IL 1 beta Recombinant eiwit

Source : Escherichia Coli. Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1b is purified by proprietary chromatographic techniques. Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

Catabolin||Lymphocyte-activating factor (LAF) ||Endogenous Pyrogen (EP) ||Leukocyte Endogenous Mediator (LEM) ||Mononuclear Cell Factor (MCF) ||IL1F2||IL-1 beta.

Greater than 98.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

The protein was lyophilized from a concentrated (1mg/mL) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.

Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b 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.

It is recommended to reconstitute the lyophilized Interleukin-1b in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions. The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.