Human/Mouse/Rat DEP-1/CD148 Antibody Summary
Arg997-Ala1337
Accession # Q12913
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Human DEP‑1/CD148 by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat DEP-1/CD148 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1934) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for DEP-1/CD148 at approximately 220 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Monkey DEP-1/CD148 by Immunocytochemistry/Immunofluorescence Proximity ligation assay reveals association of DEP-1 with its substrate FLT3.(A) COS7 cells were transiently transfected with expression constructs for FLT3, DEP-1, the catalytically inactive DEP-1 C1239S trapping mutant, or corresponding control plasmids as indicated. Complex formation was measured by in situ PLA using rabbit anti-FLT3 antibodies, goat anti-DEP-1 antibodies, and corresponding secondary reagents. In situ PLA is indicated by red signals of the rolling cycle amplification products (RCPs). FLT3 expression (green) was visualized by additional staining with FITC-labeled anti-rabbit IgG antibodies; nuclei (blue) were counterstained with Hoechst 33342. Scale bars 20 µm. (B), (C) Complex formation of endogenous DEP-1 with endogenous FLT3 in THP-1 cells. Cells were transfected with DEP-1-specific or control siRNA by Nucleofection, were then starved and either left unstimulated or were stimulated with FL (100 ng/ml) for 10 min as indicated. (B) Example images; DEP-1 knockdown efficiency was detected by immunblotting (lower panel). DEP-1-FLT3 complexes as RCPs are shown in red, nuclei are depicted in blue and scale bars represent 20 µm for the overview images and 5 µm for the insets. (C) Quantification of detected in situ PLA signals over 5 images per variant. The data are representative for 3 experiments with consistent results. Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/23650535), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: DEP-1/CD148
Density Enhanced Protein Tyrosine Phosphatase (DEP-1), also known as CD148, HPTP-eta, and PTP receptor type J (PTPRJ), is an enzyme that removes phosphate groups covalently attached to tyrosine residues in proteins. A large (220 kilodalton) glycoprotein found at the cell surface, DEP-1 levels are increased with high cell density (1). DEP-1 phosphatase activity is enhanced by basement membrane proteins (2), suggesting it is involved in regulating cell adhesion and contact interactions. High levels of expression dampen PDGF (3), VEGF (4), and T-cell receptor (5) responses. DEP-1 is widely expressed in tissues, particularly ones forming epithelioid monolayers (6). In the immune system, DEP-1 is found on all cell lineages and is highest on granulocytes (7). Dep-1 is the mutated gene in the Susceptibility to Colon Cancer locus Scc1, which is altered in many human colorectal adenomas (8). Gene knockout mice lacking DEP-1 die at midgestation due to failures in cardiovascular development (9). DEP-1 dephosphorylates a variety of proteins, including the HGF (10), PDGF (11), and VEGF (4) receptors, and beta ‑catenin (12). The recombinant protein is the intracellular region of DEP-1 containing the catalytic domain. Over aa 997-337, human Dep-1 shares 95% aa sequence identity with mouse and rat Dep-1.
- Ostman, A. et al. (1994) Proc. Natl. Acad. Sci. USA 91:9680.
- Sorby, M. et al. (2001) Oncogene 20:5219.
- Jandt, E. et al. (2003) Oncogene 22:4175.
- Lampugnani, M.G. et al. (2003) J. Cell Biol. 161:793.
- Baker, J.E. et al. (2001) Mol. Cell. Biol. 21:2393.
- Borges, L.G. et al. (1996) Circ. Res. 79:570.
- de la Fuente-Garcia, M.A. et al. (1998) Blood 91:2800.
- Ruivenkamp, C.A. et al. (2002) Nat. Genet. 31:295.
- Takahashi, T. et al. (2003) Mol. Cell. Biol. 23:1817.
- Palka, H.L. et al. (2003) J. Biol. Chem. 278:5728.
- Kovalenko, M. et al. (2000) J. Biol. Chem. 275:16219.
- Holsinger, L.J. et al. (2002) Oncogene 21:7067.
Product Datasheets
Citations for Human/Mouse/Rat DEP-1/CD148 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 9
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The effects of CD148 Q276P/R326Q polymorphisms in A431D epidermoid cancer cell proliferation and epidermal growth factor receptor signaling
Authors: Lilly He, Keiko Takahashi, Lejla Pasic, Chikage Narui, Philipp Ellinger, Manuel Grundmann et al.
Cancer Rep (Hoboken)
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Association of the Protein-Tyrosine Phosphatase DEP-1 with Its Substrate FLT3 Visualized by In Situ Proximity Ligation Assay
Authors: Sylvia-Annette Böhmer, Irene Weibrecht, Ola Söderberg, Frank-D. Böhmer
PLoS ONE
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Enhanced insulin signaling in density-enhanced phosphatase-1 (DEP-1) knockout mice
Authors: Janine Krüger, Sebastian Brachs, Manuela Trappiel, Ulrich Kintscher, Heike Meyborg, Ernst Wellnhofer et al.
Molecular Metabolism
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PTPRJ Inhibits Leptin Signaling, and Induction of PTPRJ in the Hypothalamus Is a Cause of the Development of Leptin Resistance
Authors: T Shintani, S Higashi, R Suzuki, Y Takeuchi, R Ikaga, T Yamazaki, K Kobayashi, M Noda
Sci Rep, 2017-09-14;7(1):11627.
Species: Human, Mouse
Sample Types: Cell Lysates, Whole Cells
Applications: ICC, Western Blot -
Phosphorylation of DEP-1/PTPRJ on threonine 1318 regulates Src activation and endothelial cell permeability induced by vascular endothelial growth factor.
Authors: Spring K, Lapointe L, Caron C, Langlois S, Royal I
Cell Signal, 2014-02-28;26(6):1283-93.
Species: Human
Sample Types: Recombinant Protein
Applications: Immunoprecipitation -
T cell Ig and mucin domain-containing protein 3 is recruited to the immune synapse, disrupts stable synapse formation, and associates with receptor phosphatases.
Authors: Clayton K, Haaland M, Douglas-Vail M, Mujib S, Chew G, Ndhlovu L, Ostrowski M
J Immunol, 2013-12-13;192(2):782-91.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling.
Authors: Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K, Razumovskaya E, Ronnstrand L, Tanzer S, Bauer R, Bohmer FD, Muller JP
J. Biol. Chem., 2011-01-24;286(13):10918-29.
Species: Human
Sample Types: Whole Cells
Applications: Flow Cytometry -
Targeting density-enhanced phosphatase-1 (DEP-1) with antisense oligonucleotides improves the metabolic phenotype in high-fat diet-fed mice
Authors: Janine Krüger, Manuela Trappiel, Markus Dagnell, Philipp Stawowy, Heike Meyborg, Christian Böhm et al.
Cell Communication and Signaling
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Disrupting PTPRJ transmembrane-mediated oligomerization counteracts oncogenic receptor tyrosine kinase FLT3 ITD
Authors: Marie Schwarz, Sophie Rizzo, Walter Espinoza Paz, Anne Kresinsky, Damien Thévenin, Jörg P. Müller
Frontiers in Oncology
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