PHF20) maintains NF-kappaB in an active state in the nucleus by inhibiting the interaction between PP2A and p65. PMID: 23797602 results suggest that Notch1 can regulate PP2A dephosphorylation of critical cellular regulators including AKT, AMPKalpha, and p70S6K PMID: 23788636 results identify downregualtion of PP2A activity as an important protective mechanism of melanoma cells against ER stress-induced apoptosis PMID: 22739989 Our data indicate that PTPA may activate PP2A through activating PTP1B and thus reducing the level of P-PP2AC, therefore upregulation of PTPA may represent a potential strategy in rescuing PP2A and arresting tau pathology in AD. PMID: 23428800 expanded CAG repeats bind to a translation regulatory protein complex containing MID1, protein phosphatase 2A and 40S ribosomal S6 kinase. PMID: 23443539

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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