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Recombinant Human Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1), partial

Recombinant Human Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1), partial

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MSDS	MSDS
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

GBF1

Uniprot NO.

Q92538

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-1859

Target Protein Sequence

MVDKNIYIIQ GEINIVVGAI KRNARWSTHT PLDEERDPLL HSFGHLKEVL NSITELSEIE PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP THEGTAEGME NMADAVTHAR FVGTDPASDE VVLMKILQVL RTLLLTPVGA HLTNESVCEI MQSCFRICFE MRLSELLRKS AEHTLVDMVQ LLFTRLPQFK EEPKNYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM TKVTPGSELP TPNGTTLSSN LTGGMPFIDV PTPISSASSE AASAVVSPST DSGLEFSSQT TSKEDLTDLE QPGSPGYSTA TEPGSSELGV PEQPDLQEGT HVEKSQSASV ESIPEVLEEC TSPADHSDSA SVHDMDYVNP RGVRFTQSSQ KEGTALVPYG LPCIRELFRF LISLTNPHDR HNSEVMIHMG LHLLTVALES APVAQCQTLL GLIKDEMCRH LFQLLSIERL NLYAASLRVC FLLFESMREH LKFQMEMYIK KLMEIITVEN PKMPYEMKEM ALEAIVQLWR IPSFVTELYI NYDCDYYCSN LFEELTKLLS KNAFPVSGQL YTTHLLSLDA LLTVIDSTEA HCQAKVLNSL TQQEKKETAR PSCEIVDGTR EASNTERTAS DGKAVGMASD IPGLHLPGGG RLPPEHGKSG CSDLEEAVDS GADKKFARKP PRFSCLLPDP RELIEIKNKK KLLITGTEQF NQKPKKGIQF LQEKGLLTIP MDNTEVAQWL RENPRLDKKM IGEFVSDRKN IDLLESFVST FSFQGLRLDE ALRLYLEAFR LPGEAPVIQR LLEAFTERWM NCNGSPFANS DACFSLAYAV IMLNTDQHNH NVRKQNAPMT LEEFRKNLKG VNGGKDFEQD ILEDMYHAIK NEEIVMPEEQ TGLVRENYVW NVLLHRGATP EGIFLRVPTA SYDLDLFTMT WGPTIAALSY VFDKSLEETI IQKAISGFRK CAMISAHYGL SDVFDNLIIS LCKFTALSSE SIENLPSVFG SNPKAHIAAK TVFHLAHRHG DILREGWKNI MEAMLQLFRA QLLPKAMIEV EDFVDPNGKI SLQREETPSN RGESTVLSFV SWLTLSGPEQ SSVRGPSTEN QEAKRVALEC IKQCDPEKMI TESKFLQLES LQELMKALVS VTPDEETYDE EDAAFCLEML LRIVLENRDR VGCVWQTVRD HLYHLCVQAQ DFCFLVERAV VGLLRLAIRL LRREEISAQV LLSLRILLLM KPSVLSRVSH QVAYGLHELL KTNAANIHSG DDWATLFTLL ECIGSGVKPP AALQATARAD APDAGAQSDS ELPSYHQNDV SLDRGYTSDS EVYTDHGRPG KIHRSATDAD VVNSGWLVVG KDDVDNSKPG PSRPGPSPLI NQYSLTVGLD LGPHDTKSLL KCVESLSFIV RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQEKRGKSH KYDSKGNRFK KKSKEGSMLR RPRTSSQHAS RGGQSDDDED EGVPASYHTV SLQVSQDLLD LMHTLHTRAA SIYSSWAEEQ RHLETGGQKI EADSRTLWAH CWCPLLQGIA CLCCDARRQV RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL LENISPADVG GMEETRMRAS TLLSKVFLQH LSPLLSLSTF AALWLTILDF MDKYMHAGSS DLLSEAIPES LKNMLLVMDT AEIFHSADAR GGGPSALWEI TWERIDCFLP HLRDELFKQT VIQDPMPMEP QGQKPLASAH LTSAAGDTRT PGHPPPPEIP SELGACDFEK PESPRAASSS SPGSPVASSP SRLSPTPDGP PPLAQPPLIL QPLASPLQVG VPPMTLPIIL NPALIEATSP VPLLATPRPT DPIPTSEVN

