ADP-ribosylation factor 4 Recombinant Protein | ARF2 recombinant protein

Recombinant Human ADP-ribosylation factor 4 protein

Cat. Num. AAA717258

• Gene Names: ARF4; ARF2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: ADP-ribosylation factor 4; Recombinant Human ADP-ribosylation factor 4 protein; ARF2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-180
• Sequence: MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDRIRPLWKHYFQNTQGLIFVVDSNDRERIQEVADELQKMLLVDELRDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR
• Sequence Length: 180

• 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 ARF2 recombinant protein

GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.

Product Categories/Family for ARF2 recombinant protein

Transport

References

Selective amplification of an mRNA and related pseudogene for a human ADP-ribosylation factor, a guanine nucleotide-dependent protein activator of cholera toxin.Monaco L., Murtagh J.J. Jr., Newman K.B., Tsai S.-C., Moss J., Vaughan M.Proc. Natl. Acad. Sci. U.S.A. 87:2206-2210(1990) Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins.Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C.J. Biol. Chem. 266:2606-2614(1991) Cloning and characterization of the human ADP-ribosylation factor 4 gene.Lebeda R.A., Haun R.S.Gene 237:209-214(1999) 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) 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) 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 human ADP-ribosylation factor 4.Structural genomics consortium (SGC) Submitted (APR-2005) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 4502205
• NCBI GeneID: 378
• NCBI Accession #: NP_001651.1
• NCBI GenBank Nucleotide #: NM_001660.3
• UniProt Accession #: P18085; P21371; B2R7J7
• Molecular Weight: 47.5 kDa
• NCBI Official Full Name: ADP-ribosylation factor 4
• NCBI Official Synonym Full Names: ADP ribosylation factor 4
• NCBI Official Symbol: ARF4
• NCBI Official Synonym Symbols: ARF2
• NCBI Protein Information: ADP-ribosylation factor 4
• UniProt Protein Name: ADP-ribosylation factor 4
• Protein Family: Auxin response factor
• UniProt Gene Name: ARF4
• UniProt Synonym Gene Names: ARF2
• UniProt Entry Name: ARF4_HUMAN

NCBI Description

This gene is a member of the human ARF gene family whose members 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 gene products include 5 ARF proteins and 11 ARF-like proteins and constitute one family of the RAS superfamily. The ARF proteins are categorized as class I, class II and class III; this gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains six exons and five introns. This gene is the most divergent member of the human ARFs. Conflicting map positions at 3p14 or 3p21 have been reported for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

ARF4: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Belongs to the small GTPase superfamily. Arf family.

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

Chromosomal Location of Human Ortholog: 3p14.3

Cellular Component: cytosol; dendritic spine; Golgi apparatus; membrane

Molecular Function: epidermal growth factor receptor binding; GTP binding; GTPase activity; protein binding

Biological Process: apical protein localization; brain development; cell migration; cellular protein metabolic process; epidermal growth factor receptor signaling pathway; ER to Golgi vesicle-mediated transport; establishment and/or maintenance of epithelial cell polarity; learning; negative regulation of apoptosis; organelle organization and biogenesis; phospholipase D activation; positive regulation of transcription from RNA polymerase II promoter; post-translational protein modification; protein amino acid ADP-ribosylation; protein amino acid N-linked glycosylation via asparagine; protein transport; response to axon injury; small GTPase mediated signal transduction