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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human ARL2BP Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 17.91 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 | Met1-Glu133 |
Aliases /Synonyms | BART1, Binder of ARF2 protein 1, ARL2-binding protein, ARF-like 2-binding protein, BART, ARL2BP, ADP-ribosylation factor-like protein 2-binding protein |
Reference | ARO-P11860 |
Note | For research use only. |
Recombinant proteins have become essential tools in both basic research and biotechnology due to their ability to mimic natural proteins and perform specific functions. One such protein is Recombinant Human ARL2BP Protein, which has gained significant attention in recent years for its diverse structural and functional properties. In this article, we will delve into the structure, activity, and application of this protein, highlighting its importance in various fields of science.
Recombinant Human ARL2BP Protein, also known as ADP-ribosylation factor-like 2 binding protein, is a 22 kDa protein consisting of 195 amino acids. It belongs to the ARL2BP family of proteins and is highly conserved among different species, with a 98% similarity between human and mouse ARL2BP sequences.
The protein structure is composed of three functional domains: an N-terminal coiled-coil domain, a central zinc finger domain, and a C-terminal domain. The coiled-coil domain allows ARL2BP to interact with its binding partner, ARL2, and form a stable complex. The central zinc finger domain is responsible for binding to GTP-bound ARL2, while the C-terminal domain is involved in protein-protein interactions and is crucial for the protein’s function.
Recombinant Human ARL2BP Protein is a multifunctional protein involved in various cellular processes. Its main function is to act as a GTPase-activating protein (GAP) for ARL2, a small GTPase protein involved in cytoskeletal organization and vesicular trafficking. ARL2BP binds to ARL2 and stimulates its intrinsic GTPase activity, leading to the hydrolysis of GTP to GDP and the release of ARL2 from its target proteins.
In addition to its role as a GAP, Recombinant Human ARL2BP Protein also functions as an effector protein for ARL2. It can interact with ARL2 in its GTP-bound form and regulate its activity, thereby modulating various cellular processes such as microtubule dynamics, cell adhesion, and cell cycle progression.
Due to its multifunctional nature, Recombinant Human ARL2BP Protein has a wide range of applications in both basic research and biotechnology. In basic research, it is used as a tool to study the role of ARL2 in various cellular processes. Recombinant ARL2BP can be overexpressed or silenced in cells to investigate its effect on ARL2 activity and its downstream signaling pathways.
In biotechnology, Recombinant Human ARL2BP Protein has potential applications in drug discovery and development. ARL2 has been implicated in various diseases, including cancer and neurodegenerative disorders. By targeting ARL2BP, researchers can modulate ARL2 activity and potentially develop new therapies for these diseases.
Furthermore, Recombinant Human ARL2BP Protein has been used in the development of biosensors for detecting ARL2 activity in cells. These biosensors can be used to study the dynamics of ARL2 signaling in real-time and provide insights into its role in different cellular processes.
In summary, Recombinant Human ARL2BP Protein is a crucial protein with diverse structural and functional properties. Its structure allows it to interact with ARL2 and regulate its activity, making it an essential component in various cellular processes. Its multifunctional nature and potential applications in both basic research and biotechnology make it a valuable tool for scientists studying ARL
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