NAP 2 Human
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
The NAP-2 is purified by proprietary chromatographic techniques.
Product Specs
(a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Product Science Overview
NAP-2 is derived from a larger precursor protein known as platelet basic protein (PBP). The mature form of NAP-2 is a 70 amino acid polypeptide with a molecular weight of approximately 7.6 kDa . It contains four highly conserved cysteine residues, which are characteristic of CXC chemokines, and an “ELR” motif that is crucial for its interaction with the CXCR1 and CXCR2 receptors .
NAP-2 plays a significant role in the recruitment and activation of neutrophils. It acts as a potent chemoattractant, guiding neutrophils to sites of inflammation or injury. Upon binding to its receptors, CXCR1 and CXCR2, NAP-2 triggers a cascade of intracellular signaling events that lead to neutrophil degranulation and the release of inflammatory mediators and degradative enzymes .
In addition to its role in neutrophil activation, NAP-2 is involved in several other cellular processes:
- Mitosis: NAP-2 stimulates cell division, contributing to tissue repair and regeneration.
- Extracellular Matrix Production: It promotes the synthesis of extracellular matrix components, which are essential for tissue structure and function.
- Angiogenesis: NAP-2 induces endothelial cell proliferation and chemotaxis, facilitating the formation of new blood vessels .
NAP-2’s involvement in angiogenesis makes it a critical player in tumor growth and metastasis. By promoting the formation of new blood vessels, NAP-2 provides a pathway for cancer cells to enter the circulation and spread to other parts of the body . This angiogenic role is distinct from its function in neutrophil chemoattraction and activation, highlighting its multifaceted nature.
Studies have shown that NAP-2 is upregulated in various cancer types, and its interaction with CXCR2 is associated with tumor progression and poor prognosis . As a result, NAP-2 is being explored as a potential target for cancer therapy, with the aim of inhibiting its angiogenic and mitotic activities to suppress tumor growth and metastasis .
Recombinant human NAP-2 is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically purified to high levels of purity (≥98%) and is used in various research applications, including cell culture studies and functional assays . The availability of recombinant NAP-2 allows researchers to investigate its biological functions and therapeutic potential in a controlled laboratory setting.
