Recombinant Human ARF1 Protein (His Tag)

Name: Recombinant Human ARF1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0250
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P84077
Synonym	ARF1
Background	Invasion of tumor cells is a key step in metastasis that depends largely on the ability of these cells to degrade the extracellular matrix. The ARF1+ARF4 and ARF1+ARF3 pairs are both required for integrity of recycling endosomes but are involved in distinct transport pathways: the former pair regulates retrograde transport from endosomes to the TGN, whereas the latter is required for the transferrin recycling pathway from endosomes to the plasma membrane. The ADP-ribosylation factors (ARFs) 1 and 6 are small GTP-binding proteins, highly expressed and activated in several breast cancer cell lines and are associated with enhanced migration and invasiveness. ARF1 is a key role in invasion of breast cancer cells and suggest that targeting the ARF/Rho/MLC signaling axis might be a promising strategy to inhibit invasiveness and metastasis. ARF1 regulates cell migration and provide this GTPase as a target for the development of new therapeutics in triple negative breast cancer. ADP-ribosylation factor 1 (ARF1) is a crucial regulator in vesicle-mediated membrane trafficking and involved in the activation of signaling molecules. The aberrant MAPK signaling in prostate cancer is, at least in part, under the control of ARF1 and that, similar to Ras, ARF1 is a critical regulator in prostate cancer progression. ARF1 may represent a key molecular target for prostate cancer therapeutics and diagnosis.
Description	A DNA sequence encoding the human ARF1 (P84077) (Met1-Lys181) was expressed with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	His
AA Sequence	Met1-Lys181
Molecular Weight	The recombinant human ARF1 consists of 196 a.a. and predicts a molecular mass of 22.5 KDa. It migrates as an approximately 23 KDa band in SDS-PAGE under reducing conditions.
Purity	>85% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).; (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
Subcellular Location	Golgi apparatus. Cytoplasm, perinuclear region. Cell junction, synapse, synaptosome. Cell junction, synapse, postsynaptic density. Membrane; Lipid-anchor. Golgi apparatus, trans-Golgi network membrane; Lipid-anchor.
Protein Families	Small GTPase superfamily, Arf family
Database References	HGNC: 652 OMIM: 103180 KEGG: hsa:375 STRING: 9606.ENSP00000272102 UniGene: Hs.286221

