Endophilin I rabbit pAb
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Endophilin I rabbit pAb
Background :
Domain:An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface., function:Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature., miscellaneous:HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation., similarity:Belongs to the endophilin family., similarity:Contains 1 BAR domain., similarity:Contains 1 SH3 domain., subcellular location:Concentrated in presynaptic nerve terminals in neurons., subunit:Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity) . Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with PDCD6IP., tissue specificity:Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.Description :
Domain: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface. function: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. miscellaneous: HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation. similarity: Belongs to the endophilin family. similarity: Contains 1 BAR domain. similarity: Contains 1 SH3 domain. subcellular location: Concentrated in presynaptic nerve terminals in neurons. subunit: Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with PDCD6IP. tissue specificity: Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.Product Name Alternative :
SH3GL2; CNSA2; SH3D2A; Endophilin-A1; EEN-B1; Endophilin-1; SH3 domain protein 2A; SH3 domain-containing GRB2-like protein 2UniProt :
Q99962Swiss Prot :
Q99962Reactivity :
Human; Mouse; RatImmunogen :
Synthesized peptide derived from Endophilin I . at AA range: 30-110Target :
Endophilin IClonality :
PolyclonalSource :
RabbitApplications :
WB; ELISAConcentration :
1 mg/mlDilution :
Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications.Buffer :
-20°C/1 yearMolecular Weight :
39kDStorage Conditions :
-20°C/1 yearObserved Molecular Weight :
39kDFragment :
IgGSubcellular Location :
Cytoplasm . Membrane ; Peripheral membrane protein . Early endosome . Cell junction, synapse, presynapse .Other Product Names :
SH3GL2; CNSA2; SH3D2A; Endophilin-A1; EEN-B1; Endophilin-1; SH3 domain protein 2A; SH3 domain-containing GRB2-like protein 2Gene ID (Human) :
6456

