Rho Guanine Nucleotide Exchange Factor 7
Cat.No. : | CBCRY28 |
- Specification
- Gene Information
- Related Products
Cat. No. : | CBCRY28 |
Background : | 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 belongs to a family of cytoplasmic proteins that activate the Ras-like family of Rho proteins by exchanging bound GDP for GTP. It may form a complex with G proteins and stimulate Rho-dependent signals. This protein can induce membrane ruffling. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences have not been determined. |
Protein Classification : | Signaling Protein |
Structure Weight : | 15255.28 Da |
Polymer : | 1 |
Molecule : | Rho guanine nucleotide exchange factor 7 |
Chain Length : | 61 amino acids |
PDB ID : | 2ESW |
MMDB ID : | 38672 |
Source : | E.coli |
Method : | X-Ray Diffraction |
Resolution : | 2.01Å |
Ligand Chemical Component : | Chloride ion; Mercury ion |
Reference : | Li, X., Liu, X., Sun, F., Gao, J., Zhou, H., Gao, G.F., Bartlam, M., Rao, Z. (2006) Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor Biochem. Biophys. Res. Commun. 339: 407-414 |
Gene Name : | Arhgef7 |
Synonyms : | PIX; Cool; Pak3bp; cool-1; p85SPR; betaPix; p85Cool1; betaPix-b; betaPix-c; mKIAA0142; Arhgef7; PAK-interacting exchange factor beta; OTTMUSP00000023238; Pak3 binding protein; Pak interacting exchange factor; Dkfzp761k1021; kiaa0412; p50; p50bp; p85; pak3; pixb |
UniProt ID : | Q6XPA5 |
Gene ID : | 54126 |
Chromosome Location : | 8 A1.1 |
Function : | guanyl-nucleotide exchange factor activity; Rho guanyl-nucleotide exchange factor activity; protein binding |
Products Types
◆ Recombinant Protein | ||
ARHGEF7-703M | Recombinant Mouse ARHGEF7 Protein, His (Fc)-Avi-tagged | +Inquiry |
ARHGEF7-3892H | Recombinant Human ARHGEF7 Protein, MYC/DDK-tagged | +Inquiry |
Arhgef7-1696M | Recombinant Mouse Arhgef7 Protein, Myc/DDK-tagged | +Inquiry |
ARHGEF7-9840H | Recombinant Human ARHGEF7, GST-tagged | +Inquiry |
ARHGEF7-3594H | Recombinant Human ARHGEF7 protein, His-tagged | +Inquiry |
◆ Lysates | ||
ARHGEF7-8729HCL | Recombinant Human ARHGEF7 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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- Q&As
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Q&As (18)
Ask a questionIn addition to Rho GTPase activation, ARHGEF7 regulates various cellular processes and pathways. It can modulate actin dynamics and actomyosin contractility, leading to changes in cell shape and motility. ARHGEF7 also contributes to the regulation of cell adhesion and cell-matrix interactions by influencing focal adhesion turnover and integrin signaling. Furthermore, ARHGEF7 has been reported to interact with and modulate the activity of other signaling molecules, such as kinases and phosphatases, suggesting its involvement in diverse signaling pathways within the cell.
Currently, there are no pharmacological agents specifically designed to modulate ARHGEF7 expression or activity. However, certain drugs or therapeutic approaches that target upstream signaling pathways and regulators of ARHGEF7, such as growth factor receptor inhibitors or kinase inhibitors, may indirectly affect ARHGEF7 activity. Manipulating ARHGEF7 expression or activity using gene therapy or RNA interference techniques may also hold potential for therapeutic intervention, but further research is required in this area.
ARHGEF7 activates downstream signaling pathways primarily through its interaction with and activation of Rho GTPases, particularly RAC1. Activation of RAC1 by ARHGEF7 leads to the activation of various effector proteins, including p21-activated kinase (PAK), to regulate cytoskeletal dynamics, cell migration, and other cellular processes. ARHGEF7-mediated RhoA activation can also contribute to downstream signaling events related to actomyosin contractility and cell adhesion.
Yes, there have been studies reporting genetic mutations or alterations in ARHGEF7 that are associated with certain diseases. For example, mutations in ARHGEF7 have been found in individuals with X-linked intellectual disability (XLID) and epilepsy, suggesting a role for ARHGEF7 in neurological development and function. Additionally, alterations in ARHGEF7 expression have been observed in various cancers, including breast, lung, and pancreatic cancer, and have been linked to tumor progression and metastasis.
ARHGEF7 interacts with multiple proteins to carry out its functions. It interacts with RAC1, PAK1, and other components of the cytoskeleton, such as actin and microtubules. ARHGEF7 can also interact with various signaling molecules and adaptor proteins, allowing it to integrate and transduce signals from multiple cellular pathways.
