ARHGAP35
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Official Full Name
Rho GTPase activating protein 35
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Overview
The human glucocorticoid receptor DNA binding factor, which associates with the promoter region of the glucocorticoid receptor gene (hGR gene), is a repressor of glucocorticoid receptor transcription. The amino acid sequence deduced from the cDNA sequences show the presence of three sequence motifs characteristic of a zinc finger and one motif suggestive of a leucine zipper in which 1 cysteine is found instead of all leucines. The GRLF1 enhances the homologous down-regulation of wild-type hGR gene expression. Biochemical analysis suggests that GRLF1 interaction is sequence specific and that transcriptional efficacy of GRLF1 is regulated through its interaction with specific sequence motif. The level of expression is regulated by glucocorticoids. -
Synonyms
glucocorticoid receptor DNA binding factor 1; Rho GAP p190A; ARHGAP35; Rho GTPase-activating protein 35; GRF-1; MGC10745; KIAA1722; P190-A; P190A; glucocorticoid receptor DNA-binding factor 1; p190ARhoGAP; GRF1; p190RhoGAP; Glucocorticoid receptor repression factor 1; GRLF1; Rho GTPase activating protein 35;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | ARHGAP35-26370TH | Recombinant Human ARHGAP35, His-tagged | E.coli | His | ||
Human | ARHGAP35-5363H | Recombinant Human ARHGAP35 Protein, GST-tagged | Wheat Germ | GST | ||
Human | ARHGAP35-26370H | Recombinant Human ARHGAP35 Protein, N-His tagged | E.coli | N-His | ||
Human | ARHGAP35-5578HF | Recombinant Full Length Human ARHGAP35 Protein, GST-tagged | In Vitro Cell Free System | GST | 36 amino acids |
- Involved Pathway
- Protein Function
- Interacting Protein
- ARHGAP35 Related Articles
ARHGAP35 involved in several pathways and played different roles in them. We selected most pathways ARHGAP35 participated on our site, such as Focal adhesion, Platelet activation, Leukocyte transendothelial migration, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARHGAP35 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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Focal adhesion | BADB;PTEN;PDGFC;SOS1;ITGA2B;SHC3;ROCK1;PRKCBB;PIK3R1 |
Platelet activation | PLCB4;FCER1G;Adcy4;PTGIR;MYLK4;ROCK1;COL27A1;FYN;ARHGEF1 |
Leukocyte transendothelial migration | PIK3R1;GNAI1;RASSF5;AASS;F11R;ACTN1;ITGB2L;GNAI3;PIK3CG |
Regulation of actin cytoskeleton | MYL1;ITGA11A;PIP5K2;SCINLB;FGF3;FN1;WASB;PIP5K1C;MSNA |
ARHGAP35 has several biochemical functions, for example, DNA binding, GTP binding, GTPase activator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ARHGAP35 itself. We selected most functions ARHGAP35 had, and list some proteins which have the same functions with ARHGAP35. You can find most of the proteins on our site.
Function | Related Protein |
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DNA binding | EPAS1;ZFP143;HMBOX1A;SIX4B;ZFP1;IRF7;HELT;NKX2.5;TRERF1 |
GTP binding | RAB11B;MX1;RAB7A;CDC42L;ARL3L2;SUCLG1;GTPBP1;EIF2B2;RAB27B |
GTPase activator activity | RAP1GAP2B;ACAP3;PLEKHG6;TBC1D22A;SMAP2;TSC2;RIC8A;RALGAPA1;MURC |
RNA polymerase II regulatory region sequence-specific DNA binding | RXRB;ZNF792;ZNF711;BARHL1A;SATB1;IRF2;PRDM15;ELF5;E4F1 |
transcription corepressor activity | ZHX2;HDAC5;ZEB1;CTBP2A;PSMC3;TSG101;NCOR1;SMARCA4;DMAP1 |
transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding | ZNF350;MITF;CDX2;VAX1;PCGF6;CSDA;ETV3;MSX1;BCL6 |
ARHGAP35 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 ARHGAP35 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARHGAP35.
pi3p; BCL6
- Q&As
- Reviews
Q&As (23)
Ask a questionYes, ARHGAP35 can be regulated by post-translational modifications. Phosphorylation has been reported to regulate its activity and interactions with other proteins. Additionally, sumoylation and ubiquitination have also been shown to modulate ARHGAP35 function, affecting its stability and subcellular localization.
