growth-regulated α protein

C-X-C motif chemokine 2 (CXCL2,MIP-2) belongs to the intercrine alpha (chemokine CxC) family. It was originally identified as a heparin-binding protein secreted from a murine macrophage cell line in response to endotoxin stimulation. The expression of mouse MIP-2 is stimulated by endotoxin. The mouse MIP-2 shares approximately 63% aa sequence identity with murine KC, another mouse alpha chemokine, which is induced by PDGF. It has been suggested that mouse KC and MIP-2 are the homologs of the human GROs and rat CINCs. Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. The expression of MIP-2 was found to be associated with neutrophil influx in pulmonary inflammation and glomerulonephritis, suggesting that MIP-2 may contribute to the pathogenesis of inflammatory diseases.

Growth-regulated alpha protein (CXCL1,KC), is a member of the alpha chemokine subfamily, was initially identified as an immediate early gene induced in mouse fibroblasts by platelet-derived growth factor. The N-terminal processed form KC(5-72) of the protein is produced by proteolytic cleavage after secretion from bone marrow stromal cells, and shows a highly enhanced hematopoietic activity. Mouse KC shows approximately 63% identity to that of mouse MIP-2. KC is also approximately 60% identical to the human GROs. It has been suggested that mouse KC and MIP-2 are the orthologs of the human GROs and rat CINCs. Cxcl1 has chemotactic activity for neutrophils, and contributes to neutrophil activation during inflammation. Hematoregulatory chemokine, in vitro, suppresses hematopoietic progenitor cell proliferation.

GHR Growth Hormone R Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 29.6 kDa and the accession number is P16310-1.

Pegvisomant, a growth hormone receptor (GHR) antagonist, is a well-known drug that was designed to treat acromegaly. However, recent studies have indicated that the GHR is a moonlighting protein that may exhibit dual functions based on its localization in the plasma membrane and nucleus.

Growth Hormone Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 22.1 kDa and the accession number is P01241.

Growth Hormone Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 24.7 kDa and the accession number is P01241.

GHR Growth Hormone R Protein, Mouse, Recombinant (His & hFc) is expressed in HEK293 mammalian cells with His and hFc tag. The predicted molecular weight is 56.8 kDa and the accession number is Q3UP14.

Somatotropin(GH) is a member of the somatotropin prolactin family of hormones which play an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. GH stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

Growth hormone receptor is a transmembrane receptor for growth hormone (GH). GH is a single-chain polypeptide that is mainly synthesized and released from the anterior pituitary gland and plays essential roles in growth, development and metabolism. GH exerts its physiological actions via GH binding to its receptor in its extracellular domain. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. Growth hormone receptor has been shown to interact with SGTA, PTPN11, Janus kinase 2, Suppressor of cytokine signaling 1 and CISH.

GHR Growth Hormone R Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 30.3 kDa and the accession number is Q3UP14.

GHR Growth Hormone R Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 55.4 kDa and the accession number is P16310-1.

Biliverdin reductase (hBVR) is a serine threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin. BVR consists of an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a six-stranded β-sheet that is flanked on one face by several α-helices. The C-terminal and N-terminal domains interact extensively, forming the active site cleft at their interface. Biliverdin reductase (BVR) catalyzes the last step in heme degradation by reducing the γ-methene bridge of the open tetrapyrrole, biliverdin IXα, to bilirubin with the concomitant oxidation of a β-nicotinamide adenine dinucleotide (NADH) or β-nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. It is now recognized that human BVR (hBVR) is a dual-specificity kinase (Ser Thr and Tyr) upstream activator of the insulin insulin growth factor-1 (IGF-1) and mitogen-activated protein kinase (MAPK) signaling pathways. Human BVR (hBVR) is essential for MAPK-extracellular signal-regulated kinase (ERK)1 2 (MEK)-eukaryotic-like protein kinase (Elk) signaling and has been identified as the cytoplasm-nuclear heme transporter of ERK1 2 and hematin, the key components of stress-responsive gene expression.