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Anti-PP2A-alpha Antibody
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Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P67775 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform(PPP2CA) detection. Tested with WB, IHC-P in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 5515 |
|---|---|
| Other Names | Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha, 3.1.3.16, Replication protein C, RP-C, PPP2CA |
| Calculated MW | 35594 Da |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Rat, Mouse, By Heat Western blot, 0.1-0.5 µg/ml, Human, Rat, Mouse |
| Subcellular Localization | Cytoplasm . Nucleus . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle pole . In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 (By similarity). . |
| Source | Eukaryota |
| Protein Name | Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform(PP2A-alpha) |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human PP2A-alpha(6-20aa FTKELDQWIEQLNEC), identical to the related rat and mouse sequences. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | PPP2CA |
|---|---|
| Function | Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events (PubMed:10801873, PubMed:12473674, PubMed:17245430, PubMed:22613722, PubMed:33243860, PubMed:34004147, PubMed:9920888). PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (PubMed:22613722). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase (PubMed:22613722). Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate various proteins, such as SV40 large T antigen, AXIN1, p53/TP53, PIM3, WEE1 (PubMed:10801873, PubMed:12473674, PubMed:17245430, PubMed:9920888). Activates RAF1 by dephosphorylating it at 'Ser-259' (PubMed:10801873). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (PubMed:33108758). Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis: interaction with AMBRA1 enhances interaction between PPP2CA and MYC (PubMed:25438055). Mediates dephosphorylation of FOXO3; promoting its stabilization: interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3 (PubMed:30513302). Catalyzes dephosphorylation of the pyrin domain of NLRP3, promoting assembly of the NLRP3 inflammasome (By similarity). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). Catalyzes dephosphorylation of PIM3, promoting PIM3 ubiquitination and proteasomal degradation (PubMed:12473674). Part of the striatin- interacting phosphatase and kinase (STRIPAK) complexes (PubMed:33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:33633399). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:33633399). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex (PubMed:33243860, PubMed:34004147, PubMed:37080207). The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, PPP2CA catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, thereby preventing transcriptional elongation (PubMed:33243860, PubMed:34004147, PubMed:37080207). |
| Cellular Location | Cytoplasm. Nucleus. Chromosome. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle pole. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres (PubMed:16541025). During mitosis, also found at spindle poles (PubMed:16541025). Centromeric localization requires the presence of SGO2 (By similarity). Recruited to chromatin and transcription pause-release checkpoint via its association with the Integrator complex (PubMed:33243860, PubMed:34004147). {ECO:0000250|UniProtKB:P63330, ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:33243860, ECO:0000269|PubMed:34004147} |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The catalytic subunit of human protein phosphatase 2A(PPP2CA) encodes a 309-amino acid polypeptide.It is localized to chromosome 5. The gene(approximately 30 kbp) is composed of seven exons and six introns. It is predicted to be important for phosphatase enzymatic activity. Methylation of the C-terminal leucine residue(Leu309) of protein serine/threonine phosphatase 2A catalytic subunit(PP2AC) is known to regulate catalytic activity in vitro. Furthermore, PP2A has a fundamental role in cardiac function, and suggests that disturbances in protein phosphatase expression and activity may cause or exacerbate the course of cardiac diseases.
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