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.
Magnesium Colorimetric Assay Kit (Xylidyl Blue-I Method) Reference: JAI-CMG-035 Magnesium (Mg2+) is one of the most abundant trace metals in living organisms, contributing to a variety of biological functions including ATP and nucleic acid processing, energy metabolism, and enzymatic function. Magnesium forms complexes with multiple molecules such as phospholipids and ATP. Approximately 69% of magnesium ions are stored in bone. The rest are part of the intermediary metabolism about 70% being present in free form while the other 30% is bound to proteins (especially albumin), citrates, phosphate, and other complex formers. The Mg2+ serum level is kept constant within very narrow limits. Regulation takes place mainly via the kidneys, especially via the ascending loop of Henle. Low serum levels of magnesium have been associated with metabolic syndrome, diabetes mellitus type 2, and hypertension.
Zinc Colorimetric Assay Kit (5-Br-PAPS Method) Reference: JAI-CZN-001 Zinc (Zn2+) is an essential trace element, vital for the health of animals, plants, and microorganisms . Zinc is found in hundreds of enzymes, is stored and transferred in metallothioneins, and serves as structural ions in transcription factors. Zinc is often coordinated to the sides chains of amino acids, such as aspartic acid, glutamic acid, histidine and cysteine and is involved in nucleid acid and protein synthesis. It is therefore a necessary complement for cell replication. In humans, zinc interacts with a variety of organic ligands, and has roles in nucleic acid metabolism, apoptosis, neurological development, signal transduction, and gene expression. Zinc deficiency is related to skin lesions, irritability, loss of hair, growth retardation and impaired immunological functions.
Total Antioxidant Capacity (PAO) Test Kit Reference: JAI-KPA-050 Oxidative stress plays on important role in various diseases and aging. The control of oxidative stress is expected to be useful to prevent diseases and aging.Oxidative stress is caused by the imbalance between reactive oxygen species (ROS) and antioxidant defense system. For accurate assessment of oxidative stress, measurement of ROS, oxidative damage and antioxidant activity may be essential. Recently, antioxidants as functional foods which scavenge ROS attract a great deal of attention.