IL 8 Human (1-77)
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)
Cat. No.
BT15090
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 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(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 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton.
The IL-8 is purified by proprietary chromatographic techniques.
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 cells, including macrophages, epithelial cells, and endothelial cells. It plays a crucial role in the immune response by attracting neutrophils, a type of white blood cell, to the site of inflammation. 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.
Description
Recombinant Human Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 77 amino acids. With a molecular weight of 8904 Daltons, this purified protein is obtained through proprietary chromatographic techniques.
Physical Appearance
White, sterile-filtered, lyophilized powder.
Formulation
Lyophilized from a 0.2µm filtered solution at a concentration of 1mg/ml in PBS, pH 7.4.
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. The reconstituted solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Interleukin-8 remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated at a temperature below -18°C. Upon reconstitution, CXCL8 should be stored at 4°C for a period of 2-7 days. For long-term storage, freezing at -18°C is advised. To enhance stability during long-term storage, consider adding a carrier protein such as 0.1% HSA or BSA. Minimize freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using the following 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
The biological activity is assessed by evaluating its chemoattractant properties on human peripheral blood neutrophils within a concentration range of 25-150 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.
Source
Escherichia Coli.
Amino Acid Sequence
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD
GRELCLDPKE NWVQRVVEKF LKRAENS.
Product Science Overview
Structure and Function
IL-8 is a small protein with a molecular weight of approximately 8.9 kDa and consists of 77 amino acids . It contains the ELR-motif (N-terminal Glu-Leu-Arg amino acid sequence), which is critical for its interaction with its receptors, CXCR1 and CXCR2 . These receptors are found on the surface of various immune cells, including neutrophils, and mediate the chemotactic and activating effects of IL-8 .
Biological Role
IL-8 is secreted by several cell types, including macrophages, endothelial cells, and epithelial cells, in response to inflammatory stimuli . Its primary functions include:
- Chemoattraction: IL-8 attracts neutrophils to the site of infection or injury, facilitating the immune response .
- Activation: It activates neutrophils, enhancing their ability to phagocytose (engulf and digest) pathogens .
- Angiogenesis: IL-8 promotes the formation of new blood vessels, a process known as angiogenesis, which is essential for wound healing and tissue repair .
Clinical Significance
IL-8 has been implicated in various diseases and conditions due to its role in inflammation and immune response. Some of the key areas of research and clinical interest include:
- Cancer: IL-8 is involved in tumor growth and metastasis by promoting angiogenesis and recruiting immune cells to the tumor microenvironment .
- Chronic Inflammatory Diseases: Elevated levels of IL-8 are associated with chronic inflammatory conditions such as rheumatoid arthritis, inflammatory bowel disease, and chronic obstructive pulmonary disease (COPD) .
- Infectious Diseases: IL-8 plays a role in the immune response to bacterial and viral infections, making it a potential target for therapeutic interventions .
Recombinant IL-8 (1-77 a.a)
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