IL 8 Human (1-72)

Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)
Cat. No.
BT14990
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.
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
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.
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Description

Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton.
The IL-8 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-8 (IL-8), also known as Neutrophil Chemotactic Factor, is a chemokine secreted by various cell types, including macrophages, epithelial cells, and endothelial cells. Its primary function is to attract neutrophils, a type of white blood cell, to the site of inflammation. This process is initiated when macrophages, the first responders to an antigen, engulf and process it, releasing chemokines like IL-8 to signal other immune cells. Endothelial cells store IL-8 in their Weibel-Palade bodies, specialized storage vesicles.
Description
Recombinant Human Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 72 amino acids. With a molecular mass of 8452 Daltons, this purified protein is obtained through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder
Formulation
The Interleukin-8 is provided as a lyophilized powder, prepared from a concentrated (1mg/ml) solution in water without any additives.
Solubility
To reconstitute the lyophilized Interleukin-8, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-8 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store the desiccated product below -18°C. After reconstitution, CXCL8 should be stored at 4°C for 2-7 days. For extended storage, add a carrier protein (0.1% HSA or BSA) and store below -18°C. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 98.0%, as determined by: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Biological Activity
The specific activity of IL8 is determined through its chemotactic effect on donor PBL neutrophils. The threshold concentration for this activity ranges from 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000IU/mg.
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.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.

Product Science Overview

Introduction

Interleukin-8 (IL-8), also known as CXCL8, is a pro-inflammatory cytokine belonging to the CXC chemokine family. It plays a crucial role in the immune response by acting as a chemoattractant for neutrophils and other immune cells. The recombinant form of IL-8, specifically the 1-72 amino acid (a.a.) variant, is widely used in research to study its biological functions and potential therapeutic applications.

Structure and Function

IL-8 is a small protein composed of 72 amino acids with a molecular weight of approximately 8.4 kDa . It contains a characteristic ELR motif (Glu-Leu-Arg) at its N-terminus, which is essential for its interaction with the CXCR1 and CXCR2 receptors on target cells . These interactions trigger a cascade of intracellular signaling events that lead to the activation and migration of neutrophils to sites of inflammation .

Biological Role

IL-8 is primarily produced by macrophages, endothelial cells, and other cell types in response to inflammatory stimuli . It is stored in specialized vesicles called Weibel-Palade bodies within endothelial cells and is rapidly released upon activation . The main functions of IL-8 include:

  • Chemoattraction: IL-8 acts as a potent chemoattractant for neutrophils, guiding them to sites of infection or injury .
  • Angiogenesis: IL-8 promotes the formation of new blood vessels, which is essential for tissue repair and regeneration .
  • Immune Modulation: IL-8 modulates the activity of various immune cells, enhancing the overall immune response .
Clinical Significance

IL-8 has been implicated in various pathological conditions, including chronic inflammatory diseases, cancer, and infectious diseases . Elevated levels of IL-8 are often observed in patients with conditions such as rheumatoid arthritis, chronic obstructive pulmonary disease (COPD), and certain types of cancer . As a result, IL-8 is considered a potential biomarker for these diseases and a target for therapeutic intervention.

Recombinant IL-8

Recombinant IL-8 (1-72 a.a.) is produced using recombinant DNA technology, typically in Escherichia coli (E. coli) expression systems . The recombinant protein is purified to high levels of purity (≥ 98%) and is free from endotoxins, making it suitable for various research applications . It is commonly used in bioassays to study its chemoattractant properties and to investigate its role in disease pathogenesis .

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