ARFIP1
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Official Full Name
ADP-ribosylation factor interacting protein 1
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Overview
Arfaptin-1 is a protein that in humans is encoded by the ARFIP1 gene. -
Synonyms
ARFIP1; ADP-ribosylation factor interacting protein 1; arfaptin-1; arfaptin 1; HSU52521; ADP-ribosylation factor-interacting protein 1; MGC117369;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Human
- Rat
- Rhesus Macaque
- Zebrafish
- E.coli
- E.Coli or Yeast
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- ARFIP1 Related Articles
ARFIP1 involved in several pathways and played different roles in them. We selected most pathways ARFIP1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ARFIP1 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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ARFIP1 has several biochemical functions, for example, phosphatidylinositol-4-phosphate binding, protein domain specific binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ARFIP1 itself. We selected most functions ARFIP1 had, and list some proteins which have the same functions with ARFIP1. You can find most of the proteins on our site.
Function | Related Protein |
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phosphatidylinositol-4-phosphate binding | ARFIP1;SNX24;MBL1;OSBP;COL4A3BP;PLEKHF1;OSBPL8;FAM21C;PRRC2B |
protein domain specific binding | STAMBP;RAP2B;ICAL1;WNT3;CHMP1A;MLF1;XPO1;LIN7C;NFE2L2 |
ARFIP1 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 ARFIP1 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARFIP1.
PRKD2; recN; q9wmx2-pro_0000037551
- Q&As
- Reviews
Q&As (19)
Ask a questionYes, besides its role in cancer progression, ARFIP1 is involved in various cellular processes. It is associated with endocytic trafficking and recycling, as it interacts with proteins involved in clathrin-mediated endocytosis and vesicle transport, such as clathrin, AP-1, and Rab proteins. ARFIP1 is also implicated in regulating the actin cytoskeleton, cell migration, and neurite outgrowth.
Currently, there are no specific drugs or compounds that specifically target ARFIP1. However, given its involvement in membrane trafficking and its potential implications in disease processes, further research may identify potential therapeutic strategies that modulate ARFIP1 activity or its interaction with other proteins involved in vesicle trafficking.
Genetic variations or mutations in the ARFIP1 gene have not been extensively characterized. However, genomic databases such as dbSNP and ClinVar contain some reported variants in the ARFIP1 gene, including single nucleotide polymorphisms (SNPs) and rare mutations. Further investigation is needed to determine the functional consequences of these variations and their potential association with diseases or conditions.
ARFIP1 binds to ARF GTPases through its ARF-binding domain (ABD), forming a complex that modulates ARF activity. This interaction allows ARFIP1 to regulate vesicle formation, cargo selection, and membrane remodeling during various cellular processes.
Yes, alternative splicing of ARFIP1 pre-mRNA can generate different isoforms. For example, an ARFIP1 variant isoform lacking the C-terminal region has been reported in humans. These isoforms may have distinct functions or exhibit tissue-specific expression patterns.
Yes, ARFIP1 can localize to various cellular compartments depending on the cellular context. It has been observed to co-localize with endocytic markers, Golgi apparatus, and recycling endosomes, indicating its involvement in these membrane trafficking compartments. However, further studies are needed to fully understand the precise localization pattern of ARFIP1 in different cell types or conditions.
ARFIP1 has two known isoforms: full-length ARFIP1 and a shorter isoform called ARFIP1Δexon8. The main difference between the isoforms lies in the exclusion of exon 8 in ARFIP1Δexon8, resulting in a truncated protein lacking a functional clathrin-binding domain. While the full-length ARFIP1 is implicated in various cellular processes such as endocytic trafficking, membrane dynamics, and cell migration, the specific functions of ARFIP1Δexon8 are not well characterized. It is suggested that ARFIP1Δexon8 may have distinct functions or act as a dominant-negative isoform. Further investigation is needed to elucidate the specific roles of ARFIP1 isoforms and their contributions to cellular processes and diseases.
Although not extensively studied, there are emerging reports suggesting potential associations of ARFIP1 with certain diseases. For example, altered expression or function of ARFIP1 has been implicated in cancer progression, neuronal development disorders, and neurodegenerative diseases. However, further research is needed to fully understand the implications of ARFIP1 in these contexts.
