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Cell Signaling Technology Inc
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PASCO
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New England Biolabs
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PASCO
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PASCO
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KRUSS GmbH
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IRS1 pS323 Antibody is a Rabbit Polyclonal against IRS1 pS323
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The CDC25B p Ser323 Antibody from Novus Biologicals is a rabbit polyclonal antibody to CDC25B This antibody reacts with human mouse The CDC25B p Ser323 Antibody has been validated for the following applications Western Blot
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TRF2 pS323 Antibody is a Rabbit Polyclonal against TRF2 pS323
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This gene encodes a protein that is similar to a serine threonine kinase in C elegans which is involved in axonal elongation The structure of this protein is similar to the C elegans protein in
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MKP 1 pS323 Antibody is a Rabbit Polyclonal against MKP 1 pS323
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Image Search Results
Journal: Nature Communications
Article Title: Proximity proteomics identifies PAK4 as a component of Afadin–Nectin junctions
doi: 10.1038/s41467-021-25011-w
Figure Lengend Snippet: a Schematic of PAK4-BirA*GFP constructs used for SILAC BioID analysis. Summary of workflow used to identify PAK4-proximal proteins using stable cell lines cultured in either Arg/Lys isotopically heavy (H) or light (L) containing media as indicated. b Total lysate from control and PAK4-BirA*GFP cell lines were subjected to western blot to compare the expression of PAK4-BirA*GFP versus endogenous PAK4 (arrow) and repeated in two independent experiments. c Disposition of PAK4-BirA-GFP in stable U2OS cell lines. Cells were fixed in PFA and immuno-stained for anti-GFP and anti-p120 ctn . Source data are provided as a Source Data file.
Article Snippet: Primary antibodies were obtained from the following sources: rabbit PAK4 (Proteintech 14685-1-AP); mouse p120-catenin (Santa Cruz sc-23873); rabbit β-catenin (Cell Signaling #9582S); mouse β-catenin (Santa Cruz sc-7963); rabbit Afadin (Sigma A0224); mouse Afadin (R&D Systems MAB78291); rat ZO-1 (Santa Cruz sc-33725); rabbit LZTS2 (Proteintech 15677-1-AP); rabbit DLG5 (Abcam ab86783), rabbit Scribble (Santa Cruz sc-28737),
Techniques: Construct, Multiplex sample analysis, Stable Transfection, Cell Culture, Control, Western Blot, Expressing, Staining
Journal: Nature Communications
Article Title: Proximity proteomics identifies PAK4 as a component of Afadin–Nectin junctions
doi: 10.1038/s41467-021-25011-w
Figure Lengend Snippet: List of SILAC-enriched PAK4-proximal proteins.
Article Snippet: Primary antibodies were obtained from the following sources: rabbit PAK4 (Proteintech 14685-1-AP); mouse p120-catenin (Santa Cruz sc-23873); rabbit β-catenin (Cell Signaling #9582S); mouse β-catenin (Santa Cruz sc-7963); rabbit Afadin (Sigma A0224); mouse Afadin (R&D Systems MAB78291); rat ZO-1 (Santa Cruz sc-33725); rabbit LZTS2 (Proteintech 15677-1-AP); rabbit DLG5 (Abcam ab86783), rabbit Scribble (Santa Cruz sc-28737),
Techniques: Multiplex sample analysis, Binding Assay
Journal: Nature Communications
Article Title: Proximity proteomics identifies PAK4 as a component of Afadin–Nectin junctions
doi: 10.1038/s41467-021-25011-w
Figure Lengend Snippet: a Confluent MDCK cells grown on glass coverslips (4 days) were fixed with methanol and co-stained using rabbit anti-PAK4 and mouse anti-Afadin/anti-β-catenin or anti-ZO1. Images were collected on an Olympus Fluoview confocal microscope with ×100 oil objective. Lower panels show MDCK cell grown in Matrigel to form 3D-cultured acini (8 days) fixed in methanol and immuno-stained with anti-PAK4, anti-p120ctn (×60 objective). b Sub-confluent (2 day) cells were stained using rabbit antibodies specific for PAK4 and mouse antibody specific for p120 (×60 objective). Repeated in three independent experiments. Scale bars: 10 μm.
