IL18BP Human, Sf9

Interleukin-18 Binding Protein Human Recombinant, Sf9
Cat. No.
BT10483
Source
Sf9, Baculovirus cells.
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec'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

IL18BP Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 406 amino acids (31-194a.a) and having a molecular mass of 44.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). 
IL18BP is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-18 Binding Protein (IL18BP) is a naturally occurring protein that blocks the activity of interleukin-18 (IL-18), a pro-inflammatory cytokine. By binding to IL-18, IL18BP prevents it from interacting with its receptor, thereby inhibiting the cascade of events that lead to inflammation. This regulatory mechanism is crucial in maintaining immune homeostasis and preventing excessive inflammation. IL18BP is produced by various immune cells, including monocytes, and its presence is elevated in certain inflammatory conditions like Crohn's disease, highlighting its role in modulating immune responses in the gut.
Description
This product consists of the recombinant human IL18BP protein, expressed in Sf9 insect cells using a baculovirus system. It is a single polypeptide chain, devoid of any glycosylation, encompassing amino acids 31 to 194 of the IL18BP sequence, followed by a 239 amino acid hIgG-His-tag at the C-terminus. This results in a protein with a molecular weight of 44.9 kDa, which may appear between 40-57 kDa on SDS-PAGE due to the tag. The protein has been purified to a high degree using proprietary chromatographic techniques, ensuring its suitability for research applications.
Physical Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.
Formulation
The IL18BP protein is supplied in a solution containing 0.5 mg/ml of the protein in a buffer consisting of Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage to maintain protein stability. Repeated freezing and thawing of the product should be avoided to prevent degradation.
Purity
The purity of the IL18BP protein is greater than 90%, as assessed by SDS-PAGE analysis.
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADPTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQGLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

Product Science Overview

Introduction

Interleukin-18 Binding Protein (IL-18BP) is a naturally occurring inhibitor of the proinflammatory cytokine Interleukin-18 (IL-18). IL-18 is involved in the host’s inflammatory response to infections or injuries and plays a crucial role in regulating both innate and adaptive immune responses . IL-18BP binds to IL-18 with high affinity, effectively neutralizing its activity and inhibiting the inflammatory signaling pathways induced by IL-18 .

Discovery and Structure

IL-18BP was first identified in 1999 as a protein factor that specifically binds to IL-18, antagonizing its biological function . It is a glycoprotein belonging to the immunoglobulin superfamily and is expressed in various tissues and cells in both humans and animals . The human recombinant form of IL-18BP, produced in Sf9 Baculovirus cells, is a single, non-glycosylated polypeptide chain containing 406 amino acids and has a molecular mass of approximately 44.9 kDa .

Biological Function

IL-18BP serves as a natural antagonist of IL-18 by binding to it and preventing its interaction with its receptor. This inhibition results in reduced production of interferon-gamma (IFN-γ) and a decrease in T-helper type 1 immune responses . The protein is constitutively expressed and secreted in mononuclear cells, and elevated levels of IL-18BP have been detected in the intestinal tissues of patients with Crohn’s disease .

Production and Purification

The recombinant IL-18BP (Human, Sf9) is produced using Sf9 Baculovirus cells. The protein is purified through proprietary chromatographic techniques to achieve a purity greater than 90% as determined by SDS-PAGE . The recombinant protein is formulated as a sterile filtered colorless solution containing phosphate-buffered saline (pH 7.4) and 10% glycerol .

Applications and Therapeutic Potential

IL-18BP has significant therapeutic potential due to its ability to inhibit IL-18-induced inflammatory responses. It has been studied for its role in treating various chronic diseases, such as adult-onset Still’s disease and Crohn’s disease . By neutralizing IL-18, IL-18BP can help modulate the progression of these diseases and reduce inflammation .

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