P8359
Anti-Serine/Threonine Protein Phosphatase 2 A/B′ pan2 antibody produced in rabbit
~1 mg/mL, IgG fraction of antiserum, buffered aqueous solution
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About This Item
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 56 kDa
species reactivity
rat
concentration
~1 mg/mL
technique(s)
microarray: suitable
western blot: 1:500-1:1,000 using total rat brain homogenate
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
rat ... Ppp2r2b(60660)
General description
Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. Protein phosphatase 2A (PP2A) holozyme consists of a catalytic subunit (C), a structural subunit (A) and a regulatory subunit (B). The subunit B dictates the substrate specificity and is coded by at least 13 genes resulting in 3 distinct classes of subunits – B, B′ and B”. Members of the B′/B56/PR61 family regulatory subunits of PP2A determine the subcellular localization, substrate specificity, and catalytic activity of PP2A in a wide range of biological processes. B′/B56/PR61 are reportedly involved in major signaling pathways such as Wnt, Hedgehog and planar cell polarity pathway
Anti-serine/threonine protein phosphatase 2A/B′ pan 2 recognizes an epitope common to the ~56 kDa protein phosphatase 2A B′ subunits from rat brain.
Anti-serine/threonine protein phosphatase 2A/B′ pan 2 recognizes an epitope common to the ~56 kDa protein phosphatase 2A B′ subunits from rat brain.
Immunogen
synthetic peptide (VSSPHFQVAERALY) corresponding to the N-terminus of the protein phosphatase 2A/B′ pan2 subunit.
Application
Anti-protein phosphatase 2A/B′ Pan 2 antibody may be used for immunoblotting at a working dilution of 1:500-1:1000 in total rat brain homogenate. The antibody is suitable for protein microarray.
Physical form
Solution in phosphate buffered saline containing 0.08% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
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Michael Hannus et al.
Development (Cambridge, England), 129(14), 3493-3503 (2002-07-02)
We have identified widerborst (wdb), a B' regulatory subunit of PP2A, as a conserved component of planar cell polarization mechanisms in both Drosophila and in zebrafish. In Drosophila, wdb acts at two steps during planar polarization of wing epithelial cells.
J M Seeling et al.
Science (New York, N.Y.), 283(5410), 2089-2091 (1999-03-26)
Dysregulation of Wnt-beta-catenin signaling disrupts axis formation in vertebrate embryos and underlies multiple human malignancies. The adenomatous polyposis coli (APC) protein, axin, and glycogen synthase kinase 3beta form a Wnt-regulated signaling complex that mediates the phosphorylation-dependent degradation of beta-catenin. A
Hongge Jia et al.
Development (Cambridge, England), 136(2), 307-316 (2008-12-18)
The seven-transmembrane protein Smoothened (Smo) and Zn-finger transcription factor Ci/Gli are crucial components in Hedgehog (Hh) signal transduction that mediates a variety of processes in animal development. In Drosophila, multiple kinases have been identified to regulate Hh signaling by phosphorylating
Jing Yang et al.
Life sciences, 87(23-26), 659-666 (2010-10-12)
Members of the B'/B56/PR61 family regulatory subunits of PP2A determine the subcellular localization, substrate specificity, and catalytic activity of PP2A in a wide range of biological processes. Here, we summarize the structure and intracellular localization of B56-containing PP2As and review
V Janssens et al.
The Biochemical journal, 353(Pt 3), 417-439 (2001-02-15)
Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate
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