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Human Interleukin-11 Recombinant

Selected Variant

90176-B

Size: 10 µg

Recombinant IL-11 is a disulfide-linked monomer protein consisting of 180 amino acid residues, and migrates as an approximately 19 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Interleukin-11 mature chain was expressed inE. coli.

Product Specifications

Background

IL-11 is secreted by bone marrow stromal cells (fibroblasts) and is produced also by a number of mesenchymal cells. The IL-11 receptor (alpha chain) utilizes gp130 as its signal transducer, which is also a component of other cytokine receptors. The alpha chain of the IL-11 receptor has been identified independently as Etl2. IL-11 promotes primary and secondary immune responsesin vitroandin vivoand modulates antigen-specific antibody reactions. IL-11 promotes the proliferation of IL-6 dependent plasmacytoma cell lines in the presence of neutralizing IL-6 antibodies. IL-11 also stimulates the T-cell dependent development of IgG-secreting B-cells in spleen cell cultures. IL-11 inhibits the differentiation of pre- adipocytes. It induces the synthesis of some acute phase proteins by hepatocytes.

UniProt

P20809

Endotoxin

Endotoxin level was found to be < 0.1 ng/µg (1 EU/µg), using the LAL gel clot method.

Purity

≥ 97% by SDS-PAGE and HPLC

Format

Lyophilized protein

Reconstitution

A quick spin of the vial followed by reconstitution in distilled water to concentration not less than 0.1 mg/ml. This can then be diluted into other buffers.

Shipping Conditions

Gel Packs or Dry Ice

Storage Conditions

The lyophilized protein is stable for at least 2 years from date of receipt when stored at -20°C. Upon reconstitution, store in working aliquots at +4°C for up to one month, or at -20°C for up to six months, in the presence of a carrier protein. Avoid repeated freeze/thaw cycles.

Calculated Molecular Weight

19 kDa

Formulation

Lyophilized from 0.2 µm filtered phosphate buffered solution in 2.5% glycine, pH 4.5.

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