Receptor tyrosine kinases play key roles in signal transduction across cell surfaces in biological systems, including the vascular system. These receptors comprise a large and diverse family of catalytically related proteins that, on the basis of sequence and structural similarities, can be divided into several different evolutionary subfamilies. The cloning and characterization of Tie-1 (also designated Tie), a novel human endothelial cell surface receptor tyrosine kinase, has been reported. The extracellular domain of the predicted Tie-1 protein product has an unusual multidomain structure consisting of a cluster of three epidermal growth factor homology motifs localized between two immunoglobulin-like loops, which are followed by three fibronectin type III repeats next to the transmembrane region. An additional member of this family has been identified as Tie-2 (also designated Tek). Tie-1 and Tie-2 have been shown to be encoded by distinct genes and to represent members of a new class of receptor tyrosine kinases.

Angiopoietin-1 receptor; Endothelial tyrosine kinase; Tunica interna endothelial cell kinase; Tyrosine kinase with Ig and EGF homology domains-2; Tyrosine-protein kinase receptor TEK; Tyrosine-protein kinase receptor TIE-2; hTIE2; p140 TEK; CD202b; TEK; TIE2; VMCM; VMCM1

q02763

Human,Mouse,Rat

WB

WB 1:500-1:2000

~ 160 kDa

Rabbit

This antibody detects endogenous levels of Tie-2 protein when phosphorylated at Tyr1108.

Synthetic phosphopeptide derived from human Tie-2 around the phosphorylation site of Tyrosine 1108.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.