IL 8 Porcine

Interleukin-8 (1-72 a.a) Porcine Recombinant (CXCL8)
Cat. No.
BT15346
Source
Escherichia Coli.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

Interleukin-8 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 9.1kDa.
The IL8 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-8 (IL-8), also called Neutrophil Chemotactic Factor, is a signaling protein primarily known for its role in attracting neutrophils, a type of white blood cell, to the site of inflammation. Produced by a variety of cells including macrophages, epithelial cells, and endothelial cells, IL-8 is a key player in the body's immune response.
Description
This recombinant porcine Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 78 amino acids. With a molecular weight of 9.1kDa, it is purified using proprietary chromatographic techniques to ensure high quality.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered for purity.
Formulation
Lyophilized from a concentrated (0.2µm filtered) solution of 1xPBS with a pH of 7.4.
Solubility
To reconstitute the lyophilized Interleukin-8, it is recommended to dissolve it in sterile 18M-cm H2O at a concentration not less than 100µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-8, while stable at room temperature for up to 3 weeks, should ideally be stored desiccated at a temperature below -18°C. Once reconstituted, CXCL8 should be stored at 4°C for a period of 2-7 days. For long-term storage, adding a carrier protein like 0.1% HSA or BSA is recommended. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeding 95.0% as determined by two methods: (a) Analysis by RP-HPLC (Reverse-Phase High-Performance Liquid Chromatography) and (b) Analysis by SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis).
Biological Activity
Biological activity, determined by a chemotaxis bioassay using human peripheral blood neutrophils, falls within a concentration range of 20-200 ng/ml.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
Source
Escherichia Coli.
Amino Acid Sequence
ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.

Product Science Overview

Introduction

Interleukin-8 (IL-8), also known as CXCL8, is a pro-inflammatory chemokine that plays a crucial role in the immune response by attracting neutrophils to sites of infection or inflammation. The porcine recombinant form of IL-8, specifically the 1-72 amino acid sequence, is a non-glycosylated polypeptide produced in Escherichia coli (E. coli) expression systems. This recombinant protein is used extensively in research to study immune responses and inflammatory processes in porcine models.

Structure and Function

IL-8 belongs to the CXC chemokine family and is characterized by its 72 amino acid sequence. It functions primarily as a chemoattractant, guiding neutrophils to sites of infection or injury. Additionally, IL-8 is a potent angiogenic factor, promoting the formation of new blood vessels. The protein binds to cell surface receptors IL-8RA and IL-8RB, initiating a cascade of intracellular signaling that results in the activation and migration of neutrophils .

Preparation Methods

The recombinant form of IL-8 (1-72 a.a) is typically produced using E. coli expression systems. The gene encoding the IL-8 protein is inserted into a plasmid vector, which is then introduced into E. coli cells. These cells are cultured under conditions that promote the expression of the IL-8 protein. After sufficient growth, the cells are lysed, and the protein is purified using techniques such as affinity chromatography and high-performance liquid chromatography (HPLC). The resulting product is a highly pure, lyophilized protein that can be reconstituted for experimental use .

Applications in Research

Porcine recombinant IL-8 is widely used in immunological research to study the mechanisms of inflammation and immune cell recruitment. It is particularly valuable in porcine models of disease, which are often used as analogs for human conditions due to their physiological similarities. Researchers utilize IL-8 to investigate its role in various inflammatory diseases, including autoimmune disorders and cancer. Additionally, IL-8 is used in bioassays to evaluate the chemotactic response of neutrophils and other immune cells .

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