ARHGAP35 is widely expressed in various tissues and cell types. It has been detected in the brain, heart, liver, lung, kidney, and other tissues. Within the brain, ARHGAP35 is expressed in different regions, including the cortex, hippocampus, cerebellum, and striatum. Its expression levels and subcellular localization can vary depending on the tissue or cell type, suggesting context-dependent roles for ARHGAP35 in different biological processes.
Yes, the expression of ARHGAP35 can be regulated at the transcriptional level. Various transcription factors and signaling pathways, such as those involving Rho GTPases themselves, can influence ARHGAP35 expression. Post-translational modifications and protein-protein interactions can also affect its activity and localization.
The dysregulation of ARHGAP35 in certain diseases, particularly cancer, makes it a potential therapeutic target. Modulating ARHGAP35 activity could potentially alter RhoA signaling and impact cellular processes associated with disease progression. However, further research is needed to determine the feasibility and effectiveness of targeting ARHGAP35 for therapeutic purposes.
ARHGAP35 is broadly expressed in various tissues of the body, although its expression levels can vary among different cell types. It is found in both embryonic and adult tissues, indicating its involvement in diverse physiological processes.
Future research endeavors regarding ARHGAP35 include investigating its precise mechanisms of action, understanding its roles in specific cellular processes and tissues, and determining its involvement in various diseases. Additionally, exploring potential therapeutic approaches targeting ARHGAP35 and its signaling pathways will be of interest.
Yes, ARHGAP35 can interact with several other proteins and signaling molecules. For example, it has been shown to interact with the Rho GTPases Cdc42 and Rac1, which are key regulators of cytoskeletal dynamics. ARHGAP35 can also interact with other Rho GTPase activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs) to modulate Rho GTPase signaling. Additionally, ARHGAP35 has been reported to interact with synaptic proteins such as PSD-95, indicating its involvement in synaptic function.
Yes, alterations in ARHGAP35 expression and activity have been implicated in various types of cancer. Dysregulation of ARHGAP35 can lead to abnormal RhoA signaling, contributing to cancer progression and metastasis. ARHGAP35 has been shown to affect cellular processes involved in cancer, such as cell migration, invasion, and metastatic potential, making it a potential therapeutic target.
ARHGAP35 plays a crucial role in cell migration by regulating the activity of RhoA. It promotes the inactivation of RhoA, leading to the retraction of the rear of the cell and the formation of membrane protrusions at the leading edge, which are necessary for cell migration. ARHGAP35 acts as a key regulator of the balance between cellular contraction and protrusion during migration.
At present, there is limited direct evidence linking ARHGAP35 to neurodevelopmental disorders such as autism or schizophrenia. However, several studies have identified genetic variants in other Rho GTPase signaling pathway components that are associated with these disorders, suggesting a potential indirect role for ARHGAP35. Further research is needed to determine if ARHGAP35 mutations or dysregulation contribute to the pathogenesis of these disorders.
Yes, ARHGAP35 is involved in several signaling pathways. It has been shown to interact with and modulate the activity of various Rho family GTPases, including RhoA, Rac1, and Cdc42. These GTPases are key regulators of cytoskeletal dynamics and cell signaling, and ARHGAP35 plays a role in their inactivation and downstream signaling.
Yes, ARHGAP35 is involved in neuronal development and morphogenesis. It regulates processes such as neurite outgrowth, axon guidance, and dendritic branching by controlling RhoA-mediated cytoskeletal dynamics. Disruptions in ARHGAP35 function can impact the development and connectivity of the nervous system.
Yes, several mutations and genetic variations in ARHGAP35 have been reported. These can lead to alterations in its structure, function, or expression levels. Some mutations have been associated with certain developmental disorders or cancer, highlighting the importance of ARHGAP35 in these conditions.
Yes, ARHGAP35 has been studied in animal models to investigate its functions in development and disease. Knockout or knockdown of ARHGAP35 in mice has been shown to result in altered neuronal morphology, impaired synaptic plasticity, and behavioral abnormalities. These findings suggest that ARHGAP35 plays a critical role in neuronal development and function. Additionally, zebrafish models have been used to study the role of ARHGAP35 in embryonic development and organogenesis.
