Detection of DLL1 in Mouse Splenocytes by Flow Cytometry.
Mouse splenocytes were stained with Sheep Anti-Mouse/Rat DLL1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3970, filled histogram) or control antibody (Catalog # 5-001-A, open histogram), followed by NorthernLights™ 637-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # NL011).
DLL1 in Embryonic Mouse Stomach.
DLL1 was detected in immersion fixed frozen sections of embryonic mouse stomach (E13.5) using 10 µg/mL Sheep Anti-Mouse/Rat DLL1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3970) overnight at 4 °C. Tissue was stained with the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
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.
Delta-like protein 1 (DLL1) is a 90-100 kDa type I transmembrane protein in the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. Mature rat DLL1 consists of a 520 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 154 aa cytoplasmic domain (1). Within the ECD, rat DLL1 shares 90% and 95% aa sequence identity with human and mouse DLL1, respectively. It shares 26%, 36%, and 53% aa sequence identity with rat DLL2, 3, and 4, respectively. The ADAM9, 12, or 17- mediated proteolysis of DLL1 releases a 60 kDa ECD fragment and regulates the Notch-dependent proliferation of hematopoietic and myogenic progenitor cells (2-4). The residual membrane-bound portion of DLL1 can be cleaved by presenilin-dependent gamma -secretase, enabling the cytoplasmic domain to migrate to the nucleus (5). DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1 (6). DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, lymphocyte differentiation, and the maintenance of neural and myogenic progenitor cells (4, 7-13). The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis (14). DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression (15-16).
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