Other Proteins

Interferon-alpha 2b (IFNα 2b) is a Type I interferon made by leukocytes during viral infection. It has anti-viral and non-proliferative activity induced by JAK1-STAT signaling. IFN-alphas are the most widely used type for therapeutic purposes. IFNα 2b is a variant of IFNα 2a that differs by one amino acid. Recombinant human IFNα 2b is a non-glycosylated protein, containing 166 amino acids, with a molecular weight of 19.4 kDa.

Interferon gamma, IFNγ, is a major immune-modulating molecule produced mainly by T cells and natural killer cells activated by antigens, mitogens or alloantigens. Most immune cells express IFN-γ receptors and respond to IFNγ-induced signaling by up-regulating MHC class I expression. Human IFNγ does not show cross-reactivity with mouse. Recombinant human IFNγ is a non-glycosylated protein, containing 144 amino acids, with a molecular weight of 16.88 kDa.

Interferon gamma, IFNγ, is a major immune-modulating molecule produced mainly by T cells and natural killer cells activated by antigens, mitogens or alloantigens. Most immune cells express IFN-γ receptors and respond to IFNγ-induced signaling by up-regulating MHC class I expression. Human IFNγ does not show cross-reactivity with mouse. Recombinant human IFNγ is a non-glycosylated protein, containing 144 amino acids, with a molecular weight of 16.88 kDa.

Insulin-like Growth Factor I, IGF-I, is a growth factor produced by the liver when stimulated with growth hormone and can be found circulating throughout the body . IGF-I activates the IGF-I receptor (IGF1R) and the insulin receptor to mediate growth of almost every cell of the body. IGF-I is known as one of the most potent activators of the AKT signaling pathway which is known to be a stimulator of proliferation and an inhibitor of programmed cell death. Mature human IGF-I is 100% homologous with bovine and porcine proteins. Recombinant human IGF-I is a non-glycosylated protein, containing 70 amino acids, with a molecular weight of 7.7 kDa.

Insulin-like Growth Factor I, IGF-I, is a growth factor produced by the liver when stimulated with growth hormone and can be found circulating throughout the body . IGF-I activates the IGF-I receptor (IGF1R) and the insulin receptor to mediate growth of almost every cell of the body. IGF-I is known as one of the most potent activators of the AKT signaling pathway which is known to be a stimulator of proliferation and an inhibitor of programmed cell death. Mature human IGF-I is 100% homologous with bovine and porcine proteins. Recombinant human IGF-I is a non-glycosylated protein, containing 70 amino acids, with a molecular weight of 7.7 kDa.

Insulin-like Growth Factor II, IGF-II, is a major growth hormone made by Theca cells during gestation. While IGF-II is known to engage the IGF-I receptor (IGF1R) to mediate embryonic growth, IGF-II is also known to bind the IGF-II receptor (IGF2R). IGF2R is thought to be signaling dead receptor that acts as a sink by binding up free IGF-II. Recombinant human IGF-II is non-glycosylated protein, containing 67 amino acids, with a molecular weight of 7.5 kDa.

Insulin-like Growth Factor II, IGF-II, is a major growth hormone made by Theca cells during gestation. While IGF-II is known to engage the IGF-I receptor (IGF1R) to mediate embryonic growth, IGF-II is also known to bind the IGF-II receptor (IGF2R). IGF2R is thought to be signaling dead receptor that acts as a sink by binding up free IGF-II. Recombinant human IGF-II is non-glycosylated protein, containing 67 amino acids, with a molecular weight of 7.5 kDa.

Interleukin-1 alpha (IL-1α) is constitutively expressed by epithelial cells, but can also be produced by most other cells upon stimulation. IL-1β and IL-1α are two distinct and independently regulated gene products that comprise IL-1 and signal through the Type 1 IL-1 receptor (IL-1R1). Although IL-1α is cell associated and IL-1β is secreted, they have nearly identical biological activity in that they induce adhesion molecule expression on epithelial cells, control fever induction, and play a role in arthritis and septic shock. Signaling activated by the IL-1R1 promotes these activities through a MYD88 signaling pathway similar to those associated with Toll receptors. Recombinant human IL-1α is a non-glycosylated single chain protein, containing 159 amino acids, with a molecular weight of 18 kDa.

Interleukin-1 alpha (IL-1α) is constitutively expressed by epithelial cells, but can also be produced by most other cells upon stimulation. IL-1β and IL-1α are two distinct and independently regulated gene products that comprise IL-1 and signal through the Type 1 IL-1 receptor (IL-1R1). Although IL-1α is cell associated and IL-1β is secreted, they have nearly identical biological activity in that they induce adhesion molecule expression on epithelial cells, control fever induction, and play a role in arthritis and septic shock. Signaling activated by the IL-1R1 promotes these activities through a MYD88 signaling pathway similar to those associated with Toll receptors. Recombinant human IL-1α is a non-glycosylated single chain protein, containing 159 amino acids, with a molecular weight of 18 kDa.