Other Proteins

Recombinant Human IGF-BP6 (Legacy Tebubio ref. 167350-07B). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP6, which specifically inhibits IGF-II actions, is produced by bone cells and is the major IGF-BP present in cerebrospinal fluid. IGF-BP6 has been shown to inhibit IGF-II-dependent cancers such as neuroblastoma, colon cancer and rhabdomyosarcoma. Recombinant Human IGF-BP6 has a calculated mass of 22.3 kDa and consists of 213 amino acid residues, including the IGF-BP domain and thyroglobulin type-I domain. Recombinant Human IGF-BP6 migrates at an apparent molecular weight of approximately 23.0-30.0 kDa by SDS-PAGE analysis under non-reducing conditions.

Recombinant Human IGF-BP7 (Legacy Tebubio ref. 167350-09). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.

Recombinant Human IGF-BP7 (Legacy Tebubio ref. 167350-09). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. It plays a role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.

Recombinant Human IGF-BP1 (Legacy Tebubio ref. 167350-10). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high-affinity complexes with both IGF-I and IGF-II. IGF-BP1 is a 25.4 kDa, cysteine-rich, secreted protein expressed in the liver, deciduas, kidneys, and in amniotic fluid, where it is the most abundant IGF-BP. Levels of IGF-BP1 in serum are lowest after food consumption. IGF-BP1 binds to both IGF-I and IGF-II with equal affinity. Phosphorylated IGF-BP1 hinders IGF actions, whereas nonphosphorylated IGF-BP1 is stimulatory. Recombinant Human IGF-BP1 is a 25.4 kDa protein consisting of 235 amino acid residues (Isoform A).

Recombinant Human IGF-BP1 (Legacy Tebubio ref. 167350-10). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high-affinity complexes with both IGF-I and IGF-II. IGF-BP1 is a 25.4 kDa, cysteine-rich, secreted protein expressed in the liver, deciduas, kidneys, and in amniotic fluid, where it is the most abundant IGF-BP. Levels of IGF-BP1 in serum are lowest after food consumption. IGF-BP1 binds to both IGF-I and IGF-II with equal affinity. Phosphorylated IGF-BP1 hinders IGF actions, whereas nonphosphorylated IGF-BP1 is stimulatory. Recombinant Human IGF-BP1 is a 25.4 kDa protein consisting of 235 amino acid residues (Isoform A).

Recombinant Human ApoA-I (Legacy Tebubio ref. 167350-11). ApoA-I is a 29.0 kDa protein produced in the liver and intestine, and secreted as the predominant constituent of nascent high density lipoprotein (HDL) particle. ApoA-I, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol. This ApoA-I ability enables HDL to remove excess peripheral cholesterol, and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is thought to inhibit atherogenesis. For this reason, HDL is also known as the "good cholesterol". The therapeutic potential of ApoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of ApoA-I (called ApoA-I Milano). The availability of recombinant normal ApoA-I should facilitate further investigation into the potential usefulness of ApoA-I in preventing atherosclerotic vascular diseases. Recombinant

Recombinant Human ApoA-I (Legacy Tebubio ref. 167350-11). ApoA-I is a 29.0 kDa protein produced in the liver and intestine, and secreted as the predominant constituent of nascent high density lipoprotein (HDL) particle. ApoA-I, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol. This ApoA-I ability enables HDL to remove excess peripheral cholesterol, and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is thought to inhibit atherogenesis. For this reason, HDL is also known as the "good cholesterol". The therapeutic potential of ApoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of ApoA-I (called ApoA-I Milano). The availability of recombinant normal ApoA-I should facilitate further investigation into the potential usefulness of ApoA-I in preventing atherosclerotic vascular diseases. Recombinant

Recombinant Rat IL-2 (Legacy Tebubio ref. 167400-02). IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Rat IL-2 is a 15.3 kDa protein containing 134 amino acid residues.

Recombinant Rat IL-2 (Legacy Tebubio ref. 167400-02). IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Rat IL-2 is a 15.3 kDa protein containing 134 amino acid residues.