ARFGEF2
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Official Full Name
ADP-ribosylation factor guanine nucleotide-exchange factor 2 (brefeldin A-inhibited)
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Overview
ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP and is involved in Golgi transport. It contains a Sec7 domain, which may be responsible for its guanine-nucleotide exchange activity and also brefeldin A inhibition. -
Synonyms
ARFGEF2; ADP-ribosylation factor guanine nucleotide-exchange factor 2 (brefeldin A-inhibited); brefeldin A-inhibited guanine nucleotide-exchange protein 2; BIG2; Brefeldin A inhibited guanine nucleotide exchange protein 2; brefeldin A-inhibited GEP 2; PVN;
- Recombinant Proteins
- Protein Pre-coupled Magnetic Beads
- Mouse
- Rat
- HEK293
- Mammalian Cell
- His
- His (Fc)
- Avi
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Mouse | ARFGEF2-1847M | Recombinant Mouse ARFGEF2 Protein | Mammalian Cell | His | ||
Mouse | ARFGEF2-666M | Recombinant Mouse ARFGEF2 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Mouse | ARFGEF2-666M-B | Recombinant Mouse ARFGEF2 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Rat | ARFGEF2-756R | Recombinant Rat ARFGEF2 Protein | Mammalian Cell | His | ||
Rat | ARFGEF2-412R | Recombinant Rat ARFGEF2 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Rat | ARFGEF2-412R-B | Recombinant Rat ARFGEF2 Protein Pre-coupled Magnetic Beads | HEK293 |
- Involved Pathway
- Protein Function
- Interacting Protein
ARFGEF2 involved in several pathways and played different roles in them. We selected most pathways ARFGEF2 participated on our site, such as Endocytosis, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARFGEF2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Endocytosis | ARRB1;RAB4A;DNM3;PARD6GB;ARRB2;MDM2;SH3GLB2A;HRAS;HLA-F |
ARFGEF2 has several biochemical functions, for example, ARF guanyl-nucleotide exchange factor activity, GABA receptor binding, guanyl-nucleotide exchange factor activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ARFGEF2 itself. We selected most functions ARFGEF2 had, and list some proteins which have the same functions with ARFGEF2. You can find most of the proteins on our site.
Function | Related Protein |
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ARF guanyl-nucleotide exchange factor activity | CYTH2;CYTH1;PSD3;PSD4;CYTH1B;CYTH4B;CYTH3;PSD2;CYTH1A |
GABA receptor binding | AKAP5;GABARAPL2;GABARAPA;GABARAPL1;TRAK1;GABRA5;PLCL2;PLCL1;GABARAP |
guanyl-nucleotide exchange factor activity | PRSS56;KALRN;RASGEF1BA;RASGRP2;DENND5B;RAPGEF4;ARHGEF37;RIC8;GAPVD1 |
myosin binding | SLC6A4;SMYD1B;USH2A;VEZT;ARFGEF2;VETZ;ARFGEF1;STX4A;DMD |
protein kinase A regulatory subunit binding | PJA2;AKAP7;ARFGEF2;AKAP5;KCNQ1;PRKACA;AKAP6;AKAP9;EZR |
ARFGEF2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ARFGEF2 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARFGEF2.
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- Q&As
- Reviews
Q&As (19)
Ask a questionYes, ARFGEF2 can be studied using animal models such as mice. Gene knockout or knockdown approaches can be employed to investigate the consequences of ARFGEF2 loss-of-function in vivo. By analyzing these animal models, researchers can gain insight into the roles of ARFGEF2 in development, behavior, and disease.
The activity of ARFGEF2 can be regulated by several mechanisms. One of the main modes of regulation is through post-translational modifications such as phosphorylation and ubiquitination. Phosphorylation of specific residues within ARFGEF2 can either enhance or inhibit its activity, depending on the context. Ubiquitination can also impact ARFGEF2 activity by regulating its stability or subcellular localization.
Yes, animal models such as knockout mice have been generated to study the role of ARFGEF2 in vivo. These models provide valuable insights into the physiological functions of ARFGEF2 and its implications in diseases.
Currently, there are no specific drugs available that directly target ARFGEF2 activity. However, there may be potential for the development of small molecules or inhibitors that can modulate ARFGEF2 function or interaction with its binding partners. Further research is needed to explore this possibility.
ARFGEF2 has been demonstrated to play important roles in neuronal development and function. It is involved in the regulation of neuronal migration, axon outgrowth, dendritic spine formation, and synaptic vesicle trafficking. Mice lacking ARFGEF2 exhibit defects in neuronal morphology and synaptic function, highlighting its significance in neurodevelopmental processes.
