ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, 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 alpha-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. The calculated molecular weight of Recombinant Human ANG-2 is 50.1 kDa.
DAPLEYDDSV QRLQVLENIM ENNTQWLMKL ENYIQDNMKK EMVEIQQNAV QNQTAVMIEI GTNLLNQTAE QTRKLTDVEA QVLNQTTRLE LQLLEHSLST NKLEKQILDQ TSEINKLQDK NSFLEKKVLA MEDKHIIQLQ SIKEEKDQLQ VLVSKQNSII EELEKKIVTA TVNNSVLQKQ QHDLMETVNN LLTMMSTSNS AKDPTVAKEE QISFRDCAEV FKSGHTTNGI YTLTFPNSTE EIKAYCDMEA GGGGWTIIQR REDGSVDFQR TWKEYKVGFG NPSGEYWLGN EFVSQLTNQQ RYVLKIHLKD WEGNEAYSLY EHFYLSSEEL NYRIHLKGLT GTAGKISSIS QPGNDFSTKD GDNDKCICKC SQMLTGGWWF DACGPSNLNG MYYPQRQNTN KFNGIKWYYW KGSGYSLKAT TMMIRPADFH HHHHH
Greater than 95% by SDS-PAGE gel and HPLC analyses.
Determined by its ability to stimulate tubulogenesis in HUVEC cells using a concentration of 0.2μg/ml
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