Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
Angiopoietin 2 and angiopoietin 1 have an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain. The coiled coil domains mediate ligand homo-oligomerization and the fibrinogen-like domains mediate ligand activity. Recombinant human angiopoietin 2 has a molecular mass of approximately 66 kDa in SDS-PAGE under reducing and non-reducing conditions. Angiopoietin 2 probably acts as a natural antagonist for Ang1 and Tie2 both in vivo and in vitro. In adult mice and humans, angiopoietin 2 is expressed at sites of vascular remodeling.
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Protein Aliases: ANG-2; Angiopoietin-2; angiopoietin-2a; angiopoietin-2B; Tie2-ligand
Gene Aliases: AGPT2; Ang-2; ANG2; ANGPT2
Molecular Function: signaling molecule