Somatostatin is a regulatory hormone that is expressed throughout the body and inhibits the release of numerous secondary hormones by binding to high-affinity G protein-coupled somatostatin receptors. This cyclic tetradecapeptide inhibits the secretion of many important hormones, including somatotropin (also designated growth hormone, or GH), insulin and glucagon. Somatostatin is found in both the hypothalamus and pancreas. Somatostatin is thought to be involved in the regulation of insulin

Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. Binding of this growth factor to its affinity receptor elicits a variety of cellular responses. It is released by platelets upon wounding and plays an important role in stimulating adjacent cells to grow and thereby heal the wound. [SUBUNIT] Antiparallel disulfide-linked dimer of nonidentical (A and B) chains. Homodimers of A and B chains are implicated in transformation processes. A-A and B-B, as well as A

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophos

This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq, Jul 2008].

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophos

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophos