Anti-DLL1 / Delta-like 1 antibody

Cat.#: 102771

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Product Information

  • Product Name
    Anti-DLL1 / Delta-like 1 antibody
  • Documents
  • Description
    Rabbit polyclonal to DLL1 / Delta-like 1
  • Tested applications
    ELISA, WB
  • Species reactivity
    Human DLL1 / Delta-1
  • Alternative names
    Delta antibody; DELTA1 antibody; Delta1 antibody; DL1 antibody; DLL1 antibody; Dll1 antibody; H-Delta-1 antibody; Delta1 antibody; Delta1 antibody; DL1 antibody; Delta antibody
  • Immunogen
  • Isotype
    Rabbit IgG
  • Preparation
    Produced in rabbits immunized with purified, recombinant Human DLL1 / Delta-1 (rh DLL1; NP_005609.3; Met 1-Gly 540). Total IgG was purified by Protein A affinity chromatography
  • Clonality
    Polyclonal
  • Formulation
    0.2 μm filtered solution in PBS with 5% trehalose
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    WB: 10-20 μg/ml

    ELISA: 0.5-1 μg/mL

    This antibody can be used at 0.5-1 μg/mL with the appropriate secondary reagents to detect Human DLL1. The detection limit for Human DLL1 is approximately 0.00975 ng/well.

  • Validations

    DLL1 / Delta-1 Antibody, Rabbit PAb, Western blot

    DLL1 / Delta-1 Antibody, Rabbit PAb, Western blot

  • Background
    Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains,  acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
  • References
    • Dyczynska E, et al. (2007) Proteolytic processing of delta-like 1 by ADAM proteases. J Biol Chem. 282(1): 436-44.
    • Sun D, et al. (2008) The role of Delta-like 1 shedding in muscle cell self-renewal and differentiation. J Cell Sci. 121(Pt 22): 3815-23.
    • Srensen I, et al. (2009) DLL1-mediated Notch activation regulates endothelial identity in mouse fetal arteries. Blood. 113(22): 5680-8.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"