Galectins are a new family of animal lectins which appear to exhibit a variety of biological functions and may in fact be a broad-spectrum biological response modifier. Galectin 3 is one of the more extensively studied member of this family and is a 30kD protein known by various other names including eBP (IgE binding protein), Mac-2, CBP-30 and L-29. Due to a C-terminal carbohydrate binding site, Galectin 3 is capable of binding IgE and mammalian cell surfaces only when homodimerized or homooligomerized. This antibody has been shown to potentiate the binding of Galectin 3 to IgG. Among its numerous proposed functions, Galectin 3 may be a component of a cell-growth regulating system given its elevated expression and nuclear localization in proliferating cells. It has also been found to be a major non-integrin laminin-binding protein suggesting a role in cell adhesion. One of its more interesting proposed functions is as an inhibitor of apoptosis. Galectin 3 shares an NWGR motif with Bcl-2 which has been shown to be an important region in Bcl-2 for suppression of apoptosis. Galectin 3 has been shown to interact with Bcl-2 which may account for the ability of Galectin 3 to suppress programmed cell death in anti-Fas (an apoptosis inducer) treated Jurkat cells transfected with Galectin 3. In contrast to Galectin 3, Galectin 1 actually induces apoptosis when added to cultures of activated human T cells.