IL 1RA Mouse

Interleukin-1 Receptor Antagonist Mouse Recombinant
Cat. No.
BT1156
Source
Escherichia Coli.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel Filtration.
(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.
Shipped with Ice Packs
In Stock

Description

IL1 ra Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.4kDa.
The IL1ra is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-1 receptor antagonist (IL-1ra) is a protein that regulates inflammation by blocking the activity of interleukin-1 (IL-1) cytokines. IL-1ra is part of the IL-1 cytokine family and plays a crucial role in maintaining immune balance. It achieves this by binding to IL-1 receptors, preventing the binding and signaling of IL-1α and IL-1β. This inhibitory action modulates various immune and inflammatory responses associated with IL-1, such as fever, inflammation, and tissue damage. The gene encoding IL-1ra is located on chromosome 2 in humans, clustered with five other related cytokine genes. Variations in this gene have been linked to an increased susceptibility to conditions like osteoporosis and gastric cancer. Furthermore, four different isoforms of IL-1ra, resulting from alternative splicing of the IL-1ra gene transcript, have been identified.
Description
Recombinant Mouse Interleukin-1ra, expressed in E. coli, is a purified protein with a molecular weight of 17.4 kDa. It exists as a single, non-glycosylated polypeptide chain consisting of 153 amino acids. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
White, lyophilized (freeze-dried) powder that has been sterilized by filtration.
Formulation
The protein was lyophilized from a solution containing a high concentration (1 mg/ml) of Interleukin-1ra in water with sodium bicarbonate (NaHCO3).
Solubility
To reconstitute the lyophilized Interleukin-1ra, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-1ra remains stable at room temperature for up to 3 weeks; however, it is recommended to store it in a dry environment below -18°C for extended periods. After reconstitution, IL-1ra should be stored at 4°C for no more than 2-7 days. For long-term storage, freezing below -18°C is recommended. To preserve its stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Minimize freeze-thaw cycles to prevent protein degradation.
Purity
The purity of Interleukin-1ra is greater than 98.0%, as determined by two methods: (a) Gel Filtration analysis and (b) SDS-PAGE analysis.
Biological Activity
Mouse IL-1Ra effectively inhibits IL-1-alpha activity in the helper T cell line D10.G4.1, confirming its biological functionality.
Protein Content
Protein concentration was accurately determined using two independent methods: (1) UV spectroscopy at 280 nm, utilizing an extinction coefficient of 0.91 for a 0.1% (1 mg/ml) solution, calculated using the PC GENE computer analysis program (IntelliGenetics); (2) Reverse-phase high-performance liquid chromatography (RP-HPLC), employing a known concentration of IL-1ra as a reference standard.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.

Product Science Overview

Introduction

Interleukin-1 Receptor Antagonist (IL-1Ra) is a naturally occurring protein that plays a crucial role in regulating the immune response. It is part of the interleukin-1 (IL-1) family of cytokines, which are involved in the initiation and regulation of inflammatory responses. The recombinant form of IL-1Ra, specifically derived from mice, has been extensively studied for its therapeutic potential in various inflammatory diseases.

Discovery and Development

IL-1Ra was first discovered in 1984 in the urine and serum of patients with leukemia and in the supernatant of cultured monocytes . The protein was named for its ability to competitively bind to the IL-1 receptor, thereby antagonizing the function of IL-1, a potent pro-inflammatory cytokine.

The recombinant form of IL-1Ra, known as anakinra or Kineret™, was developed to mimic the natural antagonist. This recombinant protein differs from the native IL-1Ra by the addition of an N-terminal methionine . It binds to the IL-1 receptor type I with the same affinity as IL-1β, effectively inhibiting its pro-inflammatory effects.

Mechanism of Action

IL-1Ra functions by binding to the IL-1 receptor without eliciting a signal, thereby blocking the binding of IL-1α and IL-1β. This competitive inhibition prevents the downstream signaling that leads to inflammation and tissue damage. By modulating the IL-1 signaling pathway, IL-1Ra helps to control excessive inflammatory responses that can lead to chronic inflammatory diseases .

Therapeutic Applications

Recombinant IL-1Ra has been investigated for its potential in treating various inflammatory conditions. One of the most well-studied applications is in the treatment of rheumatoid arthritis (RA). Clinical trials have demonstrated that anakinra, in combination with methotrexate, significantly reduces the signs and symptoms of RA in patients who have inadequate responses to methotrexate alone . The treatment is generally well-tolerated, with the most common side effect being mild to moderate injection site reactions.

In addition to RA, IL-1Ra has shown promise in treating other inflammatory diseases, including psoriasis, atopic dermatitis, and other skin disorders . Its ability to modulate the immune response makes it a valuable therapeutic agent in conditions where excessive inflammation is a key pathological feature.

Research and Future Directions

Ongoing research continues to explore the potential of IL-1Ra in various disease contexts. Studies are investigating its role in other autoimmune and inflammatory diseases, as well as its potential in combination therapies. The development of new delivery methods and formulations aims to improve the efficacy and patient compliance of IL-1Ra treatments.

In conclusion, the recombinant form of Interleukin-1 Receptor Antagonist (Mouse) represents a significant advancement in the treatment of inflammatory diseases. Its ability to effectively inhibit IL-1 signaling and modulate the immune response holds great promise for future therapeutic applications.

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