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>   首页   >   产品   >   一抗   >   癌症   >   PPP2CA Antibody (Center)   

PPP2CA Antibody (Center)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - PPP2CA Antibody (Center) AP20181c
    PPP2CA Antibody (Center) (Cat. #AP20181c) western blot analysis in mouse cerebellum tissue lysates (35ug/lane).This demonstrates the PPP2CA antibody detected the PPP2CA protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P67775
Other Accession P23696, P63331, P67777, P67776, P63330, P67774, NP_002706.1
Reactivity Human, Mouse
Predicted Bovine, Pig, Rabbit, Rat, Drosophila
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 35594 Da
Antigen Region 88-116 aa
Additional Information
Gene ID 5515
Other Names Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha, Replication protein C, RP-C, PPP2CA
Target/Specificity This PPP2CA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 88-116 amino acids from the Central region of human PPP2CA.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPPP2CA Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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, promotinh 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

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes an alpha isoform of the catalytic subunit.

REFERENCES

Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Jayadeva, G., et al. J. Biol. Chem. 285(39):29863-29873(2010)
Pradhan, S., et al. J. Biol. Chem. 285(38):29059-29068(2010)
Schmitz, M.H., et al. Nat. Cell Biol. 12(9):886-893(2010)
Antony, R., et al. J. Biol. Chem. 285(24):18301-18308(2010)

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