Human Interleukin-5 (Recombinant)

Recombinant Human Interleukin-5 (IL-5)

Source: E.Coli

Background: Interleukin-5 (IL5), also known as eosinophil differentiation factor (EDF), is a lineage-specific cytokine for eosinophilpoiesis [1, 2]. It regulates eosinophil growth and activation [1], and thus plays an important role in diseases associated with increased levels of eosinophils, including asthma. IL5 has a similar overall fold to other cytokines (e.g., IL2, IL4 and GCSF), but while these exist as monomeric structures, IL5 is a homodimer. The fold contains an anti-parallel 4-alpha-helix bundle with a left handed twist, connected by a 2-stranded anti-parallel beta-sheet . The monomers are held together by 2 interchain disulphide bonds.

Description: Recombinant Human IL-5 produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 26522.84 Dalton. The rHuIL-5 is purified by proprietary chromatographic techniques.

Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation: The protein was lyophilized from a concentrated (1mg/ml) sterile solution with no additives.

Solubility: It is recommended to reconstitute the lyophilized rHuIL-5 in sterile 18M?-cm H2O not less than 100 g/ml, which can then be further diluted to other aqueous solutions.

Stability: Lyophilized rHuIL-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution rHuIL-5 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 avoid freeze-thaw cycles.

Purity: Greater than 98.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

Amino acid sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ile-Pro-Thr-Glu.

Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Biological Activity: rHuIL-5 is fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be less then 0.15ng/ml, corresponding to a Specific Activity of 6 x 10 IU/m

Endotoxin: Less than 0.1 ng/ g (IEU/ g) of rHuIL-5.

Protein content: Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.625 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-5 as a Reference Standard.

Usage: BioWORLD's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.