IL 8 Human, Pichia
Description
The IL-8 is purified by proprietary chromatographic techniques.
Product Specs
This Interleukin-8 exhibits potent chemotactic activity, as evidenced by its ability to induce chemotaxis in human neutrophils at a concentration of 25ng/ml. This confirms its biological functionality in attracting neutrophils.
Product Science Overview
Interleukin-8 (IL-8), also known as CXCL8, is a chemokine produced by various cell types, including macrophages, epithelial cells, and endothelial cells. 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 1-77 amino acid sequence, is often produced using the yeast Pichia pastoris expression system.
IL-8 is a member of the CXC chemokine family and is characterized by its ability to bind to the CXCR1 and CXCR2 receptors on the surface of target cells . The protein consists of 77 amino acids and has a molecular weight of approximately 8.9 kDa . It contains the ELR motif (Glu-Leu-Arg) at its N-terminus, which is essential for its interaction with CXCR1 and CXCR2 .
The primary function of IL-8 is to act as a chemoattractant, guiding neutrophils to sites of infection or inflammation . It also has potent angiogenic properties, promoting the formation of new blood vessels, which is crucial in wound healing and tumor growth .
The recombinant production of IL-8 in Pichia pastoris involves the insertion of the human IL-8 gene into the yeast’s genome. Pichia pastoris is a popular expression system due to its ability to perform post-translational modifications and secrete high levels of recombinant protein . The process typically involves the following steps:
- Gene Cloning: The human IL-8 gene is cloned into an expression vector compatible with Pichia pastoris.
- Transformation: The expression vector is introduced into Pichia pastoris cells, which integrate the IL-8 gene into their genome.
- Expression: The transformed yeast cells are cultured under conditions that induce the expression of the IL-8 protein.
- Purification: The recombinant IL-8 protein is purified from the culture medium using techniques such as affinity chromatography and SDS-PAGE .
Recombinant IL-8 has several applications in research and medicine. It is used to study the mechanisms of inflammation and immune response, as well as the role of chemokines in various diseases . Additionally, IL-8 is utilized in cancer research to investigate its role in tumor angiogenesis and metastasis .