ARFGEF2 is widely expressed in various cell types and tissues. However, its expression levels may vary between different cell types depending on their specific functions and requirements for vesicle trafficking and membrane dynamics.
Currently, no specific small molecules or drugs targeting ARFGEF2 have been reported. However, ongoing research on ARFGEF2 function and regulation may identify potential therapeutic strategies in the future.
Yes, ARFGEF2 can interact with a variety of proteins and signaling pathways. It can interact with small GTPases such as ARF and Rho family members to regulate vesicle trafficking and cytoskeletal dynamics. ARFGEF2 can also interact with other proteins involved in membrane fusion, such as SNARE proteins. Additionally, it has been found to interact with signaling molecules such as protein kinases and phosphatases, suggesting its involvement in signal transduction pathways.
Understanding the role of ARFGEF2 in vesicle trafficking and its association with neurological disorders could provide insights into potential therapeutic targets for treating conditions related to abnormal membrane trafficking and vesicle formation. Additionally, ARFGEF2 may be an attractive candidate for drug development targeted towards modulating cellular processes reliant on ARF1 activation.
Yes, ARFGEF2 has been implicated in various cellular processes such as vesicle budding, trafficking, and fusion, as well as membrane remodeling and cytoskeletal organization.
While further research is required, some studies suggest that dysregulation of ARFGEF2 expression or activity may promote tumor progression and metastasis by affecting vesicle trafficking and membrane dynamics. However, the exact mechanisms and implications of ARFGEF2 in cancer development remain to be fully elucidated.
ARFGEF2 activity is tightly regulated by multiple mechanisms. It can be regulated through post-translational modifications such as phosphorylation and sumoylation. Additionally, its activity can be modulated by interacting with regulatory proteins or through changes in subcellular localization.
Yes, ARFGEF2 interacts with multiple proteins involved in vesicle trafficking and signaling pathways. Some known interacting partners include ARF GTPases, Rho GTPases, SNARE proteins, protein kinases (such as ROCK and PKC), and phosphatases (such as PP2A). Additional interacting partners may be identified through further research.
Yes, mutations in the ARFGEF2 gene have been implicated in neurological disorders such as autosomal recessive pontocerebellar hypoplasia (PCH). PCH is characterized by underdevelopment of the brainstem and cerebellum, leading to severe developmental delays and neurological deficits.
Mutations in the ARFGEF2 gene have been identified in individuals with neurodevelopmental disorders such as intellectual disability and autism spectrum disorders. These mutations disrupt the proper function of ARFGEF2, leading to impaired neuronal development and function. Additionally, altered expression or activity of ARFGEF2 has been implicated in cancers, including breast cancer and hepatocellular carcinoma, suggesting its potential involvement in tumorigenesis.
ARFGEF2 is primarily located in the Golgi apparatus and endosomes, where it regulates vesicle trafficking between these compartments.
Although there are no specific therapeutics targeting ARFGEF2 currently available, its involvement in various cellular processes and disease-related pathways makes it a potential target for drug development. Future studies may identify specific inhibitors or modulators of ARFGEF2 that could be utilized for therapeutic interventions in relevant diseases.
Yes, ARFGEF2 has been found to interact with various proteins involved in vesicle trafficking, including clathrin, AP-1, AP-3, and the COPI coat complex.
ARFGEF2 is involved in neuronal migration by regulating the dynamics of the cytoskeleton. It promotes the formation of membrane protrusions, such as lamellipodia and filopodia, which are necessary for the movement of migrating neurons. ARFGEF2 activates Rho GTPases, such as Rac1 and Cdc42, which in turn regulate actin polymerization and cytoskeletal reorganization required for neuronal migration.
Customer Reviews (8)
Write a reviewThe manufacturer's outstanding technical support serves as a valuable resource, providing prompt and knowledgeable assistance whenever I encounter difficulties or require guidance.
he ARFGEF2 protein is an exceptional choice that meets the highest standards of quality, perfectly catering to my experimental requirements.
the manufacturer's commitment to quality control and product development is admirable.
Whether studying its role in cell adhesion, signal transduction, or host-pathogen interactions, the ARFGEF2 protein consistently delivers reliable and reproducible results.
the ARFGEF2 protein's well-documented properties and thoroughly tested functionality give me the confidence to integrate it seamlessly into my experimental setup.
Their expertise and commitment to customer satisfaction are truly commendable, ensuring that I have access to the necessary resources to overcome any experimental hurdles that may arise.
This level of support has been invaluable in optimizing my protocols and ensuring the success of my experiments.
Their rigorous testing procedures and attention to detail guarantee the consistency and reliability of the ARFGEF2 protein across different batches.
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