ARHGAP10
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Zebrafish | ARHGAP10-4256Z | Recombinant Zebrafish ARHGAP10 | Mammalian Cell | His |
- Involved Pathway
- Protein Function
- Interacting Protein
ARHGAP10 involved in several pathways and played different roles in them. We selected most pathways ARHGAP10 participated on our site, such as Rho GTPase cycle, Signal Transduction, Signaling by Rho GTPases, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARHGAP10 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Rho GTPase cycle | CHN2;ARHGAP17A;GMIP;FGD4A;NET1;RALBP1;RHOT1;ARHGAP29B;RHOF |
Signal Transduction | MYO7A;USP34;DLK1;OXGR1A.3;RGS4;SOX4A;NOG;PRLRB;SHRPRBCK1R |
Signaling by Rho GTPases | ARHGEF17;KIF14;MYO9B;ABI1A;RHPN2;FAM13B1;ROPN1;NCKIPSD;DLC1 |
ARHGAP10 has several biochemical functions, for example, GTPase activator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ARHGAP10 itself. We selected most functions ARHGAP10 had, and list some proteins which have the same functions with ARHGAP10. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
GTPase activator activity | RGS14A;RALBP1;ARHGAP24;ARHGAP23;ARHGAP4;DAB2IPB;RGS3;ARHGEF1;ACAP3 |
ARHGAP10 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 ARHGAP10 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARHGAP10.
- Q&As
- Reviews
Q&As (14)
Ask a questionYes, ARHGAP10 has been implicated in various diseases. In cancer, altered ARHGAP10 expression or activity has been linked to tumor progression, metastasis, and poor prognosis in several types of cancer, including breast, ovarian, and lung cancer. Additionally, ARHGAP10 has been associated with cardiovascular diseases, where it regulates processes like vascular smooth muscle cell migration and proliferation, which are critical in vascular remodeling and atherosclerosis development.
The regulation of ARHGAP10 expression is not fully understood, but several factors have been identified as potential upstream regulators. The transcription factor AP-1 (activator protein 1) has been shown to bind to the ARHGAP10 promoter and positively regulate its expression. Additionally, growth factors such as epidermal growth factor (EGF) and fibroblast growth factor (FGF) can induce ARHGAP10 expression. Other stimuli, including oxidative stress and DNA damage, have also been reported to upregulate ARHGAP10 expression. However, further research is needed to fully elucidate the regulatory mechanisms of ARHGAP10 expression.
Yes, ARHGAP10 has been implicated in the regulation of cell proliferation. Studies have shown that ARHGAP10 can affect cell cycle progression and cell proliferation in various cellular contexts. Overexpression of ARHGAP10 has been reported to inhibit cell proliferation in cancer cell lines, suggesting a tumor-suppressive role. Conversely, downregulation of ARHGAP10 has been associated with increased cell proliferation in certain cell types. However, the specific mechanisms by which ARHGAP10 regulates cell proliferation are not yet fully understood and further research is needed to elucidate its role in this process.
Yes, ARHGAP10 has been implicated in various diseases and pathological conditions. Its dysregulation has been observed in several types of cancer, including ovarian cancer, breast cancer, and glioblastoma, where altered ARHGAP10 expression levels correlate with tumor progression and poor prognosis. Moreover, ARHGAP10 has been implicated in neurodevelopmental disorders, such as autism spectrum disorders and intellectual disabilities, as well as in cardiovascular diseases, including congenital heart defects. The exact mechanisms by which ARHGAP10 contributes to these diseases are still being investigated.
Yes, ARHGAP10 can undergo post-translational modifications that may regulate its activity and function. Phosphorylation of ARHGAP10 at specific sites by kinases such as Src or Akt has been reported to affect its GAP activity or subcellular localization. Additionally, acetylation and SUMOylation of ARHGAP10 have also been suggested to modulate its activity, although the precise consequences of these modifications are not fully understood.
Targeting ARHGAP10 for therapeutic purposes is a possibility that is being explored. Given its involvement in various diseases, including cancer and neurodevelopmental disorders, modulating ARHGAP10 activity or expression may have therapeutic potential. However, further research is needed to fully understand the complex regulatory mechanisms of ARHGAP10 and to develop strategies for targeting it effectively. This may involve the identification of small molecules or other therapeutic agents that can selectively modulate ARHGAP10 function.
