Recombinant Zebrafish ARHGAP1
Cat.No. : | ARHGAP1-2523Z |
Product Overview : | Recombinant Zebrafish ARHGAP1 full length or partial length protein was expressed. |
- Specification
- Gene Information
- Related Products
Source : | Mammalian Cells |
Species : | Zebrafish |
Tag : | His |
Form : | Liquid or lyophilized powder |
Endotoxin : | < 1.0 eu per μg of the protein as determined by the LAL method. |
Purity : | >80% |
Notes : | This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications. |
Storage : | Store it at +4 oC for short term. For long term storage, store it at -20 oC~-80 oC. |
Storage Buffer : | PBS buffer |
Gene Name : | arhgap1 Rho GTPase activating protein 1 [ Danio rerio (zebrafish) ] |
Official Symbol : | ARHGAP1 |
Gene ID : | 550478 |
mRNA Refseq : | NM_001017781 |
Protein Refseq : | NP_001017781 |
UniProt ID : | Q568D8 |
Products Types
◆ Recombinant Protein | ||
ARHGAP1-37H | Active Recombinant Human ARHGAP1 Protein (Full Length), N-His tagged | +Inquiry |
ARHGAP1-373H | Recombinant Human ARHGAP1 Protein, His (Fc)-Avi-tagged | +Inquiry |
ARHGAP1-216R | Recombinant Rhesus Macaque ARHGAP1 Protein, His (Fc)-Avi-tagged | +Inquiry |
Arhgap1-1678M | Recombinant Mouse Arhgap1 Protein, Myc/DDK-tagged | +Inquiry |
ARHGAP1-36H | Active Recombinant Human ARHGAP1 protein, GST-tagged | +Inquiry |
◆ Lysates | ||
ARHGAP1-8745HCL | Recombinant Human ARHGAP1 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 (20)
Ask a questionYes, ARHGAP1 can undergo several post-translational modifications, including phosphorylation, acetylation, and ubiquitination. These modifications can modulate its activity, localization, and protein-protein interactions.
ARHGAP1 is primarily associated with the cell membrane or the cytoskeleton. It localizes to the plasma membrane and can interact with actin filaments, contributing to cytoskeletal rearrangement and cell motility.
Yes, ARHGAP1 can interact with various proteins and molecules. It is known to interact with Rho GTPases, such as RhoA, Rac1, and Cdc42, which are key regulators of the actin cytoskeleton. ARHGAP1 can also interact with scaffolding proteins like IQGAP1 and ECT2, as well as other GAP proteins, to regulate Rho GTPase signaling. Additionally, ARHGAP1 has been found to interact with components of the Hippo pathway, such as MST1 and LATS1, indicating its involvement in cell growth control.
The dysregulation of ARHGAP1 in certain diseases suggests that it could be a potential therapeutic target. Developing drugs or strategies to modulate the activity of ARHGAP1 or its interactions with Rho GTPases may hold therapeutic potential for conditions involving aberrant Rho GTPase signaling. However, further research is needed to explore these possibilities.
Yes, genetic mutations in ARHGAP1 have been reported in certain diseases. For example, mutations in ARHGAP1 have been identified in individuals with intellectual disabilities and developmental delay. These mutations can disrupt the protein's function or impair its interactions, leading to abnormal neuronal development and function. Additionally, alterations in ARHGAP1 expression have been observed in various cancers, indicating its involvement in disease pathogenesis.
Besides its role in regulating actin cytoskeleton dynamics, ARHGAP1 has been implicated in various other cellular processes. For example, ARHGAP1 has been shown to affect cell proliferation and survival. It can modulate cell cycle progression by interacting with proteins involved in cell division, such as ECT2 and Cyclin B1. ARHGAP1 has also been found to regulate apoptosis signaling pathways by interacting with caspase-3 and Bcl-2 family proteins. Additionally, ARHGAP1 has been implicated in cell adhesion, angiogenesis, and epithelial-to-mesenchymal transition (EMT), highlighting its involvement in multiple cellular processes.
ARHGAP1 is widely expressed in various cell types and tissues. It is found in both normal and cancerous cells. While the expression levels may vary among different cell types, ARHGAP1 has been detected in neurons, fibroblasts, epithelial cells, endothelial cells, and immune cells, among others. Its expression can be regulated by various factors, including signaling pathways, developmental cues, and disease conditions.
Genetic variations in the ARHGAP1 gene have been associated with certain diseases or conditions, including cancer and neurological disorders. These variations can alter protein function, expression levels, or interactions, potentially contributing to disease pathogenesis.
