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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human CD156a/ADAM8 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 23.85 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Arg200-Arg390 |
Aliases /Synonyms | Disintegrin and metalloproteinase domain-containing protein 8, ADAM8, CD156a, MS2, Cell surface antigen MS2, ADAM 8 |
Reference | ARO-P10760 |
Note | For research use only. |
Recombinant proteins have become an essential tool in modern biotechnology and have revolutionized the field of medicine. These proteins are synthesized in a laboratory using recombinant DNA technology, allowing for the production of large quantities of highly pure and specific proteins. One such recombinant protein is the Recombinant Human CD156a/ADAM8 Protein, which has gained significant attention in the scientific community due to its unique structure, diverse activities, and potential applications.
The Recombinant Human CD156a/ADAM8 Protein, also known as disintegrin and metalloproteinase domain-containing protein 8 (ADAM8), is a member of the ADAM family of proteins. It is composed of a signal peptide, a prodomain, a metalloproteinase domain, a disintegrin-like domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic tail. The metalloproteinase domain contains the active site responsible for the proteolytic activity of the protein, while the disintegrin-like domain is involved in cell adhesion and signaling. The cysteine-rich domain and EGF-like domain are important for protein-protein interactions and binding to cell surface receptors.
The Recombinant Human CD156a/ADAM8 Protein is a multifunctional protein with diverse activities. Its main function is as a metalloproteinase, which enables it to cleave and process other proteins. This activity is essential for various physiological processes such as cell migration, tissue remodeling, and wound healing. Additionally, the disintegrin-like domain of the protein allows it to bind to integrins, which are cell surface receptors involved in cell adhesion and migration. This interaction can modulate cell signaling pathways, leading to changes in cell behavior and function. The Recombinant Human CD156a/ADAM8 Protein has also been shown to have anti-inflammatory properties by inhibiting the production of pro-inflammatory cytokines and chemokines. Furthermore, it has been reported to have a role in the immune response by regulating the activation and differentiation of immune cells.
The unique structure and diverse activities of the Recombinant Human CD156a/ADAM8 Protein make it a promising candidate for various applications in the field of biotechnology and medicine. One potential application is in cancer therapy, as the protein has been found to be overexpressed in various types of cancer cells and has been linked to tumor growth and metastasis. Inhibiting the activity of the protein could potentially slow down or prevent cancer progression. Additionally, the anti-inflammatory properties of the protein make it a potential therapeutic target for inflammatory diseases such as asthma and arthritis. The Recombinant Human CD156a/ADAM8 Protein has also been studied for its role in neurodegenerative diseases, as it has been found to be involved in the processing of amyloid precursor protein, which is associated with Alzheimer’s disease.
The Recombinant Human CD156a/ADAM8 Protein is a multifunctional protein with a complex structure and diverse activities. Its role in various physiological processes and potential applications in biotechnology and medicine make it a valuable protein for scientific research. Further studies on the structure and function of this protein could lead to new insights and potential therapeutic strategies for various diseases.
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