Currently, there are no ongoing clinical trials or research studies specifically targeting ARFIP1. However, the field of ARFIP1 research is still relatively new and expanding, so it is possible that future studies will explore its potential as a therapeutic target.
It is possible that ARFIP1 or its isoforms could serve as biomarkers for certain diseases, especially if their expression levels or subcellular localization are altered in specific pathological conditions. However, more research is needed to validate these associations and establish their clinical relevance.
Currently, there are no known specific inhibitors or activators targeting ARFIP1. However, small-molecule inhibitors or compounds that affect upstream regulators or downstream effectors of ARFIP1, such as the GTPase ARF1 or clathrin-dependent endocytosis components, may indirectly affect ARFIP1 function. Furthermore, modulating ARFIP1 expression or its interacting partners using techniques such as gene silencing or overexpression may provide insights into its functional role. Future studies may identify specific drugs or molecules that directly target ARFIP1 and modulate its activity.
ARFIP1 dysregulation has been implicated in various diseases and conditions. For example, studies have shown that altered expression or function of ARFIP1 is associated with cancer progression. Additionally, ARFIP1 has been linked to neurological disorders such as Alzheimer's disease, where it may play a role in the regulation of amyloid precursor protein (APP) trafficking and processing. Further research is needed to fully understand the extent of ARFIP1 involvement in these diseases and identify potential therapeutic targets.
Yes, several proteins have been reported to interact with ARFIP1 and modulate its function. These include members of the ARF family of GTPases, clathrin, AP-1, COP I, as mentioned earlier. Additionally, other proteins, such as the ARF GTPase-activating proteins (ARFGAPs) and ARF guanine nucleotide exchange factors (ARFGEFs), can also interact with ARFIP1, potentially influencing its activity or cellular localization.
While ARFIP1 is primarily known for its role in membrane trafficking, it has been suggested that it can also participate in cell signaling pathways. For instance, ARFIP1 has been implicated in regulating the activity of RHO GTPases, which play key roles in various signaling cascades involved in cell migration, cell polarity, and cytoskeletal dynamics.
ARFIP1 is involved in various cellular processes, including endocytosis, intracellular protein transport, and organelle biogenesis. It plays a role in the regulation of vesicle formation and trafficking between different compartments of the cell, ensuring proper cargo delivery and maintenance of cellular homeostasis.
Besides ARF GTPases, ARFIP1 can interact with other proteins involved in vesicle trafficking, including clathrin, AP-1, and COP I coat proteins. These interactions facilitate the assembly of coat protein complexes, leading to proper vesicle formation and cargo sorting.
Yes, ARFIP1 is highly conserved across various species, including mammals, birds, fish, and invertebrates. This conservation suggests that ARFIP1 plays a fundamental role in cellular processes and its function has been evolutionarily conserved throughout different organisms.
ARFIP1 has been implicated in cancer progression through its involvement in membrane trafficking, cell migration, and invasion. Studies have shown that ARFIP1 expression is upregulated in various cancer types, including breast, colorectal, and gastric cancer, and is associated with increased tumor growth and metastasis. ARFIP1 can regulate the trafficking and secretion of growth factors, extracellular matrix components, and cell adhesion molecules, thereby promoting cancer cell proliferation, angiogenesis, and invasive behavior. It is suggested that ARFIP1 may serve as a potential target for anti-cancer therapies, but further research is needed to fully understand its precise mechanisms and therapeutic implications.
Yes, animal models such as mice can be used to study the function of ARFIP1. Gene knockout or knockdown approaches can be employed to investigate the consequences of ARFIP1 loss-of-function in vivo. This can provide insights into the physiological roles of ARFIP1 and its potential contributions to disease processes.
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.
The manufacturer's support has played a vital role in my work, providing expert guidance and troubleshooting assistance whenever needed.
This quality control instills trust in the product, eliminating any worries about variability and ensuring the integrity of my research outcomes.
Its reliability, specificity, and consistent performance enable me to obtain accurate data to further my research goals.
Its impeccable purity and reliability ensure accurate and reproducible results, providing a solid foundation for my research.
With the ARFIP1 protein, I can confidently pursue my scientific objectives and overcome experimental obstacles, enabling me to make significant strides in my field of study.
the ARFIP1 protein offers exceptional advantages in my trials, facilitating my exploration of important cellular mechanisms.
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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