|Calculated MW||60-70 kDa|
|Sequence||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|
|Application Notes||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.|
|Storage||-20°C; Sterile filtered through a 0.2 micron filter. Lyophilized from 10 mM Sodium Phosphate, pH 8.0.|
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Provided below are standard protocols that you may find useful for product applications.
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 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.
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