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50 ul
gene_symbol:Best1
predicted_size:null
Uniprot ID:O8887
description:Rabbit Polyclonal Anti-Bestrophin-1 (extracellular)
clonality:Polyclonal
product_type(primary antibody, secondy antibody ,tag antibody,Loding Control...):Primary Antibodies
background:Mammalian Cl channels can be broadly classified into four different families: voltage-dependent Cl channels (CLCs), the cystic fibrosis transmembrane conductance regulator (CFTR), ligand-gated Cl channels (?-aminobutyric acid (GABA)) and glycine channels) and Ca2+-activated Cl channels (Bestrophin and Anoctamin channels). Bestrophins were first found by genetic linkage of human-Bestrophin-1 (hBest1) to a juvenile form of macular degeneration called Best vitelliform macular dystrophy (BVMD). BVMD is mainly electrophysiologically characterized by a decrease in the light peak and physiologically by the thinning of the retina layer which eventually leads to the loss of central vision. To date Bestrophin 1-4 have been identified, although Bestrophin-3 and Bestrophin-4 have been observed only at the RNA level. In addition, splice variants of some of these Ca2+-activated Cl channels (CaCCs) have also been detected. CaCCs are known to be involved in the regulation of olfaction, taste, phototransduction, and excitability in the nervous system. Recently, Bestrophin-1 was shown to be functionally expressed in astrocytes in both primary cell culture and in situ. Bestrophin-1 is also detected in retina, brain, spinal cord and testes. Two different topologies for Bestrophin-1 have been proposed. The first, the preferred structure, proposes that six hydrophobic domains span the membrane, while the second suggests that there are only four membrane-spanning domains. Bestrophin-1, along with its counterparts, is activated by intracellular Ca2+. A recent study demonstrated that Bestrophin-1 indeed binds Ca2+ and by mutating specific residues, showed which amino acid residues are essential for binding Ca2+, providing additional evidence that Bestrophin-1 is activated by direct binding of Ca2+ to the channel. Bestrophin-1 has been found to release glutamate from astrocytes and is located at microdomains near synapses.
immunogen:Peptide (C)NPNKDYPGHEMD, corresponding to amino acid residues 259-270 of mouse Bestrophin-1. 3rd extracellular loop.
recommended_dilution:WB: 1:200-1:2000; IHC: 1:100-1:3,000; FC: 1:50-1:600
predicted_size:null
buffer:Lyophilized. Concentration before lyophilization ~0.8mg/ml (lot dependent, please refer to CoA along with shipment for actual concentration). Buffer before lyophilization: Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.
host_species:Rabbit
applications:FC, IHC, WB
reactivities:Human, Rat
predicted_size:null
Uniprot ID:O8887
description:Rabbit Polyclonal Anti-Bestrophin-1 (extracellular)
clonality:Polyclonal
product_type(primary antibody, secondy antibody ,tag antibody,Loding Control...):Primary Antibodies
background:Mammalian Cl channels can be broadly classified into four different families: voltage-dependent Cl channels (CLCs), the cystic fibrosis transmembrane conductance regulator (CFTR), ligand-gated Cl channels (?-aminobutyric acid (GABA)) and glycine channels) and Ca2+-activated Cl channels (Bestrophin and Anoctamin channels). Bestrophins were first found by genetic linkage of human-Bestrophin-1 (hBest1) to a juvenile form of macular degeneration called Best vitelliform macular dystrophy (BVMD). BVMD is mainly electrophysiologically characterized by a decrease in the light peak and physiologically by the thinning of the retina layer which eventually leads to the loss of central vision. To date Bestrophin 1-4 have been identified, although Bestrophin-3 and Bestrophin-4 have been observed only at the RNA level. In addition, splice variants of some of these Ca2+-activated Cl channels (CaCCs) have also been detected. CaCCs are known to be involved in the regulation of olfaction, taste, phototransduction, and excitability in the nervous system. Recently, Bestrophin-1 was shown to be functionally expressed in astrocytes in both primary cell culture and in situ. Bestrophin-1 is also detected in retina, brain, spinal cord and testes. Two different topologies for Bestrophin-1 have been proposed. The first, the preferred structure, proposes that six hydrophobic domains span the membrane, while the second suggests that there are only four membrane-spanning domains. Bestrophin-1, along with its counterparts, is activated by intracellular Ca2+. A recent study demonstrated that Bestrophin-1 indeed binds Ca2+ and by mutating specific residues, showed which amino acid residues are essential for binding Ca2+, providing additional evidence that Bestrophin-1 is activated by direct binding of Ca2+ to the channel. Bestrophin-1 has been found to release glutamate from astrocytes and is located at microdomains near synapses.
immunogen:Peptide (C)NPNKDYPGHEMD, corresponding to amino acid residues 259-270 of mouse Bestrophin-1. 3rd extracellular loop.
recommended_dilution:WB: 1:200-1:2000; IHC: 1:100-1:3,000; FC: 1:50-1:600
predicted_size:null
buffer:Lyophilized. Concentration before lyophilization ~0.8mg/ml (lot dependent, please refer to CoA along with shipment for actual concentration). Buffer before lyophilization: Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.
host_species:Rabbit
applications:FC, IHC, WB
reactivities:Human, Rat
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Rabbit Polyclonal Anti-Bestrophin-1 (extracellular)
¥11000