Article Snippet: Primary antibodies were obtained from the following sources: rabbit PAK4 (Proteintech 14685-1-AP); mouse p120-catenin (Santa Cruz sc-23873); rabbit β-catenin (Cell Signaling #9582S); mouse β-catenin (Santa Cruz sc-7963); rabbit Afadin (Sigma A0224); mouse Afadin (R&D Systems MAB78291); rat ZO-1 (Santa Cruz sc-33725); rabbit LZTS2 (Proteintech 15677-1-AP); rabbit DLG5 (Abcam ab86783), rabbit Scribble (Santa Cruz sc-28737),
Techniques: Staining, Microscopy, Cell Culture
Journal: Nature Communications
Article Title: Proximity proteomics identifies PAK4 as a component of Afadin–Nectin junctions
doi: 10.1038/s41467-021-25011-w
Figure Lengend Snippet: The sub-apical complex includes a structure recently described as well the tight junction (TJ) and region ‘below’ this typically described adherens junction (AJ), which includes both Afadin and cadherin complexes. The smaller cadherin punctate junctions along the lateral contacts are not explicitly indicated. Typical non-transmembrane components (for example, p120ctn and β-catenin) are often used as markers and these are indicative of well-studied components. The Afadin/nectin compartment in vertebrates is often spatially segregated from cadherin as described in the text.
Article Snippet: Primary antibodies were obtained from the following sources: rabbit PAK4 (Proteintech 14685-1-AP); mouse p120-catenin (Santa Cruz sc-23873); rabbit β-catenin (Cell Signaling #9582S); mouse β-catenin (Santa Cruz sc-7963); rabbit Afadin (Sigma A0224); mouse Afadin (R&D Systems MAB78291); rat ZO-1 (Santa Cruz sc-33725); rabbit LZTS2 (Proteintech 15677-1-AP); rabbit DLG5 (Abcam ab86783), rabbit Scribble (Santa Cruz sc-28737),
Techniques:
Journal: Nature Communications
Article Title: Proximity proteomics identifies PAK4 as a component of Afadin–Nectin junctions
doi: 10.1038/s41467-021-25011-w
Figure Lengend Snippet: a To assess the effect of single amino-acid substitution on a selected optimal PAK4 substrate, we tested 13aa synthetic peptides (Pepspots, Jerini) derived from PAK4 pseudosubstrate motif (SARRPKPLVDPAD) in which the proline in bold is replaced by Ser(0). This is similar to an optimal substrate for PAKs (RKRRNSLAYKK) termed PAKtide but optimal for kinase binding. Based on structural considerations the Arg side chain at position −2 or −3 occupies a pocket that mediates interactions found in PAKs and other S/T kinases, including PKA . The contribution of each side-chain to peptide phosphorylation was assessed by sequential alanine substitution. b We selected in vivo basic-directed phosphorylation sites identified in Afadin, scribble, ZO-1, DLG5 and p120ctn as compiled in the Phosphosite database (V6.5.9.3). The corresponding synthetic peptides were synthesized and subjected to in situ phosphorylation. The extent of phosphorylation (32P signal) ranges from detectable (−/+) to very strong (+++), with no signal shown as ns. c Schematic of the domain structure and relative positions of the p120-catenin phosphorylation sites as indicated in the table. d Western blot showing the inhibition of p120ctn Ser320 phosphorylation by PF-3758309 U2OS cells .
Article Snippet: Primary antibodies were obtained from the following sources: rabbit PAK4 (Proteintech 14685-1-AP); mouse p120-catenin (Santa Cruz sc-23873); rabbit β-catenin (Cell Signaling #9582S); mouse β-catenin (Santa Cruz sc-7963); rabbit Afadin (Sigma A0224); mouse Afadin (R&D Systems MAB78291); rat ZO-1 (Santa Cruz sc-33725); rabbit LZTS2 (Proteintech 15677-1-AP); rabbit DLG5 (Abcam ab86783), rabbit Scribble (Santa Cruz sc-28737),
Techniques: Derivative Assay, Binding Assay, Phospho-proteomics, In Vivo, Synthesized, In Situ, Western Blot, Inhibition