Human sDLL-4 comprises the extracellular signaling domain of DLL, a member of a structurally-related family of single-pass type I transmembrane proteins that serve as ligands for Notch receptors. DLL-4 functions to specifically activate the Notch-1 and Notch-4 receptors. The Notch signaling pathway regulates endothelial cell differentiation, proliferation and apoptosis, and is essential for the development, maintenance and remodeling of the vascular system. Targeted deletion of the DLL-4 gene in mice resulted in severe vascular defects and death before birth. Up-regulation of DLL-4 expression has been implicated in the vascular development of certain tumors. The human DLL-4 gene consists of a 503 amino acid extracellular domain with one DSL domain, eight EGF-like repeats, a 21 amino acid transmembrane domain, and a 135 amino acid cytoplasmic domain. Recombinant Human sDLL-4 is a 54.3 kDa glycoprotein containing 498 amino acid residues.
soluble DLL-4, Delta-like protein 4, Drosophila Delta homolog 4
SGVFQLQLQE FINERGVLAS GRPCEPGCRT FFRVCLKHFQ AVVSPGPCTF GTVSTPVLGT NSFAVRDDSS GGGRNPLQLP FNFTWPGTFS LIIEAWHAPG DDLRPEALPP DALISKIAIQ GSLAVGQNWL LDEQTSTLTR LRYSYRVICS DNYYGDNCSR LCKKRNDHFG HYVCQPDGNL SCLPGWTGEY CQQPICLSGC HEQNGYCSKP AECLCRPGWQ GRLCNECIPH NGCRHGTCST PWQCTCDEGW GGLFCDQDLN YCTHHSPCKN GATCSNSGQR SYTCTCRPGY TGVDCELELS ECDSNPCRNG GSCKDQEDGY HCLCPPGYYG LHCEHSTLSC ADSPCFNGGS CRERNQGANY ACECPPNFTG SNCEKKVDRC TSNPCANGGQ CLNRGPSRMC RCRPGFTGTY CELHVSDCAR NPCAHGGTCH DLENGLMCTC PAGFSGRRCE VRTSIDACAS SPCFNRATCY TDLSTDTFVC NCPYGFVGSR CEFPVGLP
≥ 95% by SDS-PAGE gel and HPLC analyses.
The sDLL-4, when immobilized at concentrations >1.5 μg/mL, will inhibit myogenesis in C2C12 cells.
Calculated Molecular Weight:
Not for human use.