Human ARF6 protein (Recombinant) (N-His) (STJP008225)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human ARF6-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | ARF6 |
| Gene ID | 382 |
| Uniprot ID | ARF6_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Met1-Ser175 |
Additional Info
| Post Translational Modifications | GTP-bound form is myristoylated on Lys-3 by NMT1 and NMT2, allowing ARF6 to remain on membranes during the GTPase cycle, thereby promoting its activity. GDP-bound inactive form is demyristoylated on Lys-3 by SIRT2 at early endosomes or endocytic recycling compartment to allow its efficient activation by a guanine exchange factor (GEF) after GDP release. |
| Function | GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. GTP-bound form plays an important role in the transport of multiple palmitoylated proteins form the Golgi to the plasma membrane. Required for normal completion of mitotic cytokinesis. Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Potentiates the neurite outgrowth in primary neurons by interacting with the molecular adapter APBB1. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization. Regulates surface levels of adherens junction proteins such as CDH1. Required for NTRK1 sorting to the recycling pathway from early endosomes. (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. (Microbial infection) Plays a key role in the endocytosis of enterovirus 71 and thus viral entry into brain microvascular endothelial cells. |
| Protein Name | Adp-Ribosylation Factor 6 |
| Database Links | Reactome: R-HSA-8854214Reactome: R-HSA-8856828Reactome: R-HSA-8875656 |
| Cellular Localisation | CytoplasmCytosolCell MembraneLipid-AnchorEndosome MembraneRecycling Endosome MembraneCell ProjectionFilopodium MembraneRuffleCleavage FurrowMidbodyMidbody RingEarly Endosome MembraneGolgi ApparatusTrans-Golgi Network MembraneDistributed Uniformly On The Plasma MembraneAs Well As Throughout The Cytoplasm During MetaphaseSubsequently Concentrated At Patches In The Equatorial Region At The Onset Of CytokinesisAnd Becomes Distributed In The Equatorial Region Concurrent With Cleavage Furrow IngressionIn Late Stages Of CytokinesisConcentrates At The Midbody Ring/Flemming BodyRecruitment To The Midbody Ring Requires Both Activation By Psd/Efa6a And Interaction With Kif23/Mklp1After Abscission Of The Intercellular BridgeIncorporated Into One Of The Daughter Cells As A Midbody Remnant And Localizes To Punctate Structures Beneath The Plasma MembraneRecruited To The Cell Membrane In Association With Cyth2 And Arl4cColocalizes With Dab2ip At The Plasma Membrane And Endocytic VesiclesMyristoylation Is Required For Proper Localization To Membranes: Myristoylation On Lys-3 Allows Arf6 To Remain On Membranes During The Gtpase Cycle |
| Alternative Protein Names | Adp-Ribosylation Factor 6 proteinARF6 protein |
Information sourced from Uniprot.org