AGAP5
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Official Full Name
ArfGAP with GTPase domain, ankyrin repeat and PH domain 5
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Synonyms
CTGLF2; arf-GAP with GTPase, ANK repeat and PH domain-containing protein 5; AGAP-5; centaurin-gamma-like family member 2; centaurin, gamma-like family, member 2;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | AGAP5-3616H | Recombinant Human AGAP5, His-tagged | E.Coli or Yeast | His | 686 |
- Involved Pathway
- Protein Function
- Interacting Protein
AGAP5 involved in several pathways and played different roles in them. We selected most pathways AGAP5 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AGAP5 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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AGAP5 has several biochemical functions, for example, GTPase activator activity, metal ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AGAP5 itself. We selected most functions AGAP5 had, and list some proteins which have the same functions with AGAP5. You can find most of the proteins on our site.
Function | Related Protein |
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GTPase activator activity | GIT1;TBC1D13;FAM13A;TBC1D19;RGS5B;GDI2;PREX2;RAP1GAP;TBC1D10A |
metal ion binding | PAN3;ZNF350;ZKSCAN3;GFI1AB;E4F1;MAT2A;CDH24;ADAM25;MORC1 |
AGAP5 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 AGAP5 here. Most of them are supplied by our site. Hope this information will be useful for your research of AGAP5.
HSPB1
- Q&As
- Reviews
Q&As (20)
Ask a questionApart from potential roles in SMA modification, AGAP5's involvement in membrane trafficking and cellular organization suggests broader functions in intracellular transport.
AGAP5 activity is regulated by factors like post-translational modifications, protein-protein interactions, and potential cellular localization changes.
While the exact role of AGAP5 in SMA is not mentioned, its mutation suggests it could be part of the genetic landscape that influences the disease's severity.
AGAP5's ankyrin repeat domains indicate potential interactions with other proteins, possibly influencing its activity and cellular functions.
Yes, AGAP5's ankyrin repeat and PH domain also suggest possible roles in protein-protein interactions and lipid binding, respectively.
AGAP5 is primarily located at the trans-Golgi network and endosomes within cells.
The mutations in AGAP5 are noteworthy as they might contribute to altering the severity of SMA in the affected individuals, highlighting AGAP5's potential role as a genetic modifier.
AGAP5's role in cellular processes makes it a candidate for involvement in other diseases, although specific connections beyond SMA might require further research.
The mutations in AGAP5 were likely identified through genetic sequencing and analysis of the patients' genomes, alongside mutations in TLL2 and VPS13A.
Given its involvement in cellular processes, AGAP5 could potentially be targeted for therapeutic interventions aimed at modulating membrane trafficking and related disorders.
Although research is ongoing, AGAP5's dysregulation could potentially impact cellular trafficking processes and contribute to diseases like cancer and neurological disorders.
Animal models, such as genetically modified mice or cell-based models, could be used to study AGAP5's function and its effects on cellular processes.
Yes, the expression and function of AGAP5 might vary across tissues and cell types, contributing to different outcomes in different contexts.
AGAP5 comprises an ARF-GAP domain responsible for GTPase regulation, ankyrin repeat domains for protein interactions, and a PH domain possibly involved in lipid binding.
It's possible that AGAP5 interacts with other genetic modifiers to collectively impact the severity of SMA, demonstrating the complex genetic nature of the disease.
AGAP5 influences vesicle budding, cargo sorting, and membrane fusion by modulating the activity of ARF6, a GTPase involved in endocytic pathways.
AGAP5, also known as Arf-GAP with GTPase domain, Ankyrin repeat, and PH domain 5, is a protein involved in cellular processes like membrane trafficking and cytoskeleton regulation.
In the SMA discordant family case, mutations were identified in the AGAP5 gene among other genes. These mutations could play a role in modifying the severity of SMA.
AGAP5 functions as a GTPase-activating protein (GAP) that regulates the activity of small GTPases, including ADP-ribosylation factor 6 (ARF6). It controls vesicle trafficking and membrane dynamics.
AGAP5's role in membrane trafficking and cellular organization makes it crucial for maintaining proper intracellular transport and compartmentalization.
Customer Reviews (5)
Write a reviewConsistently achieving specific outcomes validated the product’s essential role in our studies.
Agap5 consistently downregulated the expression of inflammatory markers.
Our experiments with Agap5 showed no signs of protein aggregation.
The product’s unique traits propelled our research to new levels of innovation.
Using Protein Agap5, we obtained uniform results in various experimental conditions.
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