1. Capture Antibody 0.4 mg/mL of mouse anti-DLL1 monoclonal antibody. Dilute to a working concentration of 2.0 μg/mL in CBS before coating. (Catalog: # 11635-MM05) 2. Detection Antibody 0.5 mg/mL mouse anti-DLL1 monoclonal antibody conjugated to horseradish-peroxidase (HRP). Dilute to working concentration of 0.5 μg/mL in detection antibody dilution buffer before use. (Catalog: # 11635-MM07) 3. Standard Each vial contains 100 ng of recombinant DLL1. Reconstitute standard powder with 1 mL detection antibody dilution buffer. After reconstitution, store at -20℃ to -80℃ in a manual defrost freezer. A seven-point standard curve using 2-fold serial dilutions in sample dilution buffer, and a high standard of 3000 pg/mL is recommended.
This DLL1 Matched ELISA Antibody Pair Set,Human is a solid phase sandwich ELISA for quantitative determination of Human DLL1 . It contains Human DLL1 capture antibody, Human DLL1 detector antibody
and a highly purified
recombinant Human DLL1 protein. This Pair Set is at affordable price for researchers.
This Matched ELISA Antibody Pair Set is shipped at ambient temperature.
Capture Antibody: Aliquot and store at -20℃ to -80℃ for up to 6 months from date of receipt. Avoid repeated freeze-thaw cycles. Detection Antibody: Protect it from prolonged exposure to light. Aliquot and store at -20℃ to -80℃ and for up to 6 months from date of receipt. Avoid repeated freeze-thaw cycles. Standard: Store lyophilized standard at -20℃ to -80℃ for up to 6 months from date of receipt. Aliquot and store the reconstituted Standard at -80℃ for up to 1 month. Avoid repeated freeze-thaw cycles.
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.