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  • 产品名称：delta-Like4(DLL4)(AA27-524)(Active)protein(FcTag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
delta-Like4(DLL4)(AA27-524)(Active)protein(FcTag)
详情介绍：
Characteristics This protein carries a human IgG1 Fc tag at the C-terminus. The protein has a calculated MW of 81 kDa. The protein migrates as 100-110 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Delta-like protein 4 (DLL4) is also known as Drosophila Delta homolog 4 (Delta4). DLL4 contains one DSL domain and eight EGF-like domains. DLL4 is expressed in vascular endothelium. DLL4 involved in angiogenesis, negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. DLL4 plays a role in the Notch signaling pathway. DLL4 activates Notch-1 and Notch-4.
Molecular Weight 81 kDa
NCBI Accession NP_061947
UniProt Q9NR61
Research Area Chromatin and Nuclear Signaling, Cell Cycle
Pathways Notch Signaling
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for delta-Like 4 (DLL4) (AA 27-524) (Active) protein (Fc Tag) (ABIN2180973) Human DLL4, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained over...
Background publications Brütsch, Liebler, Wüstehube, Bartol, Herberich, Adam, Telzerow, Augustin, Fischer: "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting angiogenesis." in: Circulation research, Vol. 107, Issue 5, pp. 592-601, 2010 (PubMed).

Zhang, Henzel: "Signal peptide prediction based on analysis of experimentally verified cleavage sites." in: Protein science : a publication of the Protein Society, Vol. 13, Issue 10, pp. 2819-24, 2004 (PubMed).