Cell-matrix adhesion regulates membrane trafficking controlling anchorage-dependent signaling. Whereas a dynamic Golgi advanced can contribute to this pathway, its regulation by adhesion stays unclear. Right here we report that lack of adhesion dramatically disorganized the Golgi in mouse and human fibroblast cells. Golgi integrity is restored quickly upon integrin-mediated re-adhesion to FN and is disrupted by integrin blocking antibody.
In suspended cells, the cis, cis-medial and trans-Golgi networks differentially disorganize alongside the microtubule community however present no overlap with the ER, making this disorganization distinct from identified Golgi fragmentation. This pathway is regulated by an adhesion-dependent discount and restoration of Arf1 activation. Constitutively lively Arf1 disrupts this regulation and prevents Golgi disorganization because of lack of adhesion.
Adhesion-dependent Arf1 activation regulates its binding to the microtubule minus-end motor protein dynein to regulate Golgi reorganization, which is blocked by ciliobrevin. Adhesion-dependent Golgi group controls its operate, regulating cell floor glycosylation because of lack of adhesion, which is blocked by constitutively lively Arf1. This research, therefore, recognized integrin-dependent cell-matrix adhesion to be a novel regulator of Arf1 activation, controlling Golgi group and performance in anchorage-dependent cells. This text has an related First Individual interview with the primary writer of the paper.
Evaluation of Membrane Protein Topology within the Plant Secretory Pathway.
Topology of membrane proteins offers vital info for the understanding of protein operate and intermolecular associations. Combine membrane proteins are typically transported from endoplasmic reticulum (ER) to Golgi and downstream compartments within the plant secretory pathway. Right here, we describe a easy methodology to check membrane protein topology alongside the plant secretory pathway by transiently coexpressing a fluorescent protein (XFP)-tagged membrane protein and an ER export inhibitor protein, ARF1 (T31N), in tobacco BY-2 protoplast.
By fractionation, microsome isolation, and trypsin digestion, membrane protein topology may very well be simply detected by both direct confocal microscopy imaging or western-blot evaluation utilizing particular XFP antibodies. An analogous technique in figuring out membrane protein topology may very well be extensively adopted and utilized to protein evaluation in a broad vary of eukaryotic methods, together with yeast cells and mammalian cells.
Mixed concentrating on of Arf1 and Ras potentiates anticancer exercise for prostate most cancers therapeutics.
Though main enhancements have been made in surgical administration, chemotherapeutic, and radiotherapeutic of prostate most cancers, many prostate cancers stay refractory to therapy with customary brokers.
Subsequently, the identification of latest molecular targets in most cancers development and growth of novel therapeutic methods to focus on them are very needed for reaching higher survival for sufferers with prostate most cancers. Activation of small GTPases reminiscent of Ras and Arf1 is a crucial element of the signaling pathways for a lot of the receptors proven to be upregulated in superior prostate most cancers.
Which Approach In? The RalF Arf-GEF Orchestrates Rickettsia Host Cell Invasion.
Bacterial Sec7-domain-containing proteins (RalF) are identified solely from species of Legionella and Rickettsia, which have facultative and obligate intracellular existence, respectively. L. pneumophila RalF, a kind IV secretion system (T4SS) effector, is a guanine nucleotide trade issue (GEF) of ADP-ribosylation elements (Arfs), activating and recruiting host Arf1 to the Legionella-containing vacuole.
In distinction, earlier in vitro research confirmed R. prowazekii (Typhus Group) RalF is a practical Arf-GEF that localizes to the host plasma membrane and interacts with the actin cytoskeleton through a novel C-terminal area. As RalF is differentially encoded throughout Rickettsia species (e.g., pseudogenized in all Noticed Fever Group species), it could operate in lineage-specific biology and pathogenicity.
Herein, we display RalF of R. typhi (Typhus Group) interacts with the Rickettsia T4SS coupling protein (RvhD4) through its proximal C-terminal sequence. RalF is expressed early throughout an infection, with its inactivation through antibody blocking considerably decreasing R. typhi host cell invasion.
