• Aluminium pouches with a Microwell Plate coated with antibody to swine IFN-γ (8X12)
• 2 vials swine IFN-γ Standard lyophilized, 4000 pg/ml upon reconstitution
• 2 vials concentrated Biotin-Conjugate anti-swine IFN-γ antibody
• 2 vials Streptavidin-HRP solution,
• 1 bottle Standard /sample Diluent
• 1 bottle Biotin-Conjugate antibody Diluent
• 1 bottle Streptavidin-HRP Diluent
• 1 bottle Wash Buffer Concentrate 20x (PBS with 1% Tween-20)
• 1 vial Substrate Solution
• 1 vial Stop Solution
• 4 pieces Adhesive Films
package insert

Interferon-gamma (IFN- , also known as type II interferon) is an important immunoregulatory cytokine that was originally identified because of its anti-viral activity (1). It plays key roles in host defense by exerting antiviral, antiproliferative and immunoregulatory activities (2 - 5). On many cell types, IFN- induces the production of cytokines and upregulates the expression of various membrane proteins including class I and II MHC antigens, Fc receptors, leukocyte adhesion molecules and B7 family antigens. IFN- is a potent activator of macrophage effector functions. It potentiates the secretion of immunoglobulins by B cells, and directs the synthesis of IgG. IFN- also influences T-helper cell phenotype development by inhibiting Th2 differentiation and stimulating Th1 development (2 - 5). Finally, IFN- promotes mononuclear cell chemotaxis by inducing the synthesis of CXCL9, CXCL10, CCL2, CCL3, CCL4, and CCL5(3). IFN- is produced by a number of cell types, including dendritic epidermal/ T cells (6), keratinocytes (7), peripheral blood T cells (8), mast cells (9), neurons (10), CD8 T cells (11), macrophages (12), B cells (13), neutrophils (14), NK cells (15), CD4 T cells (16) and testicular spermatids (17). The production of IFN- is upregulated synergistically by IL-12, IL-18, IL-23 and IL-27 (18 - 21). Porcine IFN- cDNA encodes a 166 amino acid (aa) residue precursor protein with a 20 aa signal sequence that is cleaved to generate a 146 aa residue mature IFN- (22, 23). Porcine IFN- is presumably a noncovalently linked homodimer (3). In the mature segment, porcine IFN- shares 60%, 55%, 41%, 42%, 72%, and 72% aa sequence identity with human (24), guinea pig (25), mouse (26), rat (27), feline (28), and canine (29) IFN- , respectively.

The functional IFN- receptor complex consists of two distinct subunits (30). The alpha-subunit(IFN- R1) binds IFN- with high affinity and species specificity. The beta-subunit [IFN- R2, also known as accessory factor-1 (AF-1)] interacts with the IFN- occupied-subunit in a species-specific manner and participates in JAK-STAT mediated signal transduction. Although the functional receptor is suggested to consist of homodimeric IFN- in combination with two-chains, and two-chains (30, 31), it has been suggested that additional subunits may be involved (32, 33). Whereas the-chain is expressed constitutively on many cell types, the cellular regulation of the-chain correlates with an IFN- responsive state and is tightly regulated (30).

Wheelock, E.F. (1965) Science 146:310.

Billiau, A. (1996) Adv. Immunol. 62:61.

Schroder, K. et al. (2004) J. Leukoc. Biol. 75:163.

Paludan, S.R. (1998) Scand, J. Immunol. 48:459.

Boehm, U. et al. (1997) Annu. Rev. Immunol. 15:749.

Sugaya, M. et al. (1999) J. Invest. Dermatol. 113:350.

Howie, S.E.M. et al. (1996) J. Invest. Dermatol. 106:1218

Battistini, L. et al. (1997) J. Immunol. 159:3723.

Gupta, A.A. et al. (1996) J. Immunol. 157:2123.

Neumann, H. et al. (1997) J. Exp. Med. 186:2023.

Hoiden, I. and G. Moller (1996) Scand. J. Immunol. 44:501.

Puddu, P. et al. (1997) J. Immunol. 159:3490.

Yoshimoto, T. et al. (1997) Proc. Natl. Acad. Sci. USA 94:3948.

Yeaman, G.R. et al. (1998) J. Immunol. 160:5145.

Asea, A. et al. (1996) Clin. Exp. Immunol. 105:376.

Briscoe, D.M. et al. (1997) J. Immunol. 159:3247.

Dejuco, N. et al. (1995) Endocrinology 136:4925.Lebel-Binay, S. et al. (2000) Eur. Cytokine Netw. 11:15.

Trinchieri, G. (2003) Nat. Rev. Immunol. 3:133

Gracie, J.A. et al. (2003) J. Leukoc. Biol. 73:213.

Lankford, C.S.R. and D.M. Frucht (2003) J. Leukoc. Biol. 73:49.

Dijkmans, R. et al. (1990) Nucleic Acids Res. 18:4259.

Vandenbroeck, K. et al. (1991) Biochem. Biophys. Res. Commun. 180:1408.

Gray, P.W. and D.V. Goeddel (1982) Nature 298:859.

Jeevan, A. et al. (2003) Inf. Immun. 71:354.

Gray, P.W. and D.V. Goeddel (1983) Proc. Natl. Acad. Sci. USA 80:5842.

Dijkema, R. et al. (1985) EMBO J. 4:761.

Schijns, V.E. et al. (1995) Immunogenetics 42:440.

Zucker, K. et al. (1992) J. Interferon Res. 12:191.

Bach, E.A. et al. (1997) Annu. Rev. Immunol. 15:563.

Marsters, S.A. et al. (1995) Proc. Natl. Acad. Sci. USA 92:5401.

Thiel, D.J. et al. (2000) Structure 8:927.

Lembo, D. et al. (1996) J. Biol. Chem. 271:32659.