胰島素 ELISA 的 C 肽-C-Peptide of Insulin ELISA代理/參數/廠家-ELISA試劑盒-艾美捷科技有限公司

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中文名稱: 胰島素 ELISA 的 C 肽

英文名字: C-Peptide of Insulin ELISA

供應商: Ansh Labs

產品貨號: AL-151

產品報價: ￥詢價/96wellmicrotiter

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背景資料: Insulin is a member of a family of structurally-related regulatory proteins; other proteins in this group include the insulin-like growth factors and relaxin. Insulin is produced by the β-cells of the pancreatic islets and is initially synthesized as a 12 kDa pre-prohormone, which undergoes intracellular processing to a 9 kDa, 86-amino acid prohormone and subsequent packaging in storage granules. Within these granules, disulfide bonds are formed between the A and B chains of the insulin molecule and the C-peptide region is cleaved, resulting in the 51-amino acid, 6 kDa mature insulin molecule. Upon stimulation, the islet cells release equimolar amounts of insulin and C-peptide, and small amounts of proinsulin and other intermediates (<5% of normal total insulin secretion)1.
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nInsulin is the most important hormone of the fed-state, and is the only physiologic hormone which significantly lowers blood glucose levels. In response to a number of substrates and other stimuli, including glucose and amino acids, insulin is secreted into the hepatic portal circulation1,2. Fifty-percent of the insulin is removed on first-pass through the liver, the remainder enters the general circulation and is carried to other target tissues. Insulin then binds to specific cell-surface receptors3 and, through incompletely defined mechanisms, facilitates substrate uptake and intracellular utilization, resulting in net increases in intracellular lipid, protein and glycogen1-4. In addition to its role in peripheral metabolism, insulin may influence central regulation of energy balance5. Insulin is rapidly cleared both by liver uptake, tissue utilization and renal clearance (T1/2 of about 4 mins), and circulating insulin levels are very low during fasting. In contrast, C-peptide of insulin does not undergo significant liver or extra-renal metabolism and, therefore, has a much longer circulating half-life (~30 min).1
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nBasal- and glucose-stimulated circulating insulin concentrations are relatively stable during infancy and childhood, and increase during puberty due to decreased insulin sensitivity [6]. Insulin concentrations tend to be higher in obese individuals, particularly those with an increased proportion of visceral (abdominal) fat7. Glucose counter-regulatory hormones, such as glucagon, glucocorticoids, growth hormone and epinephrine, decrease insulin sensitivity and action; insulin levels may increase during exogenous administration of these substances. 1,2
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nMeasurement of circulating insulin concentrations may be useful in the clinical evaluation of several conditions. Elevated serum insulin levels in the presence of low glucose concentrations may be indicative of pathologic hyperinsulinism, e.g. nesidioblastosis and islet-cell tumor [8]. Elevated serum fasting insulin levels with normal or elevated glucose concentrations, and exaggerated insulin and glucose response to exogenous glucose administration are characteristic of the insulin-resistant forms of glucose intolerance and diabetes mellitus and other insulin resistant conditions.7, 9, 10 High circulating insulin concentrations may be involved in the pathogenesis of hypertension and cardiovascular disease10,11. Conversely, low insulin concentrations in the presence of hyperglycemia suggests insulin-deficiency, e.g. insulin-dependent or Type I diabetes mellitus.
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nAlthough the C-peptide of insulin is biologically inactive, it has a longer circulating half-life than insulin and undergoes relatively minimal hepatic metabolism. In addition, C-peptide of insulin assays may be analytically more sensitive than insulin assays. Because of these factors, measurement of C-peptide of insulin may be useful in evaluating insulin secretion in a variety of clinical conditions.12-14
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nReferences:
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n1. Gerich JE: Hormonal control of homeostasis. IN Galloway JA, Potvin JH, Shuman CR (eds): Diabetes Mellitus, ninth edition. Eli Lilly Co, Indianapolis, 1988, pp 46-63.
n2. Rasmussen H, Zawalick KC, Ganesan S, Calle R, Zawalich WS: Physiology and pathophysiology of insulin secretion. Diab Care 13:655-666, 1990.
n3. Gammeltoft S: Insulin receptors: binding kinetics and structure-function relationship of insulin. Physiol Rev 64:1321-1378, 1984.
n4. Rosen OM: After insulin binds. Science 237:1452-1458, 1987.
n5. Schwartz MW, Figlewicz D, Baskin DG, Woods SC, Porte D Jr: Insulin in the brain: A hormonal regulator of energy balance. Endocrin Rev 13:387- 414, 1992.
n6. Amiel SA, Caprio S, Sherwin RS, Plewe G, Haymond MW, Tamborlane WV: Insulin resistance of puberty: a defect restricted to peripheral glucose metabolism. J Clin Endocrinol Metab 72:277-282, 1991.
n7. Bj?rntorp P: Metabolic implications of body fat distribution. Diab Care 14:1132 - 1143, 1991.
n8. Haymond MW: Hypoglycemia in infants and children. Endocrinol Metab Clin North Amer 18:211-2552, 1989.
n9. O'Rahilly S, Moller DE: Mutant insulin receptors in syndromes of insulin resistance. Clin Endocrinol 36:121-132, 1992.
n10. Reaven GM: Insulin resistance, hyperinsulinemia, hypertriglyceridemia, and hypertension. Parallels between human disease and rodent models. Diab care 14:195-202, 1991.
n11. Fontbonne AM, Eschwege EM: Insulin and cardiovascular disease. Paris prospective study. Diab Care 14:461-469, 1991.
n12. Horwitz DL, Kuzaya H, Rubenstein AH: Circulating serum C-peptide: a brief review of diagnostic implications. New Engl J Med 295:207-209, 1976.
n13. Bommen M, Stanhope R, Kurtz AB, Brook CGD: Plasma C peptide in hyperinsulinaemic hypoglycaemia. Arch Dis Child 59:1096-1098, 1984.
n14. Field JB: Hypoglycemia. Definition, clinical presentations, classification, and laboratory tests. Endocrinol Metab Clin North Am 18:27-43, 1989.
n15. HHS Publication, 5th ed., 2007. Biosafety in Microbiological and Biomedical Laboratories. Available http://www.cdc.gov/biosafety/publications/bmbl5/BMBL5
n16. DHHS (NIOSH) Publication No. 78–127, August 1976. Current Intelligence Bulletin 13 - Explosive Azide Hazard. Available http:// www.cdc.gov/niosh.
n17. Approved Guideline – Procedures for the Handling and Processing of Blood Specimens, H18-A3. 2004. Clinical and Laboratory Standards Institute.
n18. Kricka L. Interferences in immunoassays – still a threat. Clin Chem 2000; 46: 1037–1038.

