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Rat Insulin ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Species:Rat
Cat. No. Size Price

RTC018R 96 wells (1 kit) $673,05
PubMed Product Details
Technical Data


Sandwich ELISA, HRP-labelled antibody


The Rat Insulin ELISA system provides direct quantitative in vitro determination of rat insulin in plasma and serum. For research use only.


Serum, Plasma

Sample Requirements

20 µl/well


On blue ice packs. Upon receipt, store the product at the temperature recommended below.



Calibration Range

0.15 – 10 ng/ml

Limit of Detection

0.1 ng/ml

Spiking Recovery

CV = 94-110%

Dilution Linearity

CV = 88-112%



  • RUO
  • calibration range 0.15-10 ng/ml
  • limit of detection 0.1 ng/ml

Research topic

Diabetology - Insulin, C-Peptide, Proinsulin, Energy metabolism and body weight regulation, Animal studies


Rat insulin is a pancreatic hormone whose molecular weight is about 6000. It is a protein composed of two polypeptide chains, a shorter A-chain of twenty-one residues and a longer B-chain of thirty. The two chains are connected by two disulphide (-S-S-) linkages, while a third such linkage forms an intra-chain precursor called pro-insulin , in which the future A- and B-chains are linked end to end by a peptide strand, C-peptide, before being joined by their –S-S-bonds. It is found in the ß-cell granules in the pancreatic Islets of Langerhans. Specific proteases act on pro-insulin to release the C-peptide and insulin within the granule. On stimulation the C-peptide and insulin are released into the bloodstream in approximately equimolar amounts. Rat insulin differs from most other species in that it has two forms that are products of non-allelic genes. Translation of the two insulin mRNAs results in the synthesis of two preproinsulins differing by 7 amino acids. Processing of these peptides involves removal of the preregion and formation of proinsulins differing in 4 of 86 amino acids. The proinsulins are cleaved to mature insulins 1 and 2 which have identical A chains but differ by 2 amino acids in the B chain (positions 9 and 29). They are found roughly in the proportion 60% insulin 1 and 40% insulin 2 in the pancreas. Several factors can effect the release of insulin. One of the main regulators of insulin release is the amount of glucose in the blood. A rise in blood glucose stimulates the release of insulin while a fall in blood glucose suppresses its secretion. Amino acids also stimulate insulin-release to allow their uptake into muscle cells. Insulin is considered to be an anabolic hormone in that it promotes the synthesis of protein, lipid and glycogen and it inhibits the degradation of these compounds. The key target tissues of insulin are liver, muscle and adipose tissue. In promotes cell growth in many different cell types and is an absolute requirement for normal growth in all immature animals. Insulin exerts its effect through a receptor complex comprising two a sub-units of molecular weight 135 kDa and two ß sub-units of molecular weight 90 kDa. It is also well known for its involvement in diabetes, where insulin deficiency results in aberrant blood glucose homeostasis.

Summary References (8)

References to Insulin

  • Flier JS, Kahn CR, Roth J. Receptors, antireceptor antibodies and mechanisms of insulin resistance. N Engl J Med. 1979 Feb 22;300 (8):413-9
  • Frier BM, Ashby JP, Nairn IM, Baird JD. Plasma insulin, C-peptide and glucagon concentrations in patients with insulin-independent diabetes treated with chlorpropamide. Diabete Metab. 1981 Mar;7 (1):45-9
  • Judzewitsch RG, Pfeifer MA, Best JD, Beard JC, Halter JB, Porte D Jr. Chronic chlorpropamide therapy of noninsulin-dependent diabetes augments basal and stimulated insulin secretion by increasing islet sensitivity to glucose. J Clin Endocrinol Metab. 1982 Aug;55 (2):321-8
  • Kosaka K, Hagura R, Kuzuya T. Insulin responses in equivocal and definite diabetes, with special reference to subjects who had mild glucose intolerance but later developed definite diabetes. Diabetes. 1977 Oct;26 (10):944-52
  • Starr JI, Mako ME, Juhn D, Rubenstein AH. Measurement of serum proinsulin-like material: cross-reactivity of porcine and human proinsulin in the insulin radioimmunoassay. J Lab Clin Med. 1978 Apr;91 (4):683-92
  • Temple R, Clark PM, Hales CN. Measurement of insulin secretion in type 2 diabetes: problems and pitfalls. Diabet Med. 1992 Jul;9 (6):503-12
  • Temple RC, Carrington CA, Luzio SD, Owens DR, Schneider AE, Sobey WJ, Hales CN. Insulin deficiency in non-insulin-dependent diabetes. Lancet. 1989 Feb 11;1 (8633):293-5
  • Temple RC, Clark PM, Nagi DK, Schneider AE, Yudkin JS, Hales CN. Radioimmunoassay may overestimate insulin in non-insulin-dependent diabetics. Clin Endocrinol (Oxf). 1990 Jun;32 (6):689-93
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