CD162 glycoprotein functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. (Shipping Cost: €200.00)

IL-12 [JJ07]

Interleukin-12 The interleukins (ILs) are a broad family of well characterized cytokines, primarily of hematopoietic cell origin. As new cytokines are molecularly characterized, they are assigned an IL number to maintain a standard nomenclature. ILs are secreted by immune cells (mainly macrophages, B cells or T cells) that regulate a wide range of immune system functions. The functions of different ILs vary from regulating inflammatory and immune responses, functioning as autocrine factor and regulating and/or inhibiting other ILs. IL-12 is secreted by macrophages and human B-lymphoblastoid cells in response to antigenic stimulation. It is responsible for the differentiation of naive CD4+ T cells into type 1 helper T cells that produce interferon-γ (IFN-γ). It also activates production of tumor necrosis factor α (TNFα) from T and natural killer (NK) cells, and it inhibits IL-4 mediated suppression of IFN-γ. IL-12 also has antiangiogenic activity, since the production of IFN-γ increases the production of inducible protein-10 (IP-10).

IL-12 [JJ07]