Other Proteins

Recombinant Human IGF-BP4 (Legacy Tebubio ref. 167350-05B). IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF-independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovari

Recombinant Human IGF-BP2 (Legacy Tebubio ref. 167350-06B). 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-BP2 is a cysteine-rich, secreted protein produced by bone cells, and is most abundant in the brain. IGF-BP2 has been shown to inhibit IGF-II action in human breast and ovarian carcinoma cells. Recombinant Human IGF-BP2 is a 31.5 kDa protein consisting of 289 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.

Recombinant Human IGF-BP2 (Legacy Tebubio ref. 167350-06B). 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-BP2 is a cysteine-rich, secreted protein produced by bone cells, and is most abundant in the brain. IGF-BP2 has been shown to inhibit IGF-II action in human breast and ovarian carcinoma cells. Recombinant Human IGF-BP2 is a 31.5 kDa protein consisting of 289 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.

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-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).