ADP-ribosylation factor 6 Recombinant Protein | ARF6 recombinant protein

Recombinant Human ADP-ribosylation factor 6

Cat. Num. AAA957148

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: ADP-ribosylation factor 6; Recombinant Human ADP-ribosylation factor 6; ARF6 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-175aa; Full Length
• Sequence: MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS
• Sequence Length: 175

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for ARF6 recombinant protein

GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase

Product Categories/Family for ARF6 recombinant protein

Developmental Biology

References

Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells.Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.J. Biol. Chem. 266:2772-2777(1991) Sequence, genomic organization, and expression of the human ADP-ribosylation factor 6 (ARF6) gene a class III ARF.Lebeda R.A., Johnson S.K., Stewart M.I., Haun R.S.DNA Cell Biol. 22:737-741(2003) Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning.Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org) .Puhl H.L. III, Ikeda S.R., Aronstam R.S. Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3) /Arfophilin-1.Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S.Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane.Hofmann I., Thompson A., Sanderson C.M., Munro S.Curr. Biol. 17:711-716(2007) Molecular characterization of Rab11-FIP3 binding to ARF GTPases.Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D., Holmes R.K., Prekeris R.Eur. J. Cell Biol. 86:417-431(2007) Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta.Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.Traffic 8:1080-1092(2007) ASAP3 is a focal adhesion-associated Arf GAP that functions in cell migration and invasion.Ha V.L., Bharti S., Inoue H., Vass W.C., Campa F., Nie Z., de Gramont A., Ward Y., Randazzo P.A.J. Biol. Chem. 283:14915-14926(2008) TBC1D24, an ARF6-interacting protein, is mutated in familial infantile myoclonic epilepsy.Falace A., Filipello F., La Padula V., Vanni N., Madia F., De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F., Minetti C., Benfenati F., Fassio A., Zara F.Am. J. Hum. Genet. 87:365-370(2010) AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.Wan T., Liu T., Zhang H., Tang S., Min W.J. Biol. Chem. 285:3750-3757(2010) A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components.Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.J. Biol. Chem. 285:31616-31633(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a.Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.Traffic 13:82-93(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity.Menetrey J., Macia E., Pasqualato S., Franco M., Cherfils J.Nat. Struct. Biol. 7:466-469(2000) The structural GDP/GTP cycle of human Arf6.Pasqualato S., Menetrey J., Franco M., Cherfils J.EMBO Rep. 2:234-238(2001) Structural basis for the activation of cholera toxin by human ARF6-GTP.O'Neal C.J., Jobling M.G., Holmes R.K., Hol W.G.Science 309:1093-1096(2005) NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6) .Gizachew D., Oswald R.FEBS Lett. 580:4296-4301(2006) The structural basis of Arf effector specificity the crystal structure of ARF6 in a complex with JIP4.Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F., England P., Franco M., Chavrier P., Houdusse A., Menetrey J.EMBO J. 28:2835-2845(2009) The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory mechanism.Ismail S.A., Vetter I.R., Sot B., Wittinghofer A.Cell 141:812-821(2010) The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold.Selyunin A.S., Sutton S.E., Weigele B.A., Reddick L.E., Orchard R.C., Bresson S.M., Tomchick D.R., Alto N.M.Nature 469:107-111(2011) Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses.Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.Cell 150:1029-1041(2012) Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors.Malaby A.W., van den Berg B., Lambright D.G.Proc. Natl. Acad. Sci. U.S.A. 110:14213-14218(2013)

NCBI and Uniprot Product Information

• NCBI GI #: 4502211
• NCBI GeneID: 382
• NCBI Accession #: NP_001654.1
• NCBI GenBank Nucleotide #: NM_001663.3
• UniProt Accession #: P62330; P26438; Q6FGZ2
• Molecular Weight: 36.1 kDa
• NCBI Official Full Name: ADP-ribosylation factor 6
• NCBI Official Synonym Full Names: ADP ribosylation factor 6
• NCBI Official Symbol: ARF6
• NCBI Protein Information: ADP-ribosylation factor 6
• UniProt Protein Name: ADP-ribosylation factor 6
• Protein Family: Auxin response factor
• UniProt Gene Name: ARF6
• UniProt Entry Name: ARF6_HUMAN

NCBI Description

This gene encodes a member of the human ARF gene family, which is part of the RAS superfamily. The ARF genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The product of this gene is localized to the plasma membrane, and regulates vesicular trafficking, remodelling of membrane lipids, and signaling pathways that lead to actin remodeling. A pseudogene of this gene is located on chromosome 7. [provided by RefSeq, Jul 2008]

Uniprot Description

ARF6: GTP-binding protein involved in protein trafficking; regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in the regulation of dendritic spine development. Contributes to the regulation of dendritic branching and filopodia extension. Interacts with ARHGAP21, ASAP2, HERC1, PIP5K1C and UACA. Interacts with NCS1/FREQ at the plasma membrane. Interacts with RAB11FIP3 and RAB11FIP4. Interacts with USP6 (via Rab-GAP TBC domain). Interacts with ECM29. Interacts with TBC1D24. Belongs to the small GTPase superfamily. Arf family.

Protein type: G protein, monomeric; G protein, monomeric, ARF; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 14q21.3

Cellular Component: cell cortex; cleavage furrow; early endosome; endocytic vesicle; endosome; filopodium membrane; focal adhesion; Golgi apparatus; membrane; midbody; myelin sheath; plasma membrane; recycling endosome membrane; ruffle

Molecular Function: GTP binding; GTPase activity; protein binding; protein N-terminus binding; thioesterase binding

Biological Process: cell adhesion; cell cycle; cell division; cell motility; cortical actin cytoskeleton organization and biogenesis; liver development; myeloid cell apoptosis; negative regulation of receptor-mediated endocytosis; positive regulation of actin filament polymerization; protein transport; regulation of filopodium formation; regulation of Rac protein signal transduction; ruffle organization and biogenesis; small GTPase mediated signal transduction; vesicle-mediated transport