Human/Mouse/Rat DEP-1/CD148 Antibody

Catalog # Availability Size / Price Qty
AF1934
AF1934-SP
Detection of Human DEP‑1/CD148 by Western Blot.
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Product Details
Citations (9)
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Human/Mouse/Rat DEP-1/CD148 Antibody Summary

Species Reactivity
Human, Mouse, Rat
Specificity
Detects human, mouse, and rat DEP-1/CD148 in Western blots.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
E. coli-derived recombinant human DEP‑1/CD148
Arg997-Ala1337
Accession # Q12913
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
1 µg/mL
See below
Immunoprecipitation
2.5 µg/500 µg cell lysate
HeLa human cervical epithelial carcinoma cell line, see our available Western blot detection antibodies

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

Western Blot Detection of Human DEP‑1/CD148 antibody by Western Blot. View Larger

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.

Immunocytochemistry/ Immunofluorescence Detection of Monkey DEP-1/CD148 by Immunocytochemistry/Immunofluorescence View Larger

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

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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.

References
  1. Ostman, A. et al. (1994) Proc. Natl. Acad. Sci. USA 91:9680.
  2. Sorby, M. et al. (2001) Oncogene 20:5219.
  3. Jandt, E. et al. (2003) Oncogene 22:4175.
  4. Lampugnani, M.G. et al. (2003) J. Cell Biol. 161:793.
  5. Baker, J.E. et al. (2001) Mol. Cell. Biol. 21:2393.
  6. Borges, L.G. et al. (1996) Circ. Res. 79:570.
  7. de la Fuente-Garcia, M.A. et al. (1998) Blood 91:2800.
  8. Ruivenkamp, C.A. et al. (2002) Nat. Genet. 31:295.
  9. Takahashi, T. et al. (2003) Mol. Cell. Biol. 23:1817.
  10. Palka, H.L. et al. (2003) J. Biol. Chem. 278:5728.
  11. Kovalenko, M. et al. (2000) J. Biol. Chem. 275:16219.
  12. Holsinger, L.J. et al. (2002) Oncogene 21:7067.
 
Long Name
Density Enhanced Receptor Protein Tyrosine Phosphatase
Entrez Gene IDs
5795 (Human); 19271 (Mouse); 29645 (Rat)
Alternate Names
CD148 antigen; CD148; Density-enhanced phosphatase 1; DEP1; DEP-1; DEP1EC 3.1.3.48; HPTP eta; HPTPeta; HPTP-eta; human density enhanced phosphatase-1; protein tyrosine phosphatase, receptor type, J polypeptide; protein tyrosine phosphatase, receptor type, J; Protein-tyrosine phosphatase eta; Protein-tyrosine phosphatase receptor type J; PTPRJ; receptor-type tyrosine-protein phosphatase eta; R-PTP-ETA; R-PTP-J; SCC1; susceptibility to colon cancer 1, mouse, homolog of

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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.

9 Citations: Showing 1 - 9
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  1. 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)
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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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