ALEXIS Biochemicals: DLL1 (human):Fc (human) (recombinant)

ALX-201-425

Revised 24-Sep-08

DLL1 (human):Fc (human) (recombinant)
SYNONYMS	Delta-like Protein 1 (human):Fc (human) (recombinant) Delta1 (human):Fc (human) (recombinant)
PRODUCT LINE	Signal Transduction
PRODUCT CATEGORY	Delta-like [DLL] & Jagged / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-201-425-C010		10 µg	230.00 USD
ALX-201-425-C050		50 µg	690.00 USD

Product Specification

SOURCE/HOST:	Produced in HEK 293 cells. Signal peptide and extracellular domain of recombinant human DLL1 (Delta-like protein 1; Delta1) (aa 1-545) is fused at the C-terminus to the Fc portion of human IgG.
CONCENTRATION:	0.3mg/ml
PURITY:	≥90% (SDS-PAGE)
FORMULATION:	Liquid. 0.2µm-filtered solution in PBS.
ENDOTOXIN CONTENT:	<0.1EU/µg protein (LAL-test).
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C
USE/STABILITY:	Working aliquots are stable for up to 3 months when stored at -20°C.
HANDLING:	After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.

Product Images

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General Information

Notch signalling pathways play key roles in cell-fate determination and differentiation in many tissues during embryonic and postnatal development. Notch ligands are divided into two subclasses, the delta and the serrate family [1]. Delta-like 1, 3, and 4 (DLL1, -3, -4), JAG1 and JAG2 with DSL (Delta, Serrate, Lag2) domain are typical Notch ligands, while DNER, F3/Contactin and NB-3 without DSL domain are atypical Notch ligands. Notch-ligand binding to NOTCH1, -2, -3, or -4 receptor induces the receptor proteolysis by metalloprotease and γ-secretase to release Notch intracellular domain (NICD). DLL1 [1] is the human homolog of the Drosophila Notch ligand Delta [2]. Sequence analysis predicted that the 723-aa DLL1 transmembrane protein, which is 88% identical to the mouse DLL1 protein [3], has a DSL domain followed by 8 tandem EGF-like repeats and a short cytoplasmic C-terminal region. A soluble fusion protein containing the DSL domain of DLL1 and its adjacent 50 N-terminal aa inhibited the differentiation of myeloid progenitors but promoted their expansion [4]. DLL1 blocks the differentiation of progenitor cells into the B cell lineage while promoting the emergence of a population of cells with the characteristics of a T cell/NK cell precursor [5]. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10 and represents a substrate for several other members of the ADAM family [6, 7]. The soluble 38kDa Delta1 intracellular domain (DICD) that is generated by the presenilin-dependent γ-secretase cleavage is transported into the nucleus and likely plays a role in transcriptional events [8-10]. Recently it has been shown that DLL1 is essential for postnatal arteriogenesis [11].
BACKGROUND/TECHNICAL INFORMATION	Swiss-Prot link O00548: DLL1 (human) [Precursor]
MANUFACTURER	Manufactured by AdipoGen, Inc.

General Literature References

[1] Human ligands of the Notch receptor: G.E. Gray, et al.; Am. J. Pathol. 154, 785 (1999) Abstract; Full Text
[2] The molecular genetics of early neurogenesis in Drosophila melanogaster: E. Knust and J.A. Campos-Ortega; Bioessays 11, 95 (1989) Abstract
[3] Transient and restricted expression during mouse embryogenesis of Dll1, a murine gene closely related to Drosophila Delta: B. Bettenhausen, et al.; Development 121, 2407 (1995) Abstract; Full Text
[4] A soluble form of human Delta-like-1 inhibits differentiation of hematopoietic progenitor cells: W. Han, et al.; Blood 95, 1616 (2000) Abstract; Full Text
[5] Differential effects of Notch ligands Delta-1 and Jagged-1 in human lymphoid differentiation: A.C. Jaleco, et al.; J. Exp. Med. 194, 991 (2001) Abstract; Full Text
[6] The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase: E. Six, et al.; PNAS 100, 7638 (2003) Abstract; Full Text
[7] Proteolytic processing of delta-like 1 by ADAM proteases: E. Dyczynska, et al.; J. Biol. Chem. 282, 436 (2007) Abstract; Full Text
[8] Notch-induced proteolysis and nuclear localization of the Delta ligand: C.E. Bland, et al.; J. Biol. Chem. 278, 13607 (2003) Abstract; Full Text
[9] The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "gamma-secretase" cleavage: T. Ikeuchi and S.S. Sisodia; J. Biol. Chem. 278, 7751 (2003) Abstract; Full Text
[10] The Notch ligands, Jagged and Delta, are sequentially processed by alpha-secretase and presenilin/gamma-secretase and release signaling fragments: M.J. LaVoie and D.J. Selkoe; J. Biol. Chem. 278, 34427 (2003) Abstract; Full Text
[11] The Notch Ligand Delta-Like 1 is Essential for Postnatal Arteriogenesis: A. Limbourg, et al.; Circ. Res. 100, 363 (2007) Abstract
[12] NOTCH signaling as a novel cancer therapeutic target: L. Miele, et al.; Curr. Cancer Drug Targets 6, 313 (2006) Abstract
[13] Notch signaling in gastrointestinal tract: M. Katoh; Int. J. Oncol. 30, 247 (2007), Review Abstract

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