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A DNA sequence encoding the human Lymphotoxin alpha (LT-a) protein sequence (containing the signal peptide sequence, and the mature human Lymphotoxin alpha sequence) was expressed in modified human 293 cells.

Lymphotoxin-alpha (LT-a?) is a pro-inflammatory cytokine expressed in activated T cells, B cells, natural killer cells, as well as some non-hematopoietic cells. Activation signals include bacterial products, virus infection, T cell receptor activation, crosslinking of surface immunoglobulin (Ig) on B-lymphocytes, and exposure to UV light in epithelial cells. LT-a regulates a variety of biological processes including cell proliferation, apoptosis, coagulation and lipid metabolism. LT-a has been shown to be cytotoxic to a broad range of tumor cells both in vitro and in vivo. LT-a plays an important role in inflammation and protective immunity by regulating cytokine release, recruitment of effector cells to infection sites and promoting adhesion of leukocytes to endothelial cells. Human LT-a is a member of the TNF superfamily. Two forms of LT-a have been identified, a soluble trimeric complex and a heterocomplex membrane bound form that involves the association of LT-a and a related protein called lymphotoxin-beta (LT-b) The LT-a/b complex can associate as two isomers differing in the ratio of subunits present, either Lta-2/b or more commonly as LT-a/b2. LT-a is synthesized as a 205 amino acid peptide including a 34 amino acid signal sequence. LT-a has one potential N-linked glycosylation site. For further information on the role of Lymphotoxin-alpha in immunity and autoimmunity please refer to McDevitt H., et al. (2002) Arthritis Res.; 4 Suppl 3:S141-52.