ANG-2 human

ANG-2 binds to the endothelial cell specific receptor Tie2, but, in contrast to ANG-1 does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie2 and, depending on the physiological and biochemical environment, can act either as a n agonist or antagonist of Tie2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an α helix rich “coiled coil” N-terminal domain and fibrinogen like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer. Recombinant human ANG-2 is a C-terminal histidine tagged glycoprotein which migrates with an apparent molecular mass of 60.0– 70.0 kDa by SDS-PAGE under reducing conditions. Sequencing analysis shows an N-terminal sequence starting with residue 68 (D) of the ANG-2 precursor protein.

Sterile filtered through a 0.2 micron filter. Lyophilized from 10 mM Sodium Phosphate, pH 8.0.

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/mL. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.