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anti-Human ARFGEF1 Antikörper:
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Human Polyclonal ARFGEF1 Primary Antibody für ICC, IF - ABIN251713
Goueslain, Alsaleh, Horellou, Roingeard, Descamps, Duverlie, Ciczora, Wychowski, Dubuisson, Rouillé: Identification of GBF1 as a cellular factor required for hepatitis C virus RNA replication. in Journal of virology 2009
Human Polyclonal ARFGEF1 Primary Antibody für ICC, IF - ABIN4281376
Christis, Munro: The small G protein Arl1 directs the trans-Golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2. in The Journal of cell biology 2012
The findings provide structural insight into how Arf1 GEFs, and hence active Arf1, achieve their correct subcellular distribution.
The data demonstrate a novel and unexpected function of BIG1 that regulates TNFR1 signaling by targeting TRAF2.
Both phospholipase D activity and vesicular trafficking were required for effects of BIG1 and BIG2 on beta-catenin activation. Levels of PKA-phosphorylated beta-catenin S675 and beta-catenin association with PKA, BIG1, and BIG2 were also diminished after BIG1/BIG2 depletion.
Arf guanine nucleotide-exchange factors BIG1 and BIG2 regulate nonmuscle myosin IIA activity by anchoring myosin phosphatase complex.
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.
BIG1, through its ability to activate ADP-ribosylation factor 1, regulates cell-surface levels and function of ABCA1.
BIG1 and KANK1 play roles in regulating cell polarity during directed migration in wound healing.
Promoter methylations of CAMK2B and ARFGEF1 are novel epigenetic markers identified in breast cancer cell lines.
BIG1 binds to FKBP13, playing a role in vesicular trafficking
data are consistent with independent intracellular movements and actions of BIG1 and BIG2, and they are also evidence of the participation of BIG1 in both Golgi and nuclear functions
myosin IXb binds to BIG1, which regulates its Rho-GTPase activating protein activity
Two critical elements of BIG1 molecular structure were identified, as well as the potential function of microtubules in a novel PKA effect on BIG1 translocation.
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.
results indicate a previously unrecognized role for BIG1 in the glycosylation of beta1 by Golgi enzymes, which is critical for its function in developmental and other vital cell processes
Phosphorylation of BIG1 and BIG2 via PKA and protein phosphatase 1gamma effects vesicular trafficking via alterations in ARF activation.
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.
Evidence that BIG1 and nucleolin, but not fibrillarin, can be present with p62 at the nuclear envelope confirms the presence of BIG1 and nucleolin in dynamic molecular complexes that change in composition while moving through nuclei
These observations indicate that BIG2 and BIG1 play redundant roles in trafficking between the trans-Golgi network and endosomes that involves the AP-1 complex.
Overexpression of full-length KIF21A and BIG1 and their fragments in HEK293 cells followed by reciprocal IP revealed that the C-terminal tail of KIF21A, with seven WD-40 repeats, may interact with structure in the C-terminal region of BIG1.
ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP. It contains a Sec7 domain, which may be responsible for guanine-nucleotide exchange activity and also brefeldin A inhibition.
ADP-ribosylation factor guanine nucleotide-exchange factor 1(brefeldin A-inhibited)
, brefeldin A-inhibited guanine nucleotide-exchange protein 1
, p200 ARF guanine nucleotide exchange factor
, brefeldin A-inhibited GEP 1
, p200 ARF-GEP1
, ADP-ribosylation factor guanine nucleotide-exchange factor 1