Other Proteins

Recombinant Murine Prokineticin-2 (Legacy Tebubio ref. 167315-38). Prokineticin-2 (PK2) is a cysteine-rich secreted protein that is expressed in the testis and, in lower levels, in the small intestine. PK2 regulates various biological functions, including gastrointestinal motility, angiogenesis and circadian rhythms. It is closely related to EG-VEGF (Prokineticin-1), and binds to two orphan B-protein-coupled receptors termed PK-R1 and PK-R2. Recombinant Murine Prokineticin-2 is an 11.6 kDa protein consisting of 103 amino acid residues, including ten cysteine residues that can potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Murine Prokineticin-2 (Legacy Tebubio ref. 167315-38). Prokineticin-2 (PK2) is a cysteine-rich secreted protein that is expressed in the testis and, in lower levels, in the small intestine. PK2 regulates various biological functions, including gastrointestinal motility, angiogenesis and circadian rhythms. It is closely related to EG-VEGF (Prokineticin-1), and binds to two orphan B-protein-coupled receptors termed PK-R1 and PK-R2. Recombinant Murine Prokineticin-2 is an 11.6 kDa protein consisting of 103 amino acid residues, including ten cysteine residues that can potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Murine C5a (Legacy Tebubio ref. 167315-40). Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b‐9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL‐8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive

Recombinant Murine C5a (Legacy Tebubio ref. 167315-40). Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b‐9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL‐8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive

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-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.