GRO a Human
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
The GRO-alpha is purified by proprietary chromatographic techniques.
Product Specs
The product is lyophilized from a 0.2 µm filtered concentrated solution (1 mg/ml) in 20 mM phosphate buffer (PB), with a pH of 7.4 and 50 mM NaCl.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
The biological activity is evaluated based on the ability to chemoattract human peripheral blood neutrophils within a concentration range of 10.0-100.0 ng/ml.
Product Science Overview
GRO-Alpha, also known as CXCL1, is a member of the CXC chemokine family. It is a proinflammatory chemokine that plays a crucial role in the immune response by mediating the migration and activation of neutrophils. The protein is also referred to as Growth-regulated oncogene-alpha (GRO-Alpha), Keratinocyte-derived chemokine (KC), and Cytokine-induced neutrophil chemoattractant-1 (CINC-1) .
CXCL1 is an approximately 8 kDa protein that shares significant sequence identity with its mouse and rat counterparts. The mature form of human CXCL1 consists of 72 amino acids and is characterized by the presence of an ELR motif (Glu-Leu-Arg) at its N-terminus, which is critical for its interaction with CXC chemokine receptors, particularly CXCR2 .
CXCL1 is primarily involved in the recruitment and activation of neutrophils during inflammatory responses. It is produced by various cell types, including macrophages, neutrophils, and epithelial cells, in response to proinflammatory stimuli such as interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-α). The binding of CXCL1 to its receptor CXCR2 triggers a cascade of intracellular signaling events that result in the directed migration of neutrophils to sites of infection or injury .
The expression of CXCL1 is upregulated in several pathological conditions, including cancer, where it has been implicated in tumor progression and metastasis. High levels of CXCL1 have been observed in various types of human cancers, such as uterine cervical cancer, where it facilitates tumor cell malignant processes through autocrine and paracrine mechanisms . Additionally, CXCL1 has been linked to poor clinical outcomes and advanced stages of cancer .
Recombinant human CXCL1 is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically purified to high levels of purity (>97%) and is available in both carrier-free and carrier-containing formulations. The carrier protein, often bovine serum albumin (BSA), enhances the stability and shelf-life of the recombinant protein .
Recombinant CXCL1 is widely used in research to study its role in inflammation, cancer, and other diseases. It is also utilized in various assays to investigate the chemotactic activity of neutrophils and other immune cells. The protein’s ability to induce myeloperoxidase release from neutrophils and chemoattract BaF3 mouse pro-B cells transfected with human CXCR2 are some of the key functional assays performed using recombinant CXCL1 .
