IL 11 Human

Interleukin-11 Human Recombinant
Cat. No.
BT30303
Source
Escherichia Coli.
Synonyms

AGIF, Adipogenesis inhibitory factor, IL-11.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek'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.
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Description

Interleukin-11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19256.29 Dalton.
The IL-11 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin 11 (IL-11) belongs to a family of cytokines that share a common signaling pathway through the gp130 receptor subunit. These cytokines play crucial roles in various cellular processes, including immune response, hematopoiesis, and tissue repair. IL-11, in particular, contributes to the development of antibody-producing B cells and supports the growth and differentiation of blood stem cells and megakaryocyte progenitors, which are responsible for platelet production.
Description
This product consists of the recombinant form of human Interleukin-11, produced in E. coli. It is a single polypeptide chain without any glycosylation modifications, comprising 179 amino acids and exhibiting a molecular weight of 19256.29 Daltons. The purification of IL-11 is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein was freeze-dried from a solution with a concentration of 1mg/ml, containing no additional substances.
Solubility
To reconstitute the lyophilized Interleukin-11, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. Subsequently, the reconstituted solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Interleukin-11 demonstrates stability at room temperature for a period of 3 weeks. However, for long-term storage, it is recommended to store it in a desiccated state below -18°C. Once reconstituted, IL11 can be stored at 4°C for 2-7 days. For extended storage, freezing at -18°C is recommended, but freeze-thaw cycles should be avoided. To enhance long-term stability during storage, the addition of a carrier protein like HSA or BSA (0.1%) is suggested.
Purity
The purity of this product exceeds 98.0%, as determined by two independent analytical methods: Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Biological Activity
The biological activity of this product was assessed by its ability to stimulate the proliferation of murine 7TD1 cells. The half-maximal effective concentration (ED50) for this stimulation was determined to be less than 10ng/ml. This corresponds to a specific activity of 100,000 international units per milligram (IU/mg).
Protein Content
The protein content of this product was quantified using two independent methods. The first method involved measuring the absorbance of a 0.1% (1mg/ml) solution at 280 nm using UV spectroscopy. An extinction coefficient of 0.95, calculated by the PC GENE computer program (IntelliGenetics), was used for this determination. The second method utilized RP-HPLC, employing a calibrated solution of IL-11 as a reference standard.
Synonyms

AGIF, Adipogenesis inhibitory factor, IL-11.

Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.

Product Science Overview

Biological Functions

IL-11 has multiple effects on both hematopoietic and non-hematopoietic cells. Many of the biological effects described for IL-11 overlap with those for IL-6. In vitro, IL-11 can synergize with IL-3, IL-4, and stem cell factor (SCF) to shorten the G0 period of early hematopoietic progenitors . It also enhances IL-3-dependent megakaryocyte colony formation and stimulates the T cell-dependent development of specific immunoglobulin-secreting B cells .

Gene and Protein Structure

The human IL-11 gene, consisting of 5 exons and 4 introns, is located on chromosome 19 and encodes a 23 kDa protein . IL-11 is a member of the IL-6-type cytokine family, distinguished based on their use of the common co-receptor gp130. Signal specificity is provided by the IL-11Rα subunit, which is expressed at high levels in fibroblasts and other stromal cells but not immune cells .

Recombinant Human IL-11

Recombinant human IL-11 (rhIL-11) was developed as the drug substance oprelvekin. It has been shown to have potent thrombopoietic activity in vivo and has been used therapeutically to ameliorate chemotherapy-induced thrombocytopenia . Recombinant human IL-11 is typically expressed in Chinese Hamster Ovary (CHO) cells or Escherichia coli and is supplied in a lyophilized form .

Applications and Research

IL-11 has been found to stimulate cell proliferation of T11 cells and has been used in various research applications to study its effects on hematopoietic progenitors, megakaryocyte colony formation, and immunoglobulin-secreting B cells . It is also being explored for its potential therapeutic applications in treating various conditions related to the hematopoietic and immune systems .

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