MCP 1 Mouse

Monocyte Chemotactic Protein-1 (MCP-1), also known as CCL2, is a small cytokine belonging to the CC chemokine family. It plays a crucial role in the immune system by recruiting monocytes, memory T cells, and dendritic cells to sites of inflammation caused by tissue injury or infection . MCP-1 is produced by various cell types, including monocytes, macrophages, and dendritic cells .

Recombinant MCP-1 (Mouse) is typically produced using E. coli expression systems. The gene encoding mouse MCP-1 is cloned into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and accumulated within the cells. The cells are then lysed, and the protein is purified using techniques such as affinity chromatography .

The purified protein is lyophilized from a 0.2 μm filtered solution in phosphate-buffered saline (PBS) with or without carrier proteins like bovine serum albumin (BSA). The lyophilized protein can be reconstituted in sterile PBS or other aqueous solutions for use in various applications .

MCP-1 exhibits chemotactic activity, meaning it can attract specific cell types to its location. It primarily attracts monocytes and basophils, but not neutrophils or eosinophils . The chemotactic activity is mediated through its interaction with cell surface receptors, mainly CCR2 and CCR4 .

MCP-1 is a monomeric polypeptide with a molecular weight of approximately 13-15 kDa, depending on its glycosylation status . It is anchored in the plasma membrane of endothelial cells by glycosaminoglycan side chains of proteoglycans . The protein can be cleaved by metalloproteinases, such as MMP-12, which can alter its activity and function .

In the context of bone biology, MCP-1 is expressed by mature osteoclasts and osteoblasts and is regulated by nuclear factor κB (NFκB) . It is found at sites of tooth eruption and bone degradation, indicating its role in bone remodeling processes .