Human S100A9 Recombinant Protein (RPES3295)

Human S100A9 Recombinant Protein

The S100 protein is a family of low-molecular-weight proteins with two EF-hand calcium binding regions that may be found in vertebrates. There are at least 21 distinct S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. The vast majority of S100 proteins are homodimers that are linked through disulfide bonds, and they may be found in cells from the neural crest, chondrocytes, macrophages, dendritic cells, and so on. S100 proteins have been linked to a wide range of intracellular and extracellular. They control protein phosphorylation, transcription factors, cytoskeletal element dynamics, enzyme activities, cell growth and maturation, and the inflammatory response. S100-A9, also known as S100 calcium-binding protein A9, S100A9, and CAGB, is a member of the S-100 family. Macrophages make the enzyme S100A9 in acute inflammation and persistent inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein with anti-microbial activity against bacteria and fungi. Zinc ions counteract the anti-microbial and proapoptotic action of S100A9. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when it is unphosphorylated. It also promotes phagocyte migration and granulocyte infiltration at wounds. S100A9 is a pro-inflammatory cytokine in acute and chronic inflammation, which upregulates the release of IL8 and cell-surface expression of ICAM1. Human S100A9 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.