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PPP2R1A (GeneName), Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (ProteinName), 2AAA_HUMAN.
Product Name:

Human PPP2R1A/ Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform Recombinant Protein

 
Cat.#:
-
Brand:
EIAab®
Regulatory Status:
Alternative:

Medium tumor antigen-associated 61 kDa protein,PP2A subunit A isoform PR65-alpha,PP2A subunit A isoform R1-alpha

Source:
E.coli
Species:
Human
Tags:
His
Purity:
>90% by SDS-PAGE
Concentration:
Reconstitution Dependent
Form:
Liquid
Storage Buffer:
50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole,10%glycerol(PH8.0)
Storage:
Store at -20°C. (Avoid repeated freezing and thawing.)
Research Area:
Cancer
Human PPP2R1A Protein
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Human PPP2R1A Protein
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Product Datasheets
Instruction:
MSDS:


General Annotation


Sub Unit:
Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (By similarity). PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9. Interacts with TP53 and SGO1. Interacts with PLA2G16; this interaction might decrease PP2A activity. Interacts with CTTNBP2NL.


Function:
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis.


Subcellular Location:
Cytoplasm Chromosome Centromere Centromeric localization requires the presence of BUB1.


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