Recombinant Human Arfaptin-1 protein is a Human Full Length protein, in the 1 to 341 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M A Q E S P K N S A A E I P V T S N G E V D D S R E H S F N R D L K H S L P S G L G L S E T Q I T S H G F D N T K E G V I E A G A F Q G G Q R T Q T K S G P V I L A D E I K N P A M E K L E L V R K W S L N T Y K C T R Q I I S E K L G R G S R T V D L E L E A Q I D I L R D N K K K Y E N I L K L A Q T L S T Q L F Q M V H T Q R Q L G D A F A D L S L K S L E L H E E F G Y N A D T Q K L L A K N G E T L L G A I N F F I A S V N T L V N K T I E D T L M T V K Q Y E S A R I E Y D A Y R T D L E E L N L G P R D A N T L P K I E Q S Q H L F Q A H K E K Y D K M R N D V S V K L K F L E E N K V K V L H N Q L V L F H N A I A A Y F A G N Q K Q L E Q T L K Q F H I K L K T P G V D A P S W L E E Q
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network (PubMed:22981988). Mechanistically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold (PubMed:22981988, PubMed:9038142). Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs (PubMed:22981988). In turn, ARFs induce fission (PubMed:22981988). Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells (PubMed:22981988).
Arfaptin-1, ADP-ribosylation factor-interacting protein 1, ARFIP1
Recombinant Human Arfaptin-1 protein is a Human Full Length protein, in the 1 to 341 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 7.4
Constituents: 69% PBS, 30% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab187475 was purified using conventional chromatography techniques.
Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network (PubMed:22981988). Mechanistically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold (PubMed:22981988, PubMed:9038142). Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs (PubMed:22981988). In turn, ARFs induce fission (PubMed:22981988). Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells (PubMed:22981988).
Phosphorylated by PRKD1; phosphorylation delocalizes ARFIP1 from the Golgi and disrupts its ability to inhibit the activity of ADP-ribosylation factor, an important component of the vesicle scission machinery.
Arfaptin-1 also known as ARFIP1 acts mechanically by modulating membrane dynamics and cell signaling. This protein with a mass of approximately 36 kDa associates with membranes through a BAR domain which induces curvature. It interacts with small GTPases including ARF and Rac1 to facilitate various intracellular trafficking processes. Arfaptin-1 expression occurs in multiple tissue types suggesting its wide role in cellular functions.
Arfaptin-1 plays a part in intracellular transport and membrane receptor regulation. It is also recognized as a component of larger protein complexes contributing to the reorganization of actin cytoskeleton. Through its interactions with GTPases Arfaptin-1 influences endocytosis and exocytosis affecting cell surface receptor turnover. This adaptability allows it to play important roles in cellular communication and response to environmental stimuli.
Arfaptin-1 is integral in cellular trafficking and signal transduction pathways. It is involved in the ARF small GTPase pathway influencing vesicle formation and trafficking. Arfaptin-1 also interacts with other proteins like Rac1 in the regulation of actin dynamics impacting the actin cytoskeleton remodeling pathway. These interactions highlight its central position in coordinating cellular architecture and material transport.
Arfaptin-1 involvement links to conditions like cancer and neurological disorders. Altered expression of Arfaptin-1 has been observed in cancer cells where it affects cell migration and invasion linking with other proteins such as Rac1. In neurological disorders abnormal Arfaptin-1 function disrupts synaptic vesicle trafficking potentially interacting with proteins involved in neurodegenerative diseases. These associations emphasize its potential as a target in therapeutic strategies.
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15% SDS-PAGE analysis of 3 μg ab187475.
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