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Recombinant Human Interleukin-4 (research grade) ( rHuIL-4) Price: 199 Euro/ 50 µgCertificate of Analysis and Data Sheet Description: Recombinant Human IL-4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15000 Dalton. The rHuIL-4 is purified by proprietary chromatographic techniques.
Source: Escherichia Coli.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation & packaging: Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Solubility: The lyophilized rHuIL-4 is very soluble in water and most aqueous buffers below and above the isoelectric point.
Stability: Lyophilized rHuIL-4 although stable at room temperature, should be stored desiccated below 0°C. Reconstituted rHuIL-4 is best stored refrigerated at 4°C.
Purity: Greater than 99.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained.
Amino Acid Composition: In total agreement with the expected amino acid composition of native human IL-4.
Amino acid sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Met-His-Lys-Cys-Asp, conforming to the sequence of native human IL-4.
Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
Biological Activity: ProSpec’s rHuIL-4 is fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 13 x106 IU/mg.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rHuIL-4.
Protein content: Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm. 2. Analysis by RP-HPLC, using a calibrated solution of IL-4 as a Reference Standard.
Usage: This material is offered by Gentaur BVBA for research applications.
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