
BIG1 Polyklonale Antilichaam, AbBy FluorTM 555 Vervoeging
Kwaliteit
ISO Gecertificeerd
Levering
24-48 uur
Technische Specificaties
Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.
ADPribosylation factor guanine nucleotide exchange factor 1brefeldin A inhibited; ARFGEF1; ARFGEP1; Brefeldin A inhibited GEP 1; Brefeldin A inhibited guanine nucleotide exchange protein 1; p200 ARF GEP1; p200 ARF guanine nucleotide exchange factor; BIG1_HUMAN.
10565
Cytoplasm, Nucleus, Cell membrane
• Rabbit
Mouse
1-200/1849
BIG1
• Polyclonal
• IgG
AbBy Fluor™ 555
KLH conjugated synthetic peptide derived from human BIG1/ARFGEF1
WB, IF (IHC-P), IF (IHC-F), IF (ICC)
Purified by Protein A.
553nm/568nm
1µg/µl
WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)
Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Unmodified
Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.
10565
Human, Rat, Dog, Cow, Sheep, Pig, Chicken
Beschrijving
BIG1 Polyklonale Antilichaam, AbBy FluorTM 555 Vervoeging Beschikbaar in 100 µL. Bestel eenvoudig online met snelle levering.
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