Recombinant human DLL4 Protein

Cat # Size Price Quantity
63190150 μg$300
631902500 μg$1250

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameDLL-4, Delta-like protein 4, Dll4, hdelta2
SpeciesHuman
accession numberNP_061947.1
SourcesA DNA sequence encoding the extracellular domain (Met1-Pro524) of human DLL4 (NP_061947.1) was expressed with the Fc region of human IgG1 at the C-terminus.
Molecular WeightThe recombinant human DLL4/Fc is a disulfide-linked homodimeric protein after removal of the signal peptide. The reduced monomer consists of 736 amino acids and predicts a molecular mass of 81 kDa. As a result of glycosylation, the rh DLL4/Fc monomer migrates as approximately 100-110 kDa band in SDS-PAGE under reducing conditions.
Affinity TagC-Fc
Purity≥ 95 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC. ≥ 90 % as determined by SEC-MALS(Routinely tested)
Regulatory StatusRUO
Endotoxin level< 1.0 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information


Human Delta-like ligand 4 (DLL4) is a membrane-bound protein encoded by the DLL4 gene and is a critical component of the Notch signaling pathway, which regulates cell fate determination, differentiation, proliferation, and survival. DLL4 is expressed predominantly in vascular endothelial cells and plays an essential role in embryonic vascular development, angiogenesis, and maintenance of the arterial vasculature. By activating Notch receptors on adjacent cells, particularly Notch1 and Notch4, DLL4 helps coordinate endothelial cell behavior, limiting excessive blood vessel sprouting while promoting the formation of functional vascular networks.

Structurally, DLL4 is a type I transmembrane glycoprotein consisting of an extracellular domain containing a Delta/Serrate/LAG-2 (DSL) domain required for receptor binding, multiple epidermal growth factor (EGF)-like repeats that contribute to receptor specificity, a single transmembrane region, and a short intracellular cytoplasmic tail. Its principal ligands are the Notch family receptors (Notch1–4), with strongest functional interactions occurring with Notch1 and Notch4 in vascular tissues.

Aberrant DLL4 signaling has been implicated in several diseases. Overexpression is associated with tumor angiogenesis in many solid cancers, where it promotes maturation of tumor blood vessels and can contribute to resistance against anti-vascular endothelial growth factor (VEGF) therapies. Conversely, impaired DLL4 function can disrupt vascular development and has been linked to congenital cardiovascular abnormalities.

Because of its central role in regulating angiogenesis, DLL4 has emerged as an attractive therapeutic target. Monoclonal antibodies, bispecific antibodies targeting DLL4 and VEGF, and other inhibitors have been investigated as anticancer agents to induce nonproductive tumor angiogenesis and suppress tumor growth. However, systemic inhibition of DLL4 may produce vascular and hepatic toxicities, highlighting the need for carefully controlled therapeutic strategies. DLL4-targeted approaches therefore remain an active area of oncology research, with the goal of improving efficacy while minimizing adverse effects.

Data Sheets


Recombinant human DLL4 Protein TDS

Frequently Asked Questions


What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.

What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.

How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.

Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.

Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

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