P8859
Anti-Protein Phosphatase X/C Interior antibody produced in sheep
IgG fraction of antiserum, buffered aqueous solution
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About This Item
biological source
sheep
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~34 kDa
species reactivity
mouse, rat, bovine, human
technique(s)
immunocytochemistry: suitable
western blot: suitable
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PPP4C(5531)
mouse ... Ppp4c(56420)
rat ... Ppp4c(171366)
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 X/C (or PP4) is a member of PP2A subfamily and shares 65% structural idENTITY_TYPE_CODE with PP2A in humans. PPX/C is actively involved in regulation of growth and organization of microtubule at the centrososmes and centrosome maturation during cell division by mitosis and meiosis. PPX/C reportedly has a pro-apoptotic role in T lymphocytes. PPX/C takes part in important cellular processes through signaling pathways involving NF-κB and c-Jun N-terminal kinase
Anti-Protein Phosphatase X/C Interior recognizes an internal sequence of protein phosphatase XCatalytic domain (34 kDa).
Anti-Protein Phosphatase X/C Interior recognizes an internal sequence of protein phosphatase XCatalytic domain (34 kDa).
Immunogen
highly purified peptide corresponding to amino acid residues 289-302 of protein phosphatase X/C.
Application
Anti-Protein Phosphatase X/C is suitable for immunoblotting at a working dilution of 1:500-1:1000. The recommended dilution for immunocytochemistry is 1:500-1:1000.
Physical form
Solution supplied at 1 mg/mL in phosphate buffered saline with 0.08% sodium azide.
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Storage Class
10 - Combustible liquids
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Protein phosphatase 4 is required for centrosome maturation in mitosis and sperm meiosis in C. elegans
Sumiyoshi E et al
Journal of Cell Science, 15, 1403-1410 (2002)
Guisheng Zhou et al.
The Journal of biological chemistry, 277(8), 6391-6398 (2001-11-08)
Protein phosphatase 4 (PP4, previously named protein phosphatase X (PPX)), a PP2A-related serine/threonine phosphatase, has been shown to be involved in essential cellular processes, such as microtubule growth and nuclear factor kappa B activation. We provide evidence that PP4 is
M C Hu et al.
The Journal of biological chemistry, 273(50), 33561-33565 (1998-12-05)
Nuclear factor kappaB (NF-kappaB) and the Rel family of proteins are pleiotropic transcription factors that play central roles in the immune and inflammatory responses, as well as apoptosis. Here, we identified a serine/threonine protein phosphatase X (PPX; also called protein
Kathie A Mihindukulasuriya et al.
The Journal of biological chemistry, 279(45), 46588-46594 (2004-08-28)
Protein phosphatase 4 (PP4; also named PPX or PPP4) is a PP2A-related protein serine/threonine phosphatase with important roles in a variety of cellular processes such as microtubule growth/organization, apoptosis, tumor necrosis factor (TNF)-alpha signaling, and activation of c-Jun N-terminal kinase
M Mourtada-Maarabouni et al.
Cell death and differentiation, 10(9), 1016-1024 (2003-08-23)
Functional expression cloning strategies are highly suitable for the analysis of the molecular control of apoptosis. This approach has two critical advantages. Firstly, it eliminates prior assumptions about the properties of the proteins involved, and, secondly, it selectively targets proteins
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