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Lipocalin 2 is a member of the lipocalin family which encompass more than 25 members (including proteins like retinol binding protein, a1 microglobulin, b lactoglobulin, apolipoprotein D and odorant binding protein). The members of the lipocalin family are characterized by their ability to bind small lipophilic substances in their hydrophobic core, and thereby serve as transporters of substances.

This gene encodes a lymphokine involved in cell-mediated immunity, immunoregulation, and inflammation. It plays a role in the regulation of macrophage function in host defense through the suppression of anti-inflammatory effects of glucocorticoids. This lymphokine and the JAB1 protein form a complex in the cytosol near the peripheral plasma membrane, which may indicate an additional role in integrin signaling pathways. [provided by RefSeq, Jul 2008]

This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 ａ

This gene encodes a cell surface membrane protein of the immunoglobulin superfamily. This protein is expressed in pro-B-cells and is thought to play a role in their differentiation. In mice, expression of this gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for this gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that this gene

Interferon-Beta, IFN-Beta mainly by the fibroblast cell factor, belonging to a single gene encodes a protein that can interfere with the virus RNA or DNA replication and inhibit virus growth, and significantly enhance NK cell activity, through the promotion of MHC Ⅰ molecule expression and enhance the CTL of the virus-infected cells role in the identification and destruction.$n

The complement component proteins: C2, C3, C4 and C5 are potent anaphyl-atoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Activation of the complement system leads to the formation of C5b-9 terminal complex, ａn