There is accumulating evidence that genetic variations in ARHGEF7 can contribute to disease susceptibility. Single nucleotide polymorphisms (SNPs) and structural variations in the ARHGEF7 gene have been associated with conditions such as cancer, neurodevelopmental disorders, and neurodegenerative diseases, suggesting a potential role of ARHGEF7 in disease pathogenesis.
Currently, there are no specific small molecule inhibitors available for ARHGEF7. However, inhibitors targeting the downstream effectors or regulators of ARHGEF7, such as inhibitors of Rho GTPases or ROCK, may indirectly impact ARHGEF7-mediated signaling. Developing specific small molecule inhibitors for ARHGEF7 remains an active area of research.
Yes, ARHGEF7 is involved in cell adhesion and migration processes. It promotes the formation of focal adhesions and actin stress fibers, which are essential for cell attachment and migration. ARHGEF7-mediated activation of RAC1 regulates important cytoskeletal rearrangements necessary for cell motility, including the formation of lamellipodia and filopodia.
While there are no specific therapeutics targeting ARHGEF7 currently available, its downstream target RAC1 has been a focus of drug development. Inhibitors of RAC1 signaling are being explored as potential anti-cancer agents. Modulating the activity or expression of ARHGEF7 itself may also hold therapeutic potential, but more research is needed to understand its precise role in disease pathogenesis and identify effective targeting strategies.
Dysregulation of ARHGEF7 has been implicated in various diseases. For example, ARHGEF7 is involved in cancer progression, where its overexpression can promote tumor cell migration and metastasis. ARHGEF7 variants or mutations have also been associated with neurodevelopmental disorders such as autism spectrum disorder (ASD) and intellectual disabilities.
Yes, ARHGEF7 can undergo alternative splicing, resulting in the generation of different isoforms. These isoforms may have distinct functions or subcellular localizations, contributing to the functional diversity of ARHGEF7. Further research is needed to fully understand the individual roles of these isoforms and their significance in different cellular contexts.
ARHGEF7 interacts with RAC1 and catalyzes the exchange of GDP for GTP on RAC1. This activates RAC1 by promoting its transition from the inactive GDP-bound form to the active GTP-bound form. Activated RAC1 then regulates downstream signaling pathways involved in cytoskeletal rearrangement and cell behavior.
Yes, ARHGEF7 plays a role in neuronal development and synaptic plasticity. It is expressed in the brain and has been implicated in dendritic spine morphogenesis and synapse formation. ARHGEF7 interacts with PAK1, a kinase important for synaptic plasticity, suggesting its involvement in neuronal signaling and connectivity.
Yes, ARHGEF7 has other functions and roles beyond cell migration and cytoskeletal dynamics. It has been implicated in the regulation of cell polarity, epithelial-mesenchymal transition (EMT), and cell adhesion. ARHGEF7 has also been shown to be involved in the regulation of cell proliferation, cell survival, and angiogenesis. Furthermore, studies have suggested a potential role for ARHGEF7 in neuronal development and synaptic plasticity in the brain.
Yes, ARHGEF7 has been implicated in cancer progression and metastasis. It is known to promote tumor cell invasion and migration by enhancing cytoskeletal dynamics and modulating cell-matrix adhesion. Increased expression of ARHGEF7 has been associated with poor prognosis in various cancer types, suggesting its potential as a therapeutic target. However, further research is needed to fully elucidate the specific mechanisms and roles of ARHGEF7 in cancer progression.
Yes, several regulators and inhibitors of ARHGEF7 activity have been identified. One example is the Rho GTPase-activating protein (RhoGAP) ARHGAP25, which can bind and inhibit ARHGEF7, thereby negatively regulating its activity. Additionally, certain proteins or signaling pathways, such as Rho kinase (ROCK) and protein kinase C (PKC), can modulate ARHGEF7 activity through phosphorylation or other post-translational modifications.
Yes, mouse models with targeted disruption or mutations in the Arhgef7 gene have been generated. These models have been utilized to investigate the role of ARHGEF7 in various physiological processes, including neuronal development, neural circuit formation, and disease-related phenotypes.
Yes, besides its well-known interaction with RAC1, ARHGEF7 can also interact with other members of the Rho GTPase family, such as RhoA and CDC42. These interactions enable ARHGEF7 to regulate the activity and signaling of multiple Rho GTPases, allowing for a coordinated control of cytoskeletal dynamics and cell behaviors.
Customer Reviews (8)
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ARHGEF7 protein is highly recommended for researchers and scientists due to its exceptional performance in ELISA assays.
ARHGEF7 protein has proven to be instrumental in protein electron microscopy structure analysis.
the ARHGEF7 protein's versatility extends beyond its use in vitro experiments.
Its stability and well-defined structure make it an excellent candidate for visualizing and understanding the three-dimensional arrangement of proteins at a high resolution.
Whether investigating the role of ARHGEF7 in angiogenesis, vascular development, or disease pathways, this protein surpasses expectations and guarantees reliable results.
Its superior binding affinity and specificity enable accurate and reliable detection of target analytes in various biological samples.
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