Recombinant Full Length Human ARF1 Protein, GST-tagged
Cat.No. : | ARF1-1165HF |
Product Overview : | Human ARF1 full-length ORF ( AAH11358, 1 a.a. - 181 a.a.) recombinant protein with GST-tag at N-terminal. |
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Description : | ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] |
Source : | In Vitro Cell Free System |
Species : | Human |
Tag : | GST |
Molecular Mass : | 45.65 kDa |
Protein Length : | 181 amino acids |
AA Sequence : | MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDVV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K |
Applications : | Enzyme-linked Immunoabsorbent Assay; Western Blot (Recombinant protein); Antibody Production; Protein Array |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Storage Buffer : | 50 mM Tris-HCl, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Gene Name : | ARF1 ADP-ribosylation factor 1 [ Homo sapiens ] |
Official Symbol : | ARF1 |
Synonyms : | ARF1; ADP-ribosylation factor 1 |
Gene ID : | 375 |
mRNA Refseq : | NM_001024226 |
Protein Refseq : | NP_001019397 |
MIM : | 103180 |
UniProt ID : | P84077 |
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◆ Lysates | ||
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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 (21)
Ask a questionYes, ARF1 can undergo various post-translational modifications, including phosphorylation, acetylation, and lipidation. These modifications can affect its activity, localization, and interactions with other proteins, providing a means of regulation and modulation in response to cellular cues and signaling events.
Dysregulation of ARF1 has been observed in some cancers, where it can contribute to abnormal membrane trafficking and facilitate tumor cell proliferation, invasion, and metastasis. Targeting ARF1 and its associated pathways may hold therapeutic potential in cancer treatment.
ARF1 regulates membrane trafficking pathways, including protein sorting, vesicle formation, and transport between organelles such as the Golgi apparatus, plasma membrane, and endosomes.
Yes, ARF1 is involved in various neuronal processes, including axonal development, synapse formation, and neurotransmitter release. It regulates the trafficking and recycling of synaptic vesicles, ensuring the proper function of neuronal communication.
Yes, ARF1 and its regulators are potential targets for therapeutic intervention in diseases involving abnormal membrane trafficking, such as cancer and neurodegenerative disorders. Modulating ARF1 activity could potentially impact these processes.
Although rare, mutations in ARF1 have been associated with certain genetic disorders. For example, mutations in ARF1 have been linked to arthrogryposis, renal dysfunction, and cholestasis syndrome (ARC) characterized by multisystemic impairments.
Yes, ARF1 activity can be modulated by various signaling pathways. For example, certain protein kinases can phosphorylate ARF1, leading to its activation or inactivation, depending on the context.
ARF1 activation is regulated by guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, and GTPase-activating proteins (GAPs) that promote GTP hydrolysis, inactivating ARF1.
ARF1 is essential for the recycling of membranes and receptors within the cell. It regulates the formation of endosomal compartments and mediates the sorting and retrieval of cargo molecules from endosomes back to the plasma membrane or other intracellular compartments.
Yes, mutations or dysregulation of ARF1 have been implicated in various diseases, including certain types of cancer, neurodegenerative disorders, and metabolic diseases.
Currently, there are no drugs specifically designed to target ARF1. However, certain compounds, such as brefeldin A, have been shown to inhibit ARF1 function by disrupting its activation and guanine nucleotide exchange factors (GEFs). These compounds have been used as research tools to study ARF1 function and vesicular trafficking in cellular processes.
ARF1 interacts with adaptor proteins, such as AP-1 and AP-3, to facilitate the recognition and targeting of specific cargo molecules. This ensures that the appropriate cargo is packaged into vesicles for transport to their intended destinations.
Yes, ARF1 can be regulated by lipid signaling pathways. Certain lipids, such as phosphoinositides, can directly bind and modulate the activity of ARF1 and its associated factors, influencing vesicle formation and cargo sorting.
ARF1 is involved in clathrin-mediated endocytosis, a process in which extracellular molecules are internalized by cells. It helps regulate the formation of clathrin-coated pits, which are responsible for the uptake of specific cargo molecules.
ARF1 plays a central role in the maintenance of Golgi structure and function. It promotes the recruitment of coat proteins to specific Golgi compartments, enabling the formation of transport vesicles and the sorting of proteins for proper secretion or delivery to other organelles.
Yes, like many other proteins, ARF1 undergoes post-translational modifications. One common modification is lipidation, where it is covalently attached to a lipid moiety, which helps anchor it to specific membrane compartments.
Yes, ARF1 has been shown to interact with components of the cytoskeleton, such as actin and microtubules. These interactions play a role in vesicle trafficking and membrane remodeling processes, allowing for the movement of vesicles along the cytoskeletal network.
ARF1 interacts with various effector proteins, such as coatomer protein complex I (COPI), clathrin, and adaptor proteins like AP-1 and AP-3, which mediate vesicle formation and cargo selection.
ARF1 plays a crucial role in the formation of coated vesicles. It recruits coat proteins, such as COPI and clathrin, to specific membranes, initiating the budding process and ultimately leading to the formation of vesicles.
ARF1 plays a role in lipid metabolism by regulating the transport and sorting of lipids within cells. It helps control the intracellular trafficking of lipid droplets, contributes to the formation of lipid rafts, and influences the activity of lipid-modifying enzymes, impacting lipid homeostasis and metabolism.
Yes, ARF1 can interact with other small GTPases, such as Rho and Rab proteins, to coordinate and regulate various cellular processes. These interactions provide a means of crosstalk and integration between different signaling pathways.
Customer Reviews (8)
Write a reviewThe manufacturer's support has played a vital role in my work, providing expert guidance and troubleshooting assistance whenever needed.
Its reliable bioactivity makes it an ideal choice for a diverse range of experimental applications.
Its reliability, specificity, and consistent performance enable me to obtain accurate data to further my research goals.
The manufacturer offers exceptional technical assistance, guiding researchers through various stages of their experiments.
By providing comprehensive data and resources, the manufacturer enables researchers to design and implement their trials with confidence, ensuring the desired outcomes.
the ARF1 protein offers exceptional advantages in my trials, facilitating my exploration of important cellular mechanisms.
This information is crucial for researchers in understanding the protein's behavior and interaction within their specific experimental context.
I am grateful for their dedication and commitment to ensuring the success of my experiments.
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