CXCL2 (C-X-C motif chemokine ligand 2), also known as GROβ or MIP-2α, is a small, secreted protein belonging to the CXC chemokine family. It plays a critical role in inflammatory and immune responses by recruiting and activating neutrophils via binding to its receptor CXCR2. Structurally, it consists of approximately 73 amino acids in humans, with a conserved four-cysteine motif forming disulfide bonds essential for its tertiary structure and function. The protein is produced by various cell types, including macrophages, endothelial cells, and fibroblasts, in response to pro-inflammatory stimuli such as TNF-α, IL-1β, or bacterial lipopolysaccharides (LPS).

Recombinant CXCL2 protein is typically produced using expression systems like *E. coli* or mammalian cells, followed by purification steps to ensure high homogeneity and bioactivity. Its production enables researchers to study neutrophil chemotaxis, inflammatory pathways, and tissue repair mechanisms in controlled experimental settings. In disease contexts, CXCL2 is implicated in chronic inflammation, autoimmune disorders, and cancer progression, where excessive neutrophil infiltration can exacerbate tissue damage or promote tumor angiogenesis. For example, elevated CXCL2 levels are observed in conditions like rheumatoid arthritis, atherosclerosis, and certain metastatic cancers.

In research, recombinant CXCL2 is widely used to model inflammatory diseases *in vitro* or *in vivo*, screen anti-inflammatory drugs, or explore its dual role in wound healing versus pathological scarring. Its murine homolog, MIP-2. is often studied in preclinical models to mimic human CXCL2 functions. Despite its pro-inflammatory nature, CXCL2 also exhibits regenerative properties, making it a molecule of interest in balancing therapeutic interventions for inflammation-related disorders. Quality assessments, including SDS-PAGE, endotoxin testing, and functional assays (e.g., neutrophil migration), are critical to validate recombinant CXCL2 for experimental reproducibility.