Recombinant Human ANG-2
Catalog Number : 130-07
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.
Above 95% as determined by SDS-PAGE Analysis.
Determined by its ability to stimulate tubulogenesis in HUVEC cells using a concentration of 0.2μg/ml
DAPLEYDDS VQRLQVLEN IMENNTQWL MKLENYIQD NMKKEMVEI QQNAVQNQT AVMIEIGTN LLNQTAEQT RKLTDVEAQ VLNQTTRLE LQLLEHSLS TNKLEKQIL DQTSEINKL QDKNSFLEK KVLAMEDKH IIQLQSIKE EKDQLQVLV SKQNSIIEE LEKKIVTAT VNNSVLQKQ QHDLMETVN NLLTMMSTS NSAKDPTVA KEEQISFRD CAEVFKSGH TTNGIYTLT FPNSTEEIK AYCDMEAGG GGWTIIQRR EDGSVDFQR TWKEYKVGF GNPSGEYWL GNEFVSQLT NQQRYVLKI HLKDWEGNE AYSLYEHFY LSSEELNYR IHLKGLTGT AGKISSISQ PGNDFSTKD GDNDKCICK CSQMLTGGW WFDACGPSN LNGMYYPQR QNTNKFNGI KWYYWKGSG YSLKATTMM IRPADFHHH HHH
|Research Interest:||Apoptosis, Angiogenesis, Bone Biology|
|Cell Type:||Endothelial Cells|
|Protein Cross Reactivity:||NULL|