Periostin (human) Matched Pair Detection Set Reference: AG-46B-0005 Periostin is a 90-kDa matricellular protein that consists of a typical signal sequence, followed by a cysteine-rich region, an EMI domain (protein-protein interactions), four tandem fasciclin-like domains that are responsible for integrin binding, and a C-terminal region. Periostin was originally isolated as an osteoblast-specific factor that functions as a cell adhesion molecule for pre-osteoblasts and in osteoblast recruitment, attachment and spreading. Periostin is also involved in many fundamental biological processes such as cell proliferation, cell invasion and angiogenesis. Periostin expression is increased by both transforming growth factor beta1 (TGF-beta1) and bone morphogenetic protein 2 (BMP-2). Changes in periostin expression are commonly detected in various cancers and pre-cancerous conditions, and periostin may be involved in regulating cancer cell activities that contribute to tumorigenesis, cancer progression and metastasis. Periostin up-regulation in cancers usually correlates with aggressiveness and/or poor survival. Periostin has shown to be involved in many aspects of allergic inflammation, such as eosinophil recruitment, airway remodeling, development of a Th2 phenotype and increased expression of inflammatory mediators. It is evaluated as a biomarker for bronchial asthma and airway inflammation.
IL-36Ra (human) Matched Pair Detection Set Reference: AG-46B-0006 IL-36Ra/IL-1F5 is a highly and specific antagonist of the IL-1 receptor-related protein 2-mediated response to IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9). These cytokines bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. Recently mutations that affect the levels and the activity of IL-36Ra have been found in patients with pustular psoriasis, leading to enhanced production of inflammatory cytokines (IL-8 in particular) by keratinocytes.
IL-38 (human) Matched Pair Detection Set Reference: AG-46B-0007 IL-38 (also called IL-1F10, and previously named IL1HY2, FIL1theta, or IL-1theta) is expressed in skin, tonsil, thymus, spleen, fetal liver, and salivary glands. The expression in a variety of immune tissues and similarity to IL-36Ra and IL-1Ra suggest a role of IL-38 in the inflammatory response. IL-38 binds to the IL-36R and exerts antagonistic effects similar to those of IL-36Ra.
Zinc-alpha-2-glycoprotein (human) Matched Pair Detection Set Reference: AG-46B-0008 Zinc-alpha-2-glycoprotein (ZAG), first identified in the 1960s, derives its name from its precipitation from human plasma upon the addition of zinc salts. ZAG has since been found in secretory epithelial cells and in a range of body fluids. ZAG is identical to a lipid mobilizing factor isolated from the urine of patients with cancer cachexia and stimulates lipolysis in in vitro and in vivo experiments. Due to its expression in, and secretion from adipocytes, ZAG is considered an adipokine. Recently the clinical significance of ZAG has been clarified. ZAG expression in adipocytes is inversely related to fat mass, thus it is intimately involved in the maintenance of body weight in mice and humans. Epidemiological studies have uncovered an association between ZAG and plasma cholesterol. The non-synonymous single nucleotide polymorphism rs4215 in ZAG is associated with plasma cholesterol and obesity. Structurally ZAG possesses a class I major histocompatibility complex (MHC) protein fold. It is distinct from other members of this protein family in that it is soluble, rather than being anchored to plasma membranes, and it associates with prolactin inducible protein rather than beta2-microglobulin. Similar to peptide antigen-presenting class I MHC molecules, ZAG possesses an open apical groove between its alpha1 and alpha2 domain helices.
IL-36beta (human) Matched Pair Detection Set Reference: AG-46B-0009 IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination.
IL-36gamma (human) Matched Pair Detection Set Reference: AG-46B-0010 IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination.
Asprosin (human) Matched Pair Detection Set Reference: AG-46B-0011 Asprosin is a new fasting-induced protein hormone that targets the liver to increase plasma glucose levels. Asprosin is the C-terminal cleavage product of the protein pro-Fibrillin-1. Asprosin is secreted from white adipose tissue and increases hepatic glucose production by using cAMP as a second messenger, leading to activation of protein Kinase A. Reduction of Asprosin levels protects against metabolic syndrome-associated hyperinsulinism. Asprosin may act as a circulating hunger signal. Indeed, peripherally injected recombinant asprosin can cross the blood-brain barrier and intracerebroventricular (i.c.v.) injection of recombinant asprosin stimulated appetite in wild-type mice, indicating a central mechanism of action. Loss of Asprosin in mice and human leads to decreased fat mass and body weight, and hypophagia. Mice are also completely protected from the development of diet-induced obesity. Asprosin works by stimulating the orexigenic AgRP+ (Agouti related neuropeptide) neurons via a cAMP-dependent pathway and by inhibiting the anorexigenic neurons POMC+ (pro-opiomelanocortin) neurons in a GABA-dependent manner. Mutation in Asprosin in human leads to the pattern of metabolic dysregulation, including partial lipodystrophy, accompanied by reduced plasma insulin. Due to its key role in food regulation, Asprosin function could serve as a potentially unique therapeutic target against obesity, diabetes or metabolic diseases.
