|Product Name||Anti-PP2A-alpha/PPP2CA Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, 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.|
|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.|
|Cite This Product||Anti-PP2A-alpha/PPP2CA Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1068)|
|Contents/Buffer||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.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Rat, Mouse, By Heat
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti-PP2A-alpha antibody, PA1068, Western blotting
All lanes: Anti PP2A-alpha(PA1068) at 0.5ug/ml
Lane 1: Rat kidney Tissue Lysate at 50ug
Lane 2: HELA Whole Cell Lysate at 40ug
Predicted bind size: 36KD
Observed bind size: 36KD
Anti-PP2A-alpha antibody, PA1068, IHC(P)
IHC(P): Human Mammary Cancer Tissue
Anti-PP2A-alpha antibody, PA1068, IHC(P)
IHC(P): Rat Kidney Tissue
Protein Target Info (Source: Uniprot.org)
|Protein Name||Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform|
|Alternative Names||Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;PP2A-alpha;126.96.36.199;Replication protein C;RP-C;PPP2CA;|
|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). .|
|Molecular Weight||35594 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. .|
|Research Areas||Cancer, Cardiovascular, Cell Biology, Cell Cycle, Contractility, Cytoplasmic, Epigenetics And Nuclear Signaling, Intracellular Signaling, Kinases/Phosphatases, Neuroscience, Neurotransmission, Protein Phosphorylation, Ser / Thr Phosphatases, Signal Transduction, Signaling Pathways, Stem Cells, Tgf Beta
*You can search these to find other products in these research areas.
|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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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,