ARHGEF4
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Official Full Name
Rho guanine nucleotide exchange factor (GEF) 4
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Overview
Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein may form complex with G proteins and stimulate Rho-dependent signals. This protein is similar to rat collybistin protein. Alternative splicing of this gene generates two transcript variants which encode different isoforms. Also there is possibility for the usage of multiple polyadenylation sites for this gene. -
Synonyms
ARHGEF4; Rho guanine nucleotide exchange factor (GEF) 4; rho guanine nucleotide exchange factor 4; APC stimulated guanine nucleotide exchange factor; ASEF; KIAA1112; STM6; ARHGEF 4; GEF 4; GEF; GEF4; STM 6; APC-stimulated guanine nucleotide exchange factor 1; ASEF1;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | ARHGEF4-787H | Recombinant Human ARHGEF4 protein, GST-tagged | Wheat Germ | GST | ||
Human | ARHGEF4-8730HCL | Recombinant Human ARHGEF4 293 Cell Lysate | HEK293 | N/A | ||
Human | ARHGEF4-1237HF | Recombinant Full Length Human ARHGEF4 Protein, GST-tagged | In Vitro Cell Free System | GST | 690 amino acids |
- Involved Pathway
- Protein Function
- Interacting Protein
ARHGEF4 involved in several pathways and played different roles in them. We selected most pathways ARHGEF4 participated on our site, such as Regulation of actin cytoskeleton, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARHGEF4 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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Regulation of actin cytoskeleton | PAK6B;FGD3;WASF1;ARPC5LB;GSNA;PAK6;ARHGEF4;MYLK3;SSH3 |
ARHGEF4 has several biochemical functions, for example, Rac guanyl-nucleotide exchange factor activity, guanyl-nucleotide exchange factor activity, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ARHGEF4 itself. We selected most functions ARHGEF4 had, and list some proteins which have the same functions with ARHGEF4. You can find most of the proteins on our site.
Function | Related Protein |
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Rac guanyl-nucleotide exchange factor activity | FARP1;SPATA13;VAV1;ALS2;ARHGEF2;ARHGEF4;VAV3;PREX2;DOCK2 |
guanyl-nucleotide exchange factor activity | RASGEF1BB;ARHGEF11;GCGR;RASGRP1;RAPGEF1B;FARP2;DENND5B;KNDC1;RAPGEF6 |
protein binding | INTS9;TH1L;AMIGO2;CPSF3;FABP5;P4HB;RAN;MBNL1;HOXB9 |
protein domain specific binding | OSBP;CNOT1;RAN;GNAI3;MED12;POU2F2;ZFP521;ZNF521;RAP2B |
ARHGEF4 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 ARHGEF4 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARHGEF4.
HLA-B; RAC1; NEDD8
- Q&As
- Reviews
Q&As (15)
Ask a questionYes, ARHGEF4 interacts with several other proteins to mediate its functions. It has been found to interact with Rho GTPases, as well as other signaling molecules and cytoskeletal proteins, such as actin and myosin.
Yes, ARHGEF4 does have isoforms and splice variants. Different isoforms may vary in their domain structure, protein interactions, or expression patterns. These isoforms may contribute to the diversity of functions associated with ARHGEF4.
Yes, ARHGEF4 interacts with multiple proteins and molecules to regulate various cellular processes. For example, it can interact with Rho GTPases, activating or inactivating them in response to upstream signaling cues. ARHGEF4 can also interact with other signaling molecules like kinases and phosphatases, as well as cellular adhesion proteins and cytoskeleton-associated proteins, thereby influencing cell adhesion and migration.
Limited information is available regarding specific mutations or genetic variations in ARHGEF4 and their associations with diseases. Further research and genetic studies are necessary to understand if variations in ARHGEF4 contribute to certain disorders.
Targeting ARHGEF4 for therapeutic purposes is an area of ongoing research. Since dysregulation of ARHGEF4 is associated with various diseases, developing strategies to modulate its activity or expression could have therapeutic potential. However, further studies are needed to fully understand ARHGEF4's role in diseases and to explore potential therapeutic interventions targeting this protein.
Yes, ARHGEF4 has been the subject of scientific research, and there is literature available on its functions, interactions, and associations with diseases. However, more studies are needed to fully elucidate its role in cellular processes and its relevance to human health and diseases.
Dysregulation of ARHGEF4 has been implicated in several diseases and pathologies. For example, abnormal expression or function of ARHGEF4 has been observed in certain cancers, including breast, lung, and colorectal cancer, where it contributes to tumor progression and metastasis. ARHGEF4 dysregulation has also been linked to neurological disorders, such as Alzheimer's disease, where it may play a role in synaptic dysfunction and neuronal degeneration.
Due to its involvement in diseases like cancer and neurodevelopmental disorders, targeting ARHGEF4 may have potential therapeutic implications. However, further research is required to better understand its precise molecular mechanisms and validate its therapeutic potential.
Yes, ARHGEF4 has been implicated in several diseases and pathological conditions. It has been associated with cancer progression, specifically in metastasis, as well as neurodevelopmental disorders and neurodegenerative diseases.
While information on animal models or knockout studies specifically targeting ARHGEF4 is limited, there have been studies involving the modulation of Rho GTPases or related pathways that indirectly impact ARHGEF4 function. These studies often provide insights into the cellular and physiological consequences of ARHGEF4 dysregulation.
Yes, the expression of ARHGEF4 can be dynamically regulated during development. It is expressed in various tissues and cell types, and its expression levels may change during different stages of development or in response to specific signaling cues.
ARHGEF4 is widely expressed in various tissues and cell types. It has been detected in the brain, heart, liver, lungs, and skeletal muscles, among others. Its expression levels can vary in different tissues and during different stages of development.
ARHGEF4 is not considered an essential protein for basic cellular function. However, it plays important roles in specific cellular processes, such as cell migration and cytoskeletal dynamics, which are crucial for various physiological functions.
ARHGEF4 is primarily involved in the regulation of Rho family GTPases, specifically RhoA, Rac1, and Cdc42. These GTPases play critical roles in cellular processes such as cell migration, cell adhesion, cytoskeletal organization, and cell polarity.
To the best of our knowledge, there are no specific small molecules or inhibitors that directly target ARHGEF4 activity reported in the literature. However, targeting the downstream effector proteins or pathways regulated by ARHGEF4, such as Rho GTPases, may indirectly modulate ARHGEF4-mediated functions.
Customer Reviews (8)
Write a reviewExtensive research has been conducted on ARHGEF4, making it relatively accessible and well-understood in terms of its structure and functions.
ARHGEF4 protein is highly recommended for use in various research applications, including ELISA and protein electron microscopy structure analysis.
The manufacturer's excellent technical support, commitment to innovation, and customer-centric approach further reinforce its suitability for my research.
With their support, I can confidently explore the intricacies of ARHGEF4 and make significant contributions to the understanding of its functions in various biological processes.
This existing knowledge base provides a solid foundation for designing experiments and interpreting results, ultimately enhancing the efficiency and reliability of trials involving ARIH1L protein.
ARHGEF4 protein's remarkable performance in ELISA and protein electron microscopy structure analysis positions it as a valuable tool in various fields, including cardiovascular research, developmental biology, and molecular medicine.
ARHGEF4 protein's utility extends to protein electron microscopy structure analysis, where it plays a crucial role in investigating the detailed architecture and conformational changes of proteins.
It exhibits exceptional performance in ELISA assays, making it an excellent choice for researchers studying angiopoietins, angiogenesis, or vascular biology.
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