產品描述: The C-Peptide of Insulin Enzyme-Linked Immunosorbent (ELISA) Kit provides materials for the quantitative measurement of C-peptide of insulin in human serum and plasma.

產品特點

保存建議: Store at 2 to 8°C until expiration date.

其他: Ansh labs是開發和生產免疫檢測試劑盒和定制生物技術檢測產領創者，總部位于美國休斯敦，公司產品遍及全球80多個國家。公司于2011年成立，核心團隊來自于Diagnostic system laboratory，專注于女性健康和激素檢測領域近40年，擁有全球領先的核心技術，以及多年經驗生物技術研發經驗的科學家團隊，產品覆蓋生殖健康，高危妊娠，腫瘤，糖尿病等多個疾病領域，圍繞最新的免疫分析技術，多種蛋白和單克隆抗體，如AMH，BMP-15, Follistatin, GDF-9, IGF-I, IGF-II, IGFBP-2, IGFBP-3, IGFBP-4, IGFBP-5, Inhibin Alpha, Inhibin ?A, Inhibin ?B, MBP, PAPP-A, PAPP-A2 and Vitamin D.等幾十余種試劑產品，也同時涵蓋小鼠，大鼠，狗，羊，牛等靈長類多個物種的獨特的物種特異性的試劑。 Ansh labs 坐落于美國德克薩斯州，是目前世界上唯一能提供TGF-β超家族所有成員的檢測公司，也是最早專注激素類產品研究和新型免疫檢測技術的先驅者。優勢產品涉及TGF-β super family、AMH/抑制素B(human/animal)、full panel IGFs、以及最完整的胰高血糖素系列。