Positive control:
Lane 1: F9 cell lysate
Lane 2: PC-12 cell lysate
Lane 3: A431 cell lysate
Applications
-
WB
-
ICC
-
IF
-
IHC-P
-
IP
REACTIVITY
-
Human
-
Mouse
-
Rat
SPECIFICATIONS
Product Type
Recombinant Rabbit monoclonal primary
Product Name
Recombinant Phospho PP2A (Y307) Monoclonal Antibody (ET1609-40)
Immunogen
Synthetic phospho-peptide corresponding to residues surrounding tyr307 of human pp2a.
Host
Rabbit
Modification
Phospho
Modification Site
Y307
Positive Control
F9 cell lysate, PC-12 cell lysate, A431 cell lysate, PC-12, human pancreas tissue, mouse brain tissue, mouse pancreas tissue.
Conjugation
Unconjugated
Clonality
Monoclonal
Clone Number
ST49-05
PROPERTIES
Form
Liquid
Storage Condition
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
Storage Buffer
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Concentration
1 ug/ul
PURIFICATION
Protein A affinity purified.
MOLECULAR WEIGHT
35 kDa
Isotype
IgG
APPLICATION DILUTION
-
WB
-
1:1,000-1:5,000
-
ICC/IF
-
1:50-1:200
-
IHC-P
-
1:50-1:200
TARGET
UNIPROT #
PROTEIN NAME
Phospho-PP2A(Y307)
SYNONYMS
PP2A A antibody; PP2A alpha antibody; PP2A B antibody; PP2A beta antibody; PP2A-alpha antibody; PP2AA_HUMAN antibody; PP2Ac antibody; PP2CB antibody; PPP2CA antibody; PPP2CB antibody; Protein phosphatase 2 catalytic subunit alpha isoform antibody; Protein phosphatase 2 catalytic subunit beta isoform antibody; Replication protein C antibody; RP C antibody; RP-C antibody; Serine/threonine protein phosphatase 2A catalytic subunit alpha isoform antibody; Serine/threonine protein phosphatase 2A catalytic subunit beta isoform antibody; Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform antibody
SEQUENCE SIMILARITIES
Belongs to the PPP phosphatase family. PP-1 subfamily.
POST-TRANSLATIONAL MODIFICATION
Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.; Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation.; May be monoubiquitinated by NOSIP.
SUBCELLULAR LOCATION
Spindle pole, Nucleus, Cytoplasm, centromere.
FUNCTION
Protein phosphatase type 2A (PP2A) is an essential protein serine/threonine phosphatase that is conserved in all eukaryotes. PP2A is a key enzyme within various signal transduction pathways as it regulates fundamental cellular activities such as DNA replication, transcription, translation, metabolism, cell cycle progression, cell division, apoptosis and development. The core enzyme consists of catalytic C and regulatory A (or PR65) subunits, with each subunit represented by α and β isoforms. Additional regulatory subunits belong to four different families of unrelated proteins. Both the B (or PR55) and B' regulatory protein families contain α, β, γ and δ isoforms, with the B' family also including an ε protein. B'' family proteins include PR72, PR130, PR59 and PR48 isoforms, while striatin (PR110) and SG2NA (PR93) are both members of the B''' regulatory protein family. These B subunits competitively bind to a shared binding site on the core A subunit. This variable array of holoenzyme components, particularly regulatory B subunits, allows PP2A to act in a diverse set of functions. PP2A function is regulated by expression, localization, holoenzyme composition and post-translational modification. Phosphorylation of PP2A at Tyr307 by Src occurs in response to EGF or insulin and results in a substantial reduction of PP2A activity. Reversible methylation on the carboxyl group of Leu309 of PP2A has been observed. Methylation alters the conformation of PP2A, as well as its localization and association with B regulatory subunits.