Yes, there is evidence that suggests ARHGAP35 plays a role in neuronal development and synaptic plasticity. It has been found to be expressed in the developing nervous system and interacts with proteins involved in neuronal signaling and cytoskeletal dynamics. Studies in animal models have shown that ARHGAP35 regulates dendritic spine morphology and synaptic transmission, indicating its involvement in synaptic plasticity.
While alterations in ARHGAP35 have been implicated in cancer, its involvement in other diseases is still being investigated. ARHGAP35 dysregulation may contribute to neurodevelopmental disorders, as well as pathologies associated with abnormal cell migration and cytoskeletal organization. More research is needed to fully understand the extent of its involvement in various diseases.
Targeting ARHGAP35 or its downstream signaling pathways may have therapeutic implications, particularly in diseases or conditions where dysregulated Rho GTPase activity is involved, such as cancer or neurodevelopmental disorders. However, more research is needed to fully understand the specific roles of ARHGAP35 in these contexts and develop effective therapeutic strategies.
Yes, ARHGAP35 has been found to interact with several proteins. These include other RhoGAPs, RhoGEFs, cytoskeletal components such as actin and myosin, as well as scaffolding and signaling proteins. These interactions provide a mechanism for ARHGAP35 to regulate Rho GTPases and coordinate their signaling activities within the cell.
Several experimental tools are available to study ARHGAP35 function. These include techniques such as RNA interference (RNAi) or CRISPR/Cas9-mediated gene knockdown or knockout to investigate the effects of ARHGAP35 depletion on cellular processes. Overexpression systems or gene editing approaches can be used to assess the impact of ARHGAP35 overexpression or specific mutations on cellular behavior. Biochemical assays, such as GTPase activity assays, can also be utilized to study the effects of ARHGAP35 on Rho GTPase activity.
ARHGAP35 interacts with multiple proteins to regulate its activity and localization. It has been shown to interact with cytoskeletal proteins such as actin, myosin, and vinculin, which are involved in cell migration and cytoskeletal organization. Additionally, ARHGAP35 interacts with signaling molecules such as Src family kinases and p120-catenin, which modulate its activity and downstream signaling.
Yes, alterations in ARHGAP35 expression or function have been implicated in cancer development and progression. For example, decreased expression of ARHGAP35 has been observed in certain types of cancer, including breast and colorectal cancer, and is associated with poor prognosis. Dysregulation of ARHGAP35-mediated RhoA inactivation can lead to increased cell migration, invasion, and tumor metastasis.
In addition to its role in cell migration, ARHGAP35 is involved in several other physiological processes. It participates in the regulation of cell adhesion, cell cycle progression, epithelial-to-mesenchymal transition, and neuronal development. ARHGAP35's ability to modulate RhoA signaling contributes to its involvement in various cellular functions and physiological processes.
ARHGAP35-mediated RhoA inactivation affects several important cellular processes. These include cell migration, cell adhesion, cytoskeletal dynamics, cell cycle progression, and cell polarity. By regulating RhoA activity, ARHGAP35 contributes to the coordination of these processes in various cellular contexts.
Customer Reviews (8)
Write a reviewThe manufacturer also offers valuable customer support, actively aiding researchers in their experimental journey.
Its exceptional performance, in combination with its clear and distinct protein bands, make it an absolute must-have for researchers looking to achieve accurate and reliable results in their experiments.
Their technical expertise, product quality, customer support, and supply management collectively contribute to the success and progress of my trials.
They ensure the purity, integrity, and functionality of ARHGAP35 protein through rigorous quality control measures.
the ARHGAP35 protein stands out for its exceptional quality, coupled with the outstanding technical support delivered by the manufacturer.
I enthusiastically recommend the ARHGAP35 protein to fellow researchers who seek an unparalleled product accompanied by dedicated customer assistance.
Its purity, integrity, and functionality are ensured through stringent quality control measures, which instills confidence in the reliability and accuracy of my research results.
I highly recommend the ARHGAP35 protein for a variety of experimental applications.
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