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Description

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Target Background

Function

Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP. Recruitment to cis-Golgi membranes requires membrane association of Arf-GDP and can be regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat complex to the endoplasmic reticulum exit sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi compartments which implicates ARF1 activation. Involved in COPI vesicle-dependent retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER). Involved in the trans-Golgi network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1 adapter protein complex related to chlathrin-dependent transport; the function requires its GEF activity (probably at least in part on ARF4 and ARF5). Has GEF activity towards ARF1. Has in vitro GEF activity towards ARF5. Involved in the processing of PSAP. Required for the assembly of the Golgi apparatus. The AMPK-phosphorylated form is involved in Golgi disassembly during mitotis and under stress conditions. May be involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid droplets; however, this function is under debate. In neutrophils, involved in G protein-coupled receptor (GPCR)-mediated chemotaxis und superoxide production. Proposed to be recruited by phosphatidylinositol-phosphates generated upon GPCR stimulation to the leading edge where it recruits and activates ARF1, and is involved in recruitment of GIT2 and the NADPH oxidase complex. Plays a role in maintaining mitochondrial morphology.

Gene References into Functions

Experiments confirmed that GBF1 is required for hepatitis E virus replication. PMID:29112323
Study provides evidence that GBF-1 is required in endoplasmic reticulum structure and endosomal traffic. PMID:23840591
GBF1 could regulate different metabolic pathways through the activation of different pairs of Arf proteins. PMID:26814617
Oligomerization appears to stabilize GBF1 in cells. PMID:26718629
GBF1 plays a critical role early in dengue infection that is independent of its role in the maintenance of Golgi structure. PMID:24855065
The role of GBF1 in poliovirus replication is independent of its Arf activating function. PMID:25653442
Although human rhinovirus 3A protein was previously shown to interact with ACBD3, these data suggest that PI4KIIIbeta recruitment occurred independently of both GBF1 and ACBD3. PMID:25410869
GBF1 causes increased Arf-GTP production at the Golgi, consistent with a feed-forward self-limiting mechanism of Arf activation. PMID:24213530
These data suggest that AMPK-GBF1-Arf1 signaling is involved in the regulation of Golgi fragmentation during mitosis. PMID:23418352
an early acting GEF (GBF1) activates ARFs that mediate recruitment of late acting GEFs (BIG1/2) to coordinate coating events within the pre-Golgi/Golgi/TGN continuum. PMID:23386609
GBF1-mediated Arf1 activation is necessary to unify cell polarity during chemotaxis PMID:22573891
the vesicular transport proteins ARF1 and GBF1 colocalized with PI4KIIIbeta and were both required for HCV replication PMID:22359663
The GBF1 participated in delivery of adipose triglyceride lipase (ATGL) onto the lipid droplets(LD) surface PMID:22185782
We hypothesize that sphingomyelin acquired by CERT-dependent transport of ceramide and subsequent conversion to SM is necessary for C. trachomatis replication whereas SM acquired by GBF1-dependent pathway is essential for inclusion growth and stability. PMID:21909260
The COG (conserved oligomeric Golgi) complex plays a role in the localization, but not membrane association of GBF1. PMID:21722633
GBF1 and ATGL interact directly and in cells, through multiple contact sites on each protein. PMID:21789191
The brefeldin A block of poliovirus replication is rescued by expression of only the N-terminal region of GBF1 lacking the Sec7 domain. PMID:20497182
COPII is the only coat required for sorting and export from the endoplasmic reticulum exit sites, whereas GBF1, but not BIGs, is required for COPI recruitment, Golgi subcompartmentalization, and cargo progression to the cell surface. PMID:18003980
