Interferon gamma is the only type II interferon and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is due partly to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon gamma is the only type II interferon and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is due partly to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon lambda 1, also known as interleukin 29, belongs to the newly classified type III interferon family. Expression of IFNL1 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL1 exerts antiviral activity and upregulation of MHC class I antigen expression. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interferon lambda 2, also known as interleukin 28A, belongs to the newly classified type III interferon family. Expression of IFNL2 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL2 exerts antiviral activity by activating mx proteins, 2',5'-oligoadenylate synthetase, and interferon regulatory factor 9. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interferon lambda 3, also known as interleukin 28B, belongs to the newly classified type III interferon family. Expression of IFNL3 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL3 exerts antiviral activity and up regulation of MHC class I antigen expression. It also plays a role in Toll-like receptor (TLR)-induced antiviral defense. IFNL3 signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3. In individuals with chronic hepatitis C, the presence of specific polymorphisms near this gene has been associated with an increased response in treatment for the condition with interferon and ribavirin.

Interferon omega 1 is a member of the type I family of interferons. It is the only functional interferon omega gene in humans; many pseudogenes of interferon omega exist in humans, some of which are functional in non-primate placental mammals. Expression of IFNW1 is seen in leukocytes in response to viral infection or treatment with double-stranded RNA. It stimulates NK cell activity, enhances expression of major histocompatibility complex class I antigens, and inhibits proliferation of lymphocytes stimulated with mitogens or allogeneic cells. It also inhibits proliferation of a variety of tumor cell lines in vitro.

IGF1 belongs to the insulin gene family. It is a mitogenic polypeptide growth factor that stimulates the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGF1 DES is a truncated variant of human IGF1 with the tripeptide Gly-Pro-Glu absent from the N-terminus. It has been isolated from bovine colostrum, human brain, and porcine uterus. The IGF1 DES is believed to result from post-translational cleavage of IGF1 via protease activity. It is about 10-fold more potent than IGF1 at stimulating hypertrophy and proliferation of cultured cells, a consequence of much reduced binding to IGF-binding proteins, which is in turn caused by the absence of the glutamate at position 3. Clinical opportunities for IGF1-DES have not yet been evaluated, but could apply in catabolic states as well as for the treatment of inflammatory bowel diseases.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids and 3 intra-molecular disulfide bonds. This particular product has been labeled with the stable 15N isotope to help track its activity.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. They are predominantly produced in the liver. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Sterile Filtered White lyophilized powder. Purified and tested for use in cell culture.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant murine IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. They are predominantly produced in the liver. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Insulin-like Growth Factor-Binding Protein 3 (IGFBP3) belongs to the IGFBP family, which are all proteins with conserved cysteine residues, an IGFBP domain, and a thyroglobulin type-I domain. IGFBP3 is expressed by most tissues and is the most abundant IGFBP protein. It has higher levels of expression during postnatal life, which peak during puberty. The expression of IGFBP3 in fibroblasts is stimulated by a number of mitogenic growth factors. The protein forms a ternary complex with IGFI or IGFII, and an acid-labile subunit, causing it to circulate in the plasma. As this complex, it prolongs the half-life of IGFs and alters their interaction with cell surface receptors. Decreased plasma levels of IGFBP3 often happen during the progression of prostate cancer from benign to metastatic disease.