ELISA Kits

Interleukin(IL)-12 is a 70-KDa cytokine comprised of two disulfide-linked proteins(p35 and p40) and is essential for the initiation of effective immune response. And the IL-12p70 is a heterodimer of p35 and p40 subunits; it is an important cytokine secreted by antigen-presenting cells in response to antigenic stimulation. Gene expression analysis of the IL-12 cytokine family subunits revealed that both strains induced high levels of p40(protein chain communal to IL-12 p70 and IL-23) as well as p19, a subunit of IL-23. Conversely only ACT- 18HS19 infection induced consistent transcription of IL-12 p35, a subunit of IL-12 p70. The standard product used in this kit is recombinant mouse IL-12 p70 comprising of a 193 amino acids p35 chain and a 313 amino acids p40 chain connected by a disulfide bond.

Interleukin(IL)-13 is a major inducer of fibrosis in many chronic infectious and autoimmune diseases. Recombinant IL-13 protein inhibits inflammatory cytokine production induced by lipopolysaccharide in human peripheral blood monocytes. Moreover, it synergizes with IL-13 in regulating interferon-gamma synthesis in large granular lymphocytes. Interleukin-13 may be critical in regulating inflammatory and immune responses. IL-13 and IL-4 are two cytokines produced by T helper type 2 cells, mast cells, and basophils. In addition to their physiological roles, these cytokines are also implicated in pathological conditions such as asthma and allergy. The genes encoding human IL-4 and IL-13 are located on segment q23-31 of chromosome 5.4 Recombinant mouse IL-13 is a mixture of Ser26-Phe131 amino acids with the molecular mass of 11.5KDa.

Interleukin(IL)-15 is a cytokine with the ability to stimulate the proliferation activity of Th1 and/or Th2 lymphocytes. IL-15 is a novel cytokine whose effects on T-cell activation and proliferation are similar to those of interleukin-2(IL-2), presumably because IL-15 utilizes the beta and gamma chains of the IL-2 receptor. IL-15 can play a role in the initiation and outcome of acute and chronic rejection. Anti-IL-15 therapy in combination with classic immunosuppression therapy might thus be beneficial in the prevention of acute, and especially chronic, allograft rejection. The human IL15 gene is mapped to human chromosome 4q31 by fluorescence in situ hybridization.1 The standard product used in this kit is recombinant human IL-15, consisting of 114 amino acids with the molecular mass of 12.9KDa.

Interleukin 16(IL-16) is a cytokine that released by a variety of cells(including lymphocytes and some epithelial cells) that has been characterized as a chemoattractant for certain immune cells expressing the cell surface molecule CD4. By Southern blot analysis and PCR using a human/rodent somatic cell hybrid mapping panel, The human IL16 is encoded by a single-copy gene on chromosome 15. Using a combination of STS-content mapping, radiation-hybrid mapping, and genetic mapping, it was refined the assignment to 15q26.1. The mouse Il16 gene was mapped to chromosome 7 in a region showing homology of synteny to human 15q26.1. IL-16 was originally described as a factor that could attract activated T cells in humans, it was previously called lymphocyte chemoattractant factor(LCF), and the augmentation of IL16stimulation by CCR5 plays a role in regulation of Th1 cell recruitment and activation at sites of inflammation.

IL-17 is an inflammatory cytokine produced primarily by a unique lineage of CD4 T cells that plays critical roles in the pathogenesis of multiple autoimmune diseases. Interleukin-17 is expressed by activated T cells and is 57% identical to the 17- to 26-kD secretory glycoprotein encoded by gene 13 of the herpesvirus saimiri (HVS-13). IL17 induces nuclear factor kappa-B and the expression of IL6, intercellular adhesion molecule-1, granulocyte macrophage colony-stimulating factor, and prostaglandin E2, as well as the maturation of CD34 positive hematopoietic precursors into neutrophils. Anti-IL17 antibodies significantly inhibited osteoclast formation induced by culture media of RA synovial tissues. The standard product used in this kit is recombinant human IL-17, consisting of 136 amino acids with the molecular mass of 16KDa.

IL-17 is an inflammatory cytokine produced primarily by a unique lineage of CD4 T cells that plays critical roles in the pathogenesis of multiple autoimmune diseases. Interleukin-17 is expressed by activated T cells and is 57% identical to the 17- to 26-kD secretory glycoprotein encoded by gene 13 of the herpesvirus saimiri (HVS-13). IL17 induces nuclear factor kappa-B and the expression of IL6, intercellular adhesion molecule-1, granulocyte macrophage colony-stimulating factor, and prostaglandin E2, as well as the maturation of CD34 positive hematopoietic precursors into neutrophils. Anti-IL17 antibodies significantly inhibited osteoclast formation induced by culture media of RA synovial tissues. The standard product used in this kit is recombinant mouse IL-17, consisting of 137 amino acids with the molecular mass of 15.5KDa.

Laminin is a large basement membrane glycoprotein composed of three subunits designated the A, B1, and B2.1 Laminin has diverse biological functions, which include stimulating epithelial cell growth and differentiation. The nucleotide sequence of human laminin A chain has an open reading frame encoding 3075-amino acids. The human laminin A chain is at locus 18p11.3. The nucleotide sequence of the human laminin B1 reveals a 5358-base pair open reading frame that potentially codes for 1786 amino acids, including 20 amino acids of a presumptive signal peptide.2 The gene for the human laminin-B1 chain has been localized to chromosome 7, band q31. The B2 chain consists of six distinct domains, including two domains with alpha-helical, coiled-coil structures, two domains with cysteine-rich homologous repeats, and two globular domains. The amino acid sequences of the B2 and B1 chains demonstrate considerable homology. The human laminin B2 chain gene maps to the long arm of chromosome 1 in the

Laminin is a large basement membrane glycoprotein composed of three subunits designated the A, B1, and B2. Laminin has diverse biological functions, which include stimulating epithelial cell growth and differentiation. The nucleotide sequence of human laminin A chain has an open reading frame encoding 3075-amino acids. The human laminin A chain is at locus 18p11.3. The nucleotide sequence of the human laminin B1 reveals a 5358-base pair open reading frame that potentially codes for 1786 amino acids, including 20 amino acids of a presumptive signal peptide. The gene for the human laminin-B1 chain has been localized to chromosome 7, band q31. The B2 chain consists of six distinct domains, including two domains with alpha-helical, coiled-coil structures, two domains with cysteine-rich homologous repeats, and two globular domains. The amino acid sequences of the B2 and B1 chains demonstrate considerable homology. The human laminin B2 chain gene maps to the long arm of chromosome 1 in the b