Enzymes for Research, Diagnostic and Industrial Use
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| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| NATE-1399 | Antarctic Phosphatase from E. coli, Recombinant | E. coli | Inquiry |
Antarctic phosphatase is an enzyme found in extremely cold environments, especially in the Antarctic region. This enzyme has unique properties due to its growth in the cold environment, making it an interesting research topic. Antarctic phosphatase is an alkaline phosphatase that is found in cold environments, especially in the Antarctic region. It is an enzyme commonly used in molecular biology research because of its ability to efficiently dephosphorylate DNA and RNA. The enzyme is characterized by its unique stability at low temperatures and its high affinity for substrates.
Antarctica phosphatase has a four-alpha-helical bundle structure that is stabilized by disulfide bonds. The core of the structure is the active site, which consists of two histidine residues and one lysine residue, forming a catalytic triad. This triad is responsible for the dephosphorylation activity of the enzyme.
Antarctic phosphatase was first discovered in the late 1960s when researchers began investigating the microbial communities found in the Antarctic region. It was not until the mid-1990s that the enzyme was isolated and characterized. Researchers observed that the enzyme exhibited remarkable stability in cold environments and found that it could efficiently dephosphorylate substrates without the need for cofactors.
Antarctic phosphatase is found mainly in the cold polar regions of the world, including Antarctica and the Arctic. It is commonly found in microbial communities associated with sea ice, deep-sea sediments and glaciers. Although this enzyme is found primarily in nature, it can also be produced by recombinant DNA technology, making it widely available for use in research laboratories.
Antarctica phosphatase functions primarily as a dephosphorylase, catalyzing the removal of a phosphate group from nucleic acids and certain proteins. This enzyme is particularly useful in molecular biology research because it can be used to remove phosphate groups from DNA and RNA, making the manipulation of these molecules easier.
Antarctic phosphatase is not normally involved in signal transduction pathways, as its function is mainly limited to the removal of phosphate groups from nucleic acids and proteins. However, its dephosphorylation activity may play a role in certain biochemical pathways, especially those related to nucleic acid metabolism.
Antarctica phosphatase is mainly used in molecular biology research for dephosphorylation of nucleic acids and certain proteins. The enzyme is commonly used in PCR (polymerase chain reaction) analysis because it can be used to remove phosphate groups from PCR primers, allowing for more efficient amplification of DNA. In addition, it can be used to remove phosphate groups from DNA and RNA for cloning purposes, allowing specific genes to be inserted into plasmids or other vectors.
Antarctic phosphatase is a unique enzyme due to its ability to thrive in cold environments and its high affinity for substrates. Its function as a dephosphorylase makes it an important tool for molecular biology research, especially in PCR analysis and cloning applications. The structure and mechanism of action of this enzyme has been extensively studied, providing valuable insights into how the enzyme adapts to extreme environmental conditions. Although the clinical relevance of Antarctic phosphatase is limited, its unique properties still make it a fascinating research topic.