Gene Functions References

Coincident with the loss of PICK1 by GBF1-activated ARF1, CDC42 recruitment leads to the activation of IRSp53 and the ARP2/3 complex, resulting in a burst of F-actin polymerisation potentially powering scission. PMID: 29743604
This study suggests that simultaneous blockade of Arf1 and Ras activation in prostate cancer cells is a potential targeted therapeutic strategy for preventing prostate cancer development. PMID: 28830537
Silencing of ARF1 impaired RAC1 recruitment to leading edge in neutrophil chemotaxis. PMID: 28969640
Data show that only ADP-ribosylation factor 1 (ARF1) promoter hypermethylation was significantly associated with epidermal growth factor receptor gene (EGFR) gene amplification in glioblastoma. PMID: 28631186
The zebrafish-metastasis model confirms that the ARF1 gene depletion suppresses breast cancer cells to metastatic disseminate throughout fish body. PMID: 27517156
ARF1 is a critical regulator in prostate cancer progression PMID: 27213581
our findings demonstrate that ARF1 is a molecular switch for cancer progression and thus suggest that limiting the expression/activation of this GTPase could help improve outcome for breast cancer patients. PMID: 26908458
changes in distinct lipid ratios may converge on ARF1 to increase SBP-1/SREBP-1 activity. PMID: 27320911
Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form. PMID: 28428254
ARNO-ARF1 regulates formation of podosomes by inhibition of RhoA/myosin-II and promotion of actin core assembly. PMID: 28007915
ARF1 may reverse CAM-DR by regulating phosphorylation of p27 at T157 in MM. our data shed new light on the molecular mechanism of CAM-DR in MM, and targeting ARF1 may be a novel therapeutic approach for improving the effectiveness of chemotherapy in MM. PMID: 28238095
We report here that 2-methylcoprophilinamide (M-COPA), a compound that induces disassembly of the Golgi apparatus by inactivating ADP-ribosylation factor 1 (Arf1), suppresses Stx-induced apoptosis. M-COPA inhibited transport of Stx from the plasma membrane to the Golgi apparatus and suppressed degradation of anti-apoptotic proteins and the activation of caspases PMID: 27302278
observations indicate that Arf1 and Arf3 as well as Arf6 play important roles in cytokinesis. PMID: 26330566
ARF1 activates the MAPK pathway likely using the Golgi as a main platform, which in turn activates the cytoplasmic RSK1, leading to cell proliferation. PMID: 26169956
Data indicate that ADP-ribosylation factor 1 (Arf1) colocalizes with chromogranin A and regulates secretion of insulin like growth factor 1 (IGF-1) and is required for anchorage dependent growth. PMID: 25754106
this study reports the cryo-electron microscopy structures of the Nef- and Arf1-bound AP-1 trimer in the active and inactive states. PMID: 26494761
Suggest a model in which Arf1/COPI machinery acts to control endoplasmic reticulum-lipid droplet connections for localization of key enzymes of triglyceride storage and catabolism. PMID: 24497546
ARF1 regulates cellularmigration of highly invasive triple-negative breast cancer cells, through the regulation of the focal adhesions complex. PMID: 25530216
Class I ADP-ribosylation factors are involved in enterovirus 71 replication. PMID: 24911624
Myristoylome profiling reveals a concerted mechanism of ARF GTPase deacylation by the Shigella protease IpaJ. PMID: 25773595
Study adds to the expanding role for Arf1 in the periphery and identifies a requirement for Arf1, a "Golgi Arf," in the reorganization of the cortical actin cytoskeleton on ventral surfaces, against the substratum. PMID: 24916416
Structural modeling and cellular studies show that EspG induces bidirectional traffic arrest by tethering vesicles through select ARF1-GTP/effector complexes and local inactivation of Rab1. PMID: 24582959
EFA6 is regulated by a negative feedback loop, which is mediated by an allosteric interaction of Arf6-GTP with a domain of EFA6 and monitors the activation of Arf1 and Arf6 differentially PMID: 25114232
ARF1 is the first upstream GTPase activated by EGFR. PMID: 24196838
a central role for adaptor proteins p66Shc and Grb2 in the regulation of ARF1 and ARF6 activation in invasive breast cancer cells. PMID: 24407288
ARF1+ARF4 and ARF1+ARF3 are required for integrity of recycling endosomes but are involved in distinct transport pathways: regulates retrograde transport from endosomes to the TGN, and transferrin recycling pathway from endosomes to the plasma membrane. PMID: 23783033
Inhibition of ARF1 or Rac1 expression markedly impacts the ability of MDA-MB-231 cells to migrate upon Epidermal Growth Factor stimulation. PMID: 23707487
ARF1 and ARF3 are redundantly required for the integrity of recycling endosomes PMID: 22971977
chemokine unresponsiveness in chronic lymphocytic leukemia lymphocytes results from failure of Arf1/phospholipase D1-mediated translocation of Rap1 to the plasma membrane for GTP loading and may be a specific feature of anergy induced by DNA Ags. PMID: 23804711
Arf modulates LRP6 phosphorylation for the transduction of Wnt/beta-catenin signaling. PMID: 22907437
Kinetics of interaction between ADP-ribosylation factor-1 (Arf1) and the Sec7 domain of Arno guanine nucleotide exchange factor, modulation by allosteric factors, and the uncompetitive inhibitor brefeldin A PMID: 23255605
Study solved the crystal structure of the AP-1 core in complex with GTP-bound Arf1. The most important insight is that Arf1-GTP alone, in the absence of cargo or phosphatidylinositol-4-phosphate, can unlock AP-1 and drive it into the open conformation. PMID: 23415225
Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases. PMID: 22962618
a novel molecular mechanism of circular dorsal ruffles ring size control through the ARAP1-Arf1/5 pathway. PMID: 22573888
GBF1-mediated Arf1 activation is necessary to unify cell polarity during chemotaxis PMID: 22573891
ARF1-overexpressing clones display enhanced cell proliferation, migration, and invasion. Furthermore, ARF1-overexpression might contribute to poor prognosis of gastric carcinoma patients. PMID: 22348287
the vesicular transport proteins ARF1 and GBF1 colocalized with PI4KIIIbeta and were both required for HCV replication PMID: 22359663
Arl1 acts to direct a trans-Golgi-specific Arf1 guanine nucleotide exchange factor, and hence active Arf1, to the trans side of the Golgi. PMID: 22291037
AMF-26 is a novel anticancer drug candidate that inhibits the Golgi system, targeting Arf1 activation. PMID: 22158626
A dimerization-deficient Arf1 mutant, which does not display the ability to modulate membrane curvature in vitro or to drive formation of coated vesicles, is able to recruit coatomer to allow formation of COPI-coated buds but does not support scission. PMID: 21893600
GBF1 and ATGL interact directly and in cells, through multiple contact sites on each protein. PMID: 21789191
ARF1 controls proliferation of breast cancer cells by regulating the retinoblastoma protein PMID: 21478909
Arf GTPases may be central components in WAVE signalling, acting directly, alongside Rac1. PMID: 21844371
Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain. PMID: 21454700
Arf1 regulates PLA2G6-A activity together with Arf4; and gene silencing of Arf1 was shown to alter cytosolic coat protein I subunit recruitment to the early secretory pathway. PMID: 20881058
These data provide novel insights into the role of Arf1 in the regulation of viral RNA replication and the production of infectious hepatitis C virus. PMID: 21068255
Insight into the role of dynamics in the conformational switch of the small GTP-binding protein Arf1. PMID: 20861011
Vascular endothelial growth factor receptor-2 activates ADP-ribosylation factor 1 to promote endothelial nitric-oxide synthase activation and nitric oxide release from endothelial cells PMID: 20529868
Data suggest a novel model in which ARF1 recruits PKD2 to the TGN by binding to Pro275 in its C1b domain followed by anchoring of PKD2 in the TGN membranes via binding of its C1a domain to diacylglycerol. PMID: 20089835
Data demonstrate a key role of Rab and Arf family small GTPases and intracellular trafficking in mTORC1 activation. PMID: 20457610

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