Erythroferrone (human) Matched Pair Detection Set Reference: AG-46B-0012 Erythroferrone (also called Myonectin, CTRP15 or Fam13B) is a member of CTRPs (C1q/TNF-related proteins), which are conserved paralogs of adiponectin containing collagen-like and globular C1q-like domains. Erythroferrone plays two different regulatory roles: i) Erythroferrone (called Myonectin for this role) is a myokine abundantly expressed in skeletal muscle tissue, upregulated by voluntary exercise that is suppressed by fasting and induced by refeeding; it participates in the regulation of systemic lipid metabolism by promoting the clearance of nonesterified fatty acids (NEFA) from circulation. As a myokine, Erythroferrone/Myonectin acts as an endurance exercise-driven myokine which protects the heart from ischemic injury by reducing cardiomyocyte apoptosis and macrophage inflammatory response. ii) Erythroferrone is produced by erythroblasts after bleeding or EPO treatment and acts on hepatocytes to suppress hepcidin expression, resulting in increased release of iron from cellular iron stores. Erythroferrone acts on hepcidin by inhibiting members of the BMP-5, BMP-6 and BMP-7 subgroup of BMPs. Erythroferrone functions as erythroid modulator of iron metabolism and hemoglobin synthesis. Our Erythroferrone (human) Matched Pair Detection Set has been validated by the Swiss Laboratory for Doping Analyses in a recent publication reporting that our assay can sensitively detect the stimulation of erythropoiesis, including erythropoiesis stimulating agents (ESA, such as Erythropoietin) abuse and blood withdrawal. Erythroferrone is a biomarker for different types of anemia, for cardiology and potentially also for metabolic diseases.
UIBC Colorimetric Assay Kit (Bathophenanthroline Method) Reference: JAI-CBC-800 Iron is an essential element in mammalians and is contained in various enzymes and is involved in oxidation reactions. Iron is essential during transport of oxygen as composition element of hemoglobin or myoglobin. 30% of the transferrin is associated with Fe3+ in blood. Free transferrin is not associated to iron. TIBC (Total iron binding capacity) = UIBC (Unsaturated iron binding capacity) + Serum iron. TIBC levels change in blood disorders, hepatic diseases, tumors and inflammation. UIBC levels are increased in patients with iron deficiency. Decreased levels of UIBC are seen in patients with infectious diseases, nephrotic syndrome and low proteinosis.
Calcium Colorimetric Assay Kit (O-Cresolphthalein Method) Reference: JAI-CCA-030 Calcium is the most abundant mineral, essential for all living organisms, where Ca2+ sequestration and release into and out of the cytoplasm functions as a signal for many cellular processes. 99% is present as calcium hydroxyapatite in bones and less than 1 % is present in the extra-osseous ICS (intracellular space) or ECS (extracellular space), responsible for a myriad of important physiological effects. Calcium ion channels control the migration of calcium ions across cell membranes, permitting the activation and inhibition of a wide variety of enzymes. Calcium ions affect the contractility of the heart and the skeletal musculature and are essential for the function of the nervous system. In addition, calcium ions play an important role in blood clotting and bone mineralization. Abnormal calcium levels have been tied to neurological, endocrine, cardiovascular, digestive, metabolic, and pulmonary diseases, as well as cancer. In plasma, calcium is bound to a considerable extent to proteins (approx. 40%), 10% is in the form of incorganic complexes and 50% is present as free (ionized) calcium. Clacium homeostasis is regulated by the parathyroid hormone (PTH), calcitriol (CT) and calcitonin. Low levels of calcium are found in hypoparathyroidism, pseudohypoparathyroidism, vitamin D deficiency, malnutrition and intestinal malabsorbtion.
Iron Colorimetric Assay Kit (Ferrozine Method) Reference: JAI-CFE-005 Iron is a mineral (functioning as an enzyme cofactor) that plays an essential role in many biological processes. It is essential to nearly all known organisms. As a transition element it can form a range of oxidation states, the most common being Fe2+ (or ferrous iron) and Fe3+ (or ferric iron). Ingested iron is mainly absorbed in the form of Fe2+. The trivalent form and the heme-bound Fe2+-component of iron is reduced by vitamin C. Before passing into the plasma, it is oxidized by ceruloplasmin to Fe3+ and bound to transferrin to form a transferrin-iron complex. Iron is generally stored in the centre of metalloproteins, in the heme complex, and in oxygen carrier proteins. Iron-containing proteins participate in many reactions, often utilizing transitory changes in the oxidation state of iron to carry out chemical reactions. Iron is important for redox reactions, oxygen transport (e.g. hemoglobin), short-term oxygen storage (e.g. myoglobin) and energy generation. Iron deficiency has many adverse consequences, including anemia, hemochromatosis, chronic renal disease and in children, behavioral and learning disorders. Iron excess is toxic to the body, harming the heart, liver, skin, pancreatic islet beta cells, bones, joints, and pituitary gland. Maintaining proper iron balance is essential for maintaining homeostasis and health.
Iron Colorimetric Assay Kit (Nitroso-PSAP Method) Reference: JAI-CFE-010 Iron is a mineral (functioning as an enzyme cofactor) that plays an essential role in many biological processes. It is essential to nearly all known organisms. As a transition element it can form a range of oxidation states, the most common being Fe2+ (or ferrous iron) and Fe3+ (or ferric iron). Ingested iron is mainly absorbed in the form of Fe2+. The trivalent form and the heme-bound Fe2+-component of iron is reduced by vitamin C. Before passing into the plasma, it is oxidized by ceruloplasmin to Fe3+ and bound to transferrin to form a transferrin-iron complex. Iron is generally stored in the centre of metalloproteins, in the heme complex, and in oxygen carrier proteins. Iron-containing proteins participate in many reactions, often utilizing transitory changes in the oxidation state of iron to carry out chemical reactions. Iron is important for redox reactions, oxygen transport (e.g. hemoglobin), short-term oxygen storage (e.g. myoglobin) and energy generation. Iron deficiency has many adverse consequences, including anemia, hemochromatosis, chronic renal disease and in children, behavioral and learning disorders. Iron excess is toxic to the body, harming the heart, liver, skin, pancreatic islet beta cells, bones, joints, and pituitary gland. Maintaining proper iron balance is essential for maintaining homeostasis and health.