Anti-Annexin A4 antibody is directed against annexin IV. It is a member of the annexin family of calcium/phospholipid-binding proteins and promotes membrane fusion during exocytotic processes. It also has in vitro anticoagulant activity and inhibits phospholipase A2 activity. Its function has been implicated in the progression, invasion, migration, adhesion and drug resistance of a variety of cancer cells.
The 2F11 molecule was used to immuno-precipitate possible antigens from the lysate of zebrafish embryos at 72 hpf, at a time when 2F11 foregut labeling is robust. The precipitated proteins were separated by PAGE electrophoresis under reducing conditions, and a clear band resolving between 28 and 39 kDa was identified. This band was in-gel digested to yield small peptides, which were then subjected to tandem mass spectrometry. The peptide sequences obtained accurately matched several regions of the zebrafish Annexin A4 protein (Anxa4).
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Plasma levels of annexin A5 were measured in 175 patients with systemic lupus erythematosus, 104 of whom had antiphospholipid antibodies and 23 of whom had primary antiphospholipid syndrome. Plasma levels of annexin A5 also were measured in a large number of citrated, heparinized and unheparinized plasma and serum samples from healthy individuals.
The annexin A5 levels were significantly elevated in the groups of patients with SLE and PAPS, but not in the group of controls without SLE or PAPS. This suggests that annexin A5 is not removed from cellular surfaces in vivo by antiphospholipid antibodies, and indicates that plasma levels of this protein are regulated by other mechanisms.