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Manufactured by BioVendor

Insulin Human, E. coli Recombinant

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Species:Human
Cat. No. Size Price

New RP1762700025 25 mg $275
New RP1762700250 250 mg $490
New RP1762701000 1.0 g $1365
PubMed Product Details
Technical Data


Recombinant protein


Insulin Human Recombinant produced in E. coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.


E. coli


Greater than 98.0% as determined by RP-HPLC analysis

Biological Activity

28 units/mg.


The recombinant human insulin was lyophilized from a concentrated (1 mg/ml) solution with no additives.


It is recommended to reconstitute the lyophilized Insulin in sterile 0.005N HCl to not more than 1 mg/ml.


Cell culture and/or animal studies, In vitro, COVID-19


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Lyophilized Insulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Insulin should be stored at 4°C between 2–7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

Physical Appearance

Sterile filtered white lyophilized (freeze-dried) powder.


This BioVendor product is furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.


Research topic

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


Insulin is a peptide hormone secreted from B cells of islet of Langerhans in the pancreas with a molecular weight of about 5,800 and pI 5.4. It is consisted of 2 chains, A and B. It has 3 disulfide bonds formed between A6 and A11, A7 and B7, and A20 and B19. Insulin exists as a dimer molecule in acidic to neutral solution without Zn ion, and as a hexamer including two Zn ions in neutral solution if Zn ions are present. Main targets of insulin are liver, muscle, and adipose tissue. Insulin actions in these targets are as follows. In the liver, it promotes glycogenesis, protein synthesis, fatty acid synthesis, carbohydrate utilization, and inhibition of gluconeogenesis. In the muscle, it promotes membrane permeability for carbohydrates, amino acids and K ion, glycogenesis, protein synthesis, while inhibits protein degradation. In the adipose tissue, it promotes membrane permeability for glucose and fatty acid synthesis. A precursor of insulin, called proinsulin with a single polypeptide chain, is first synthesized in the cell, then sulfide bonds are formed, and finally by enzymatic cutting at two sites, active insulin and c-peptide (connecting peptide) are formed. Potency of an insulin preparation was originally determined by bioassay. However, whole body bioassay inevitably shows poor precision owing to individual variation. WHO issued 1st International Standard for human insulin in 1986 which has the potency of 26 IU/mg (0.038 mg/IU). In the same year, 1st International Standard of bovine insulin, the potency of which is 25.7 IU/mg, and Porcine insulin 1st International Standard, 26 IU/mg, were provided. Before these standards, in 1974, 1st International Reference Preparation of human insulin for immunoassay was provided as 3 IU/ampoule. Based on the above data, if the biological activity of insulin per molecule is the same among various animal species, potencies of animal insulin might be calculated from their molecular weights. But, so far, we do not have experimental proof about this. As the molecular weights of insulin of various animals are nearly the same, and the differences are within 1%, there may be no critical fault if we think that the general potency of insulin is 26 IU/mg. Rat and mouse have two molecular species of insulin, type 1 and type 2. Amino acid sequences of these molecular species are same between rat and mouse. But as their ratios are different between these two animal species, it is recommended to use standard preparation derived from each animals.

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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