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Insulin Human Recombinant ( Insulin Human )

DescriptionInsulin 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

$259.00

Data sheet

Formulation The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Solubility It is recommended to reconstitute the lyophilized Insulin in sterile 0.005N HCl not more than 1 mg/ml.
Purity Greater than 98.0% as determined by RP-HPLC analysis.
Inactivation Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
Description 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.
Protein Background Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Expression host Escherichia Coli.
Reagent Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Stability 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.
Biological Activity The Biological Activity was determined to be 28 units/mg.
References Title: PI3K integrates the effects of insulin and leptin on large-conductance Ca2+-activated K+ channels in neuropeptide Y neurons of the hypothalamic arcuate nucleusPublication: American Journal of Physiology-Endocrinology and Metabolism 298.2 (2010): E193-E201.Link: http://ajpendo.physiology.org/content/298/2/E193.shorty

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