Both human and canine GBF1 can be inhibited by compound LG186, a small molecule derived from Exo2, a small molecule inhibitor of secretion and Shiga toxin cytotoxicity. PMID:20854417
Data suggest that Rab1 contributes to the specificity and timing of GBF1 recruitment by activating PI4KIIIalpha, and that the PtdIns(4)P produced then allows GBF1 to bind to Golgi membranes and activate Arf1. PMID:20530568
The authors demonstrate that Rab1b-activated GBF1 and ARF1 are involved in Ebolavirus virion formation, suggesting that both the COPII and COPI transport systems play a role in Ebolavirus VP40-mediated particle formation. PMID:20164217
Data propose that the phosphorylation and membrane dissociation of GBF1 and the consequent reduction in ARF-GTP levels in mitosis are important for changes in Golgi dynamics PMID:20175751
GBF1 is a cellular factor required for HCV infection. PMID:19906930
detailed subcellular localization to the cis-Golgi PMID:12047556
novel interaction between p115 and Golgi-specific brefeldin-A-resistant factor 1 (GBF1) PMID:12634853
characterization of alternatively spliced and truncated forms of GBF1 defines regions important for activity PMID:12646181
an Arf1-GBF1-Brefeldin A complex is formed and has a longer residence time on Golgi membranes than GBF1 or Arf1 alone PMID:15616190
A continuous cycle of recruitment and dissociation of GBF1 to membranes is required for sustained ARF activation and COP I recruitment that underlies ER-Golgi traffic. PMID:15813748
GBF1 is recruited to the endogenous IRF-9 promoter, and interacts with C/EBP-beta, IL-1, and IL-6 PMID:16318580
These observations strongly suggest that GBF1 regulates COPI membrane recruitment in the early secretory pathway. PMID:16926190
Two different poliovirus proteins independently recruit different Arf GEFs (GBF1 and BIG1/2) to membranes as part of cellular pathways utilized by the virus to form its membranous replication complex. PMID:17079330
analysis of the binding domain in GBF1 showed that the extreme N terminus, the dimerization/cyclophilin binding domain, and the homology upstream of Sec7 domain are required for the interaction with coxsackievirus protein 3A PMID:17329336
These data support a model where Rab1b-GTP induces GBF1 recruitment at the ERES interface and at the Golgi complex where it is required for COPII/COPI exchange or COPI vesicle formation, respectively. PMID:17429068
Required for GGA adaptor protein recruitment to Golgi membranes; plays a role in the proper processing and sorting of lysosomal cargo. PMID:17666033
These findings suggest that a secretory pathway capable of trafficking soluble proteins can be maintained in cells in which COPI recruitment is compromised by GBF1 depletion. PMID:17956946
GBF1 is a AMPK substrate and AMPK-mediated phosphorylation of GBF1 at Thr(1337) has a critical role, presumably by attenuating function of GBF1, in disassembly of the Golgi apparatus induced under stress conditions that lower the intracellular ATP PMID:18063581
Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1. PMID:18287014
GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1 PMID:18524849
siRNAs demonstrate that GBF1-mediated ARF1 activation is required for efficient MHV RNA replication PMID:18551169
AG1478 inhibits GBF1, a large nucleotide exchange factor for the ADP-ribosylation factor, in a Sec7 domain-dependent manner and mimics the phenotype of a GBF1 mutant that has an inactive mutation PMID:18799457
GBF1 is responsible for the sensitivity of poliovirus infection to BFA, and is required for virus replication PMID:19023417
crucial for coxsackievirus B3 RNA replication PMID:19740986

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Subcellular Location

Golgi apparatus, cis-Golgi network. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, trans-Golgi network. Golgi apparatus. Cytoplasm. Lipid droplet. Membrane; Peripheral membrane protein.

Tissue Specificity

Ubiquitous.

Database Links

HGNC: 4181

UNIGENE: Hs.290243

KEGG: hsa:8729

STRING: 9606.ENSP00000359000

OMIM: 603698

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