Yes, ARHGAP10 can modulate cell adhesion. It has been shown to interact with proteins involved in focal adhesion, such as focal adhesion kinase (FAK) and paxillin. By controlling Rho GTPase activity, ARHGAP10 can influence actin dynamics and focal adhesion turnover, which are critical for cell adhesion. Dysregulation of ARHGAP10 expression or activity can disrupt cell adhesion processes, impacting cell migration and cell-substrate interactions.
Currently, there are no specific drugs targeting ARHGAP10 available on the market. However, understanding the role of ARHGAP10 in diseases has sparked interest in developing therapeutic strategies. Studies exploring small molecule inhibitors or RNA interference-based approaches to inhibit ARHGAP10 function are ongoing, with the aim of developing potential treatments for cancer and cardiovascular diseases.
Yes, ARHGAP10 plays a role in cell migration. By regulating RhoA activity and actin cytoskeleton dynamics, ARHGAP10 influences processes essential for cell migration, such as lamellipodia and filopodia formation, cell protrusion, and focal adhesion turnover. ARHGAP10 has been implicated in both normal physiological cell migration, such as neuronal migration during development, and pathological cell migration, like cancer cell invasion and metastasis.
ARHGAP10 controls actin cytoskeleton dynamics through its GAP activity towards RhoA. RhoA is a member of the Rho GTPase family and is vital for actin polymerization and organization. As a GAP, ARHGAP10 accelerates the hydrolysis of GTP to GDP on RhoA, resulting in the inactivation of RhoA. This deactivation of RhoA leads to the disassembly of stress fibers and focal adhesions, resulting in cytoskeletal rearrangements.
Yes, ARHGAP10 is involved in neuronal development and function. It plays a role in neuronal migration during brain development, as demonstrated by studies using mouse models. ARHGAP10 knockout mice exhibit defects in neuronal migration and show abnormalities in brain structure.
Yes, mouse models and knockout studies have been conducted to investigate the function of ARHGAP10. These studies have demonstrated that ARHGAP10 is essential for embryonic development and is involved in various processes, including neural tube closure and cardiovascular development. ARHGAP10 knockout mice exhibit abnormalities in the brain and heart, highlighting the crucial role of ARHGAP10 in these tissues. These animal models have provided valuable insights into the physiological functions of ARHGAP10.
ARHGAP10 can interact with various proteins to regulate its activity and function. For instance, it has been shown to form complexes with tyrosine kinases, such as Src and FAK, and adaptor proteins like paxillin and Crk. These interactions can modulate ARHGAP10's GAP activity and influence downstream signaling pathways involved in cell adhesion, migration, and cytoskeletal dynamics. Additionally, ARHGAP10 has also been reported to interact with other Rho GTPase regulators, further highlighting its role in coordinating RhoA signaling.
Yes, ARHGAP10 can interact with various proteins to regulate its function. It has been shown to interact with several members of the Rho GTPase family, including RhoA, Rac1, and Cdc42. These interactions are important for ARHGAP10's GAP activity and its ability to modulate actin cytoskeleton dynamics. ARHGAP10 can also interact with other proteins involved in cytoskeletal regulation, such as focal adhesion kinase (FAK) and paxillin, which are key components of focal adhesions.
Customer Reviews (8)
Write a reviewIts high specificity and robust activity make it an ideal candidate for investigating intricate molecular interactions and elucidating complex biological mechanisms.
I have full confidence in the ARHGAP10 protein and the exceptional support provided by the manufacturer, making it my top recommendation for researchers seeking a high-quality protein for their experimental needs.
Their knowledgeable team has been readily available to address any concerns or queries, providing effective solutions and guidance whenever needed.
I am extremely pleased with the quality of the ARHGAP10 protein as it perfectly fulfills my experimental requirements.
Its impeccable purity and reliability ensure accurate and reproducible results, providing a solid foundation for my research.
With the ARHGAP10 protein, I can confidently pursue my scientific objectives and overcome experimental obstacles, enabling me to make significant strides in my field of study.
This protein exhibits exceptional purity and reliability, ensuring accurate and reproducible results in my assays.
Tthe manufacturer's commitment to exceptional technical support offers me peace of mind, knowing that any challenges or concerns I may encounter will be effectively addressed. he manufacturer's commitment to exceptional technical support offers me peace of mind, knowing that any challenges or concerns I may encounter will be effectively addressed.
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