Recombinant Human Insulin (INS)

Z101065250 mg


DescriptionAs secreted heterodimeric peptide hormone produced by the pancreas, Insulin is central to regulating the metabolism of carbohydrates and fat in the body. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids and accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Growth Factor Size250 mg
Unit quantity250 mg
FamilyIGF/Insulin Family


Gene SymbolINS
Gene ID3630
Accession NumberP01308
SourceE. coli
SpeciesHuman (H. sapiens)
AppearanceLyophilized Powder
Molecular Weight6.0 kDa
Endotoxin Level<1.0 EU/μg of recombinant protein as determined by the LAL method
Expression SystemE.coli
Purity>95% as determined by SDS-PAGE
FormulationLyophilized from a 0.2 μm filtered solution with no additives

A quick spin of the vial followed by reconstitution in distilled water. To increase solubility, a few drops of acetic acid can be added to reduce the pH; solubilize at 1-2 mg/ml in dilute acetic or HCl, pH 2–3. This solution can then be diluted into other buffers to a concentration not less than 0.1 mg/mL.

StorageThe lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
UsageFor research use only. Not for diagnostic or therapeutic use.

How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970. · Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL). · For recombinant proteins: EU is reported per microgram of protein. · One EU = 0.1-0.2 ng endotoxin/µg of protein. · At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.

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