For R. typhi and R. felis (Transitional Group), RalF ectopic expression revealed subcellular localization with the host plasma membrane and actin cytoskeleton. Remarkably, R. bellii (Ancestral Group) RalF confirmed perinuclear localization paying homage to ectopically expressed Legionella RalF, for which it shares a number of structural options. For R. typhi, RalF co-localization with Arf6 and PI(4,5)P2 at entry foci on the host plasma membrane was decided to be crucial for invasion.
Thus, we suggest recruitment of PI(4,5)P2 at entry foci, mediated by RalF activation of Arf6, initiates actin transforming and finally facilitates bacterial invasion. Collectively, our characterization of RalF as an invasin means that, regardless of carrying an identical Arf-GEF unknown from different micro organism, completely different intracellular existence throughout Rickettsia and Legionella species have pushed divergent roles for RalF throughout an infection. Moreover, our identification of lineage-specific Arf-GEF utilization throughout some rickettsial species illustrates completely different pathogenicity elements that outline numerous brokers of rickettsial ailments.
Hematopoietic stem/progenitor cells immediately contribute to arteriosclerotic development through integrin β2.
Current research described the affiliation between hematopoietic stem/progenitor cell (HSPC) enlargement within the bone marrow (BM), leukocytosis within the peripheral blood, and accelerated atherosclerosis. We hypothesized that circulating HSPC could house to infected vessels, the place they may contribute to irritation and neointima formation.
We demonstrated that Lin(-) Sca-1(+) cKit(+) (LSK cells) in BM and peripheral blood of LDLr(-/-) mice on excessive fats eating regimen expressed considerably extra integrin β2 , which was answerable for LSK cell adhesion and migration towards ICAM-1 in vitro, and homing to injured arteries in vivo, all of which have been blocked with an anti-CD18 blocking antibody. When homed LSK cells have been remoted from ligated artery and injected to irradiated recipients, they resulted in BM reconstitution.
Injection of CD18(+/+) LSK cells to immunodeficient Balb/C Rag2(-) ɣC(-/-) recipients resulted in additional extreme irritation and strengthened neointima formation within the ligated carotid artery, in comparison with mice injected with PBS and CD18(-/-) LSK cells. Hypercholesterolemia stimulated ERK phosphorylation (pERK) in LSK cells of LDLr(-/-) mice in vivo.
ARF1 antibody |
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| 70R-12842 | Fitzgerald | 100 ul | EUR 548.4 |
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Description: Affinity purified Rabbit polyclonal ARF1 antibody |
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ARF1 antibody |
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| 70R-15789 | Fitzgerald | 50 ul | EUR 522 |
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Description: Rabbit polyclonal ARF1 antibody |
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ARF1 antibody |
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| 70R-13531 | Fitzgerald | 100 ul | EUR 548.4 |
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Description: Affinity purified Rabbit polyclonal ARF1 antibody |
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ARF1 antibody |
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| 22691-100ul | SAB | 100ul | EUR 468 |
ARF1 antibody |
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| 22693-100ul | SAB | 100ul | EUR 468 |
ARF1 Antibody |
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| 31145-100ul | SAB | 100ul | EUR 302.4 |
ARF1 Antibody |
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| 31145-50ul | SAB | 50ul | EUR 224.4 |
ARF1 antibody |
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| 10R-1775 | Fitzgerald | 100 ul | EUR 386.4 |
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Description: Mouse monoclonal ARF1 antibody |
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ARF1 antibody |
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| 10R-1783 | Fitzgerald | 100 ul | EUR 386.4 |
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Description: Mouse monoclonal ARF1 antibody |
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ARF1 antibody |
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| 10-2473 | Fitzgerald | 250 ug | EUR 590.4 |
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Description: Mouse monoclonal ARF1 antibody |
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ARF1 Antibody |
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| ABD7650 | Lifescience Market | 100 ug | EUR 525.6 |
ARF1 Antibody |
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| ABD8122 | Lifescience Market | 100 ug | EUR 525.6 |
ARF1 Antibody |
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| V7900-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V7900-20UG | NSJ Bioreagents | 20 ug | EUR 219 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V7900SAF-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V7901-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V7901-20UG | NSJ Bioreagents | 20 ug | EUR 219 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V7901SAF-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF's share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| R33779-100UG | NSJ Bioreagents | 100 ug | EUR 399 |
