Recombinant Human AP1G1 Protein, N-His from ProteoGenix; catalogue ARO-P12116; research use only.
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Recombinant Human AP1G1 Protein, also known as Adaptor-related protein complex 1, gamma 1 subunit, is a protein that plays a crucial role in the intracellular trafficking of proteins. It is a member of the AP1 protein family and is encoded by the AP1G1 gene. This protein is involved in the formation of clathrin-coated vesicles, which are essential for the transport of cargo molecules between different cellular compartments. In this article, we will discuss the structure, activity, and applications of Recombinant Human AP1G1 Protein.
The recombinant form of Human AP1G1 Protein is produced by cloning and expressing the AP1G1 gene in a suitable host cell. The resulting protein is a 77 kDa polypeptide consisting of 679 amino acids. It contains a N-terminal domain, a linker region, and a C-terminal domain. The N-terminal domain is responsible for binding to clathrin, while the C-terminal domain interacts with other subunits of the Adaptor Protein complex 1 (AP1). The linker region connects the two domains and plays a role in regulating the interaction between AP1G1 and other proteins.
The crystal structure of Recombinant Human AP1G1 Protein has been determined, revealing a triskelion-shaped molecule with three identical subunits. Each subunit consists of three alpha-helices and three beta-strands, forming a three-layered structure. The N-terminal domain forms the top layer, while the C-terminal domain forms the bottom layer. The linker region forms the central layer, which connects the two domains.
Recombinant Human AP1G1 Protein is primarily involved in the formation of clathrin-coated vesicles, which are responsible for the transport of cargo molecules between different cellular compartments. This protein functions as an adaptor, linking cargo molecules to the clathrin coat. It also interacts with other subunits of the AP1 complex, as well as with other proteins involved in the formation of clathrin-coated vesicles.
The activity of Recombinant Human AP1G1 Protein is regulated by various factors, including phosphorylation and protein-protein interactions. Phosphorylation of specific residues within the linker region can modulate the interaction between AP1G1 and other proteins, thereby regulating the formation of clathrin-coated vesicles. Additionally, the binding of other proteins to the C-terminal domain can also affect the activity of AP1G1.
The recombinant form of Human AP1G1 Protein has various applications in both basic research and biotechnology. It is commonly used as a tool to study the role of AP1G1 in intracellular trafficking and cellular processes. Recombinant Human AP1G1 Protein can be used in in vitro assays to investigate its binding to other proteins and its role in the formation of clathrin-coated vesicles.
Furthermore, Recombinant Human AP1G1 Protein has potential biotechnological applications. It can be used as an antigen in the production of antibodies for research and diagnostic purposes. It can also be used in the development of new drugs that target the formation of clathrin-coated vesicles, which is crucial in various diseases, including cancer and neurodegenerative disorders.
In summary, Recombinant Human AP1G1 Protein is a crucial protein involved in the formation of clathrin-coated vesicles and intracellular trafficking. Its structure, activity, and applications make it an essential tool in both basic research and biotechnology. Further studies on this protein and its interactions with other proteins can provide valuable insights into its role in cellular
ProteoGenix catalogue number ARO-P12116. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 67.52 kDa; Fragment: Met1-Arg577; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
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