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100ug
AntibodySystem
Recombinant Proteins
Recombinant Mouse S100A8 protein, also known as calgranulin A, is a member of the S100 family of calcium-binding proteins. It is encoded by the S100a8 gene and is found in various tissues, including neutrophils, monocytes, and macrophages. This protein plays a crucial role in the innate immune response and has been extensively studied for its structure, activity, and potential applications.
Recombinant Mouse S100A8 protein is a small, acidic protein with a molecular weight of approximately 10.8 kDa. It is composed of 93 amino acids and has a highly conserved EF-hand calcium-binding motif, which is characteristic of the S100 family. This motif consists of two alpha-helices connected by a loop region that binds to calcium ions, allowing for the regulation of protein activity.
The crystal structure of recombinant Mouse S100A8 protein has been determined, revealing a dimeric structure with each monomer containing two EF-hand motifs. The dimerization of S100A8 is essential for its biological activity and is facilitated by the binding of calcium ions. The dimeric structure also allows for the formation of heterodimers with S100A9, another member of the S100 family, which further enhances the protein’s function.
Recombinant Mouse S100A8 protein has been shown to have multiple activities, including calcium binding, cytokine-like activity, and antimicrobial properties. As a calcium-binding protein, S100A8 regulates the intracellular calcium concentration, which is crucial for various cellular processes such as cell proliferation, differentiation, and apoptosis.
Furthermore, recombinant Mouse S100A8 protein has been found to have cytokine-like activity, acting as a chemoattractant for neutrophils and monocytes. It also induces the production of pro-inflammatory cytokines, such as interleukin-1 beta and tumor necrosis factor-alpha, by activating the NF-kB signaling pathway. This activity is essential for the recruitment and activation of immune cells in response to infection or injury.
In addition, recombinant Mouse S100A8 protein has been shown to have antimicrobial properties, particularly against Gram-positive bacteria. It achieves this by binding to bacterial cell wall components, disrupting the integrity of the cell membrane and leading to bacterial death. This antimicrobial activity makes S100A8 an essential component of the innate immune response against bacterial infections.
Due to its diverse activities, recombinant Mouse S100A8 protein has potential applications in various fields, including immunology, inflammation, and cancer research. It has been used as an antigen in studies investigating the role of S100A8 in autoimmune diseases, such as rheumatoid arthritis and psoriasis. In these studies, recombinant Mouse S100A8 protein has been shown to stimulate the production of autoantibodies and contribute to the pathogenesis of these diseases.
Moreover, recombinant Mouse S100A8 protein has been used as a biomarker for inflammation and infection. Its increased expression has been observed in various inflammatory diseases, and it has been proposed as a potential diagnostic and prognostic marker for these conditions.
In cancer research, recombinant Mouse S100A8 protein has been studied for its role in tumor growth and metastasis. It has been shown to promote the proliferation and migration of cancer cells, making it a potential target for cancer therapy.
In summary, recombinant Mouse S100A8 protein is a small, calcium-binding protein with diverse activities in the innate immune response. Its structure, activity, and potential applications have been extensively studied, and it has been shown to play a crucial role in various physiological and pathological processes. Further research on this protein may lead to the development of novel diagnostic and therapeutic strategies for various diseases.
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