ARF1 Antibody |
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| F49371-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 165 |
ARF1 Antibody |
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| F49371-0.4ML | NSJ Bioreagents | 0.4 ml | EUR 379 |
ARF1 Antibody |
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| V3811-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF s share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V3811-20UG | NSJ Bioreagents | 20 ug | EUR 219 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF s share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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ARF1 Antibody |
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| V3811SAF-100UG | NSJ Bioreagents | 100 ug | EUR 499 |
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Description: The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF s share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. |
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Arf1/ Rat Arf1 ELISA Kit |
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| ELI-11213r | Lifescience Market | 96 Tests | EUR 1063.2 |
ARF1 Conjugated Antibody |
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| C31145 | SAB | 100ul | EUR 476.4 |
ARF1 Conjugated Antibody |
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| C49120 | SAB | 100ul | EUR 476.4 |
anti- ARF1 antibody |
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| FNab00528 | FN Test | 100µg | EUR 606.3 |
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Description: Antibody raised against ARF1 |
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anti- ARF1 antibody |
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| FNab00529 | FN Test | 100µg | EUR 658.5 |
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Description: Antibody raised against ARF1 |
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Anti-ARF1 antibody |
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| PAab00528 | Lifescience Market | 100 ug | EUR 426 |
Anti-ARF1 antibody |
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| PAab00529 | Lifescience Market | 100 ug | EUR 463.2 |
Anti-ARF1 antibody |
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| STJ11100853 | St John's Laboratory | 100 µl | EUR 495.6 |
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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. |
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Anti-ARF1 antibody |
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| STJ113570 | St John's Laboratory | 100 µl | EUR 332.4 |
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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. |
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Anti-ARF1 Antibody |
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| STJ500153 | St John's Laboratory | 100 µg | EUR 618 |
Anti-ARF1 antibody |
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| STJ118785 | St John's Laboratory | 100 µl | EUR 332.4 |
Anti-ARF1 antibody |
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| STJ22666 | St John's Laboratory | 100 µl | EUR 332.4 |
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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. |
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ARF1 Polyclonal Antibody |
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| A73506-050 | EpiGentek | 50 ul | EUR 377.3 |
ARF1 Polyclonal Antibody |
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| A73506-100 | EpiGentek | 100 ul | EUR 577.5 |
ARF1 Polyclonal Antibody |
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| A73506 | EpiGentek |
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ARF1 siRNA |
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| 20-abx907921 | Abbexa |
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ARF1 siRNA |
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| 20-abx907922 | Abbexa |
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ARF1 Peptide |
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| 45-277P | ProSci | 0.1 mg | EUR 405.6 |
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Description: ARF1 Peptide |
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ARF1 siRNA |
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| 20-abx900400 | Abbexa |
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anti-ARF1 |
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| YF-PA23239 | Abfrontier | 50 ul | EUR 400.8 |
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Description: Mouse polyclonal to ARF1 |
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Blockade of pERK diminished ARF1 expression, resulting in decreased integrin β2 operate on HSPC. As well as, integrin β2 operate may very well be regulated through ERK-independent LRP1 pathway. Integrin β2 expression on HSPC is regulated by hypercholesterolemia, particularly LDL, in pERK-dependent and -independent manners, resulting in elevated homing and localization of HSPC to injured arteries, which is very correlated with arteriosclerosis.