Yes, ARHGAP1 has been found to interact with various proteins. For instance, it can bind to other Rho GAPs, Rho GTPases, and actin-binding proteins, forming complexes that regulate cytoskeletal dynamics and cellular processes.
Studies in animal models have indicated that ARHGAP1 is not essential for embryonic development, as mice lacking ARHGAP1 are viable and fertile. However, these mice do exhibit defects in neural tube closure and craniofacial development, suggesting a developmental role for ARHGAP1. Furthermore, ARHGAP1 has been implicated in tissue morphogenesis during embryonic development, highlighting its importance in organ formation.
ARHGAP1 acts as a GTPase-activating protein (GAP) for Rho GTPases, including RhoA, Rac1, and Cdc42. It stimulates the intrinsic GTPase activity of these proteins, leading to the hydrolysis of GTP and the inactivation of the GTPases.
ARHGAP1 is involved in diverse cellular processes, including actin cytoskeletal remodeling, cell migration, cell adhesion, cell polarity, and cell division. It can also influence signaling pathways such as the Rho GTPase signaling pathway and the Hippo signaling pathway.
Yes, studies have suggested that ARHGAP1 is involved in embryonic development. It has been found to participate in processes such as neural tube closure and morphogenesis of various tissues and organs, indicating its importance in embryonic development and organogenesis.
Yes, the expression and activity of ARHGAP1 can be regulated by various extracellular signals and stimuli. For example, growth factors, cytokines, and other signaling molecules can modulate ARHGAP1 expression levels or its interaction with other proteins, thereby influencing its function in the cell.
Given its involvement in various diseases, including cancer, ARHGAP1 has emerged as a potential therapeutic target. Strategies to target ARHGAP1 include small molecule inhibitors or modulators that can specifically regulate its activity. By modulating ARHGAP1, it may be possible to alter cell migration, invasion, or other processes involved in disease progression. However, further research is needed to fully understand the therapeutic potential of targeting ARHGAP1.
ARHGAP1 is broadly expressed in various tissues and cell types, suggesting that it may have widespread functions throughout the body.
Targeting ARHGAP1 holds potential therapeutic implications in cancer treatment. As ARHGAP1 is involved in various processes critical for cancer progression, such as cell migration, invasion, and survival, modulating its activity could potentially inhibit tumor growth and metastasis. Targeting ARHGAP1 could be achieved through the development of small molecule inhibitors or by manipulating its expression using gene therapy approaches. However, more research is needed to fully understand the mechanisms and potential side effects of targeting ARHGAP1 in cancer therapeutics.
Mutations or dysregulation of ARHGAP1 have been implicated in several diseases. For example, alterations in ARHGAP1 expression or activity have been observed in certain types of cancer, such as breast cancer. Dysregulation of ARHGAP1 has also been linked to neurological disorders, including intellectual disability and epilepsy.
Yes, ARHGAP1 can be regulated by other proteins and signaling pathways. For example, the small GTPase RhoA can interact with and activate ARHGAP1, leading to the inhibition of RhoA signaling. Additionally, various kinases, phosphatases, and scaffold proteins can modulate ARHGAP1 activity and its interactions within signaling networks.
Several regulatory mechanisms have been identified that control the expression or activity of ARHGAP1. At the transcriptional level, ARHGAP1 can be regulated by various transcription factors, such as Runx1, PPARδ, and SP1, which bind to specific regions in the ARHGAP1 gene promoter. The activity of ARHGAP1 can also be regulated through post-translational modifications. For example, phosphorylation of ARHGAP1 by kinases, such as PKC and PAK, can affect its cellular localization and GAP activity. Additionally, ARHGAP1 can interact with scaffolding proteins and other regulators, which can modulate its function and localization within the cell.
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 ARHGAP1 protein is an exceptional choice that meets the highest standards of quality, perfectly catering to my experimental requirements.
when employed in Western Blotting experiments, the ARHGAP1 protein consistently generates sharp and well-defined protein bands, enabling precise visualization and analysis of protein expression.
the ARHGAP1 protein's well-documented properties and thoroughly tested functionality give me the confidence to integrate it seamlessly into my experimental setup.
I highly recommend the use of the ARHGAP1 protein in various experimental applications.
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.
the ARHGAP1 protein has been successfully utilized in protein electron microscopy structure analysis, providing valuable insights into molecular structures and interactions.
Considering its outstanding performance across multiple assays, I confidently endorse the inclusion of the ARHGAP1 protein in diverse research studies.
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