BD-PT1559

Endophilin I Rabbit Polyclonal Antibody

SH3GL2; CNSA2; SH3D2A; Endophilin-A1; EEN-B1; Endophilin-1; SH3 domain protein 2A; SH3 domain-containing GRB2-like protein 2

常规抗体

SH3GL2

Endophilin-A1

WB

Human,Mouse,Rat

1 mg/ml

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.

6456

http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=6456

Q99962

http://www.uniprot.org/uniprotkb/Q99962/entry

20404

http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=20404

Q62420

http://www.uniprot.org/uniprot/Q62420

116743

http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=116743

O35179

http://www.uniprot.org/uniprot/O35179

Synthesized peptide derived from Endophilin I . at AA range: 30-110

Endophilin I Polyclonal Antibody detects endogenous levels of Endophilin I protein.

WB 1:500 - 1:2000. ELISA: 1:10000. Not yet tested in other applications.

39kD

-20°C/1 year

Polyclonal, Rabbit,IgG

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.,

Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.

Cytoplasm . Membrane ; Peripheral membrane protein . Early endosome . Cell junction, synapse, presynapse .

Endocytosis;

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.,

现货

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.