Other Proteins

Recombinant Murine Amphiregulin (Legacy Tebubio ref. 167315-36). Amphiregulin is an EGF-related growth factor that signals through the EGF/TGF-alpha receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, Amphiregulin's extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant Murine Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.

Recombinant Murine Amphiregulin (Legacy Tebubio ref. 167315-36). Amphiregulin is an EGF-related growth factor that signals through the EGF/TGF-alpha receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, Amphiregulin's extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant Murine Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.

Recombinant Murine VCAM-1 (Legacy Tebubio ref. 167315-37). VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Murine VCAM-1 is a 74.4 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 87-97 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Murine VCAM-1 (Legacy Tebubio ref. 167315-37). VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Murine VCAM-1 is a 74.4 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 87-97 kDa by SDS-PAGE analysis under reducing conditions.

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