Bestrophin 1 Antikörper (3rd Extracellular Loop)
Kurzübersicht für Bestrophin 1 Antikörper (3rd Extracellular Loop) (ABIN7884788)
Target
Alle Bestrophin 1 (BEST1) Antikörper anzeigenReaktivität
Wirt
Klonalität
Konjugat
Applikation
Güteklasse
-
-
Bindungsspezifität
- 3rd Extracellular Loop, AA 259-270
-
Verwendungszweck
- A Rabbit Polyclonal Antibody to Bestrophin-1 Channel
-
Homologie
- Rat - 10, human - 9,12 amino acid residues identical
-
Aufreinigung
- Affinity purified on immobilized antigen.
-
Immunogen
- (C)NPNKDYPGHEMD, corresponding to amino acid residues 259-270 of mouse Bestrophin-1
-
Isotyp
- IgG
-
-
-
-
Applikationshinweise
-
WB: 1:200
FC: 1:20
ICC: The optimal concentration should be determined by the user
IHC: 1:100
IP: The optimal concentration should be determined by the user
-
Kommentare
-
Negative Control: (ABIN7234856)
-
Beschränkungen
- Nur für Forschungszwecke einsetzbar
-
-
-
Format
- Lyophilized
-
Rekonstitution
- 0.2 mL double distilled water (DDW)
-
Konzentration
- 1 mg/mL
-
Buffer
- PBS pH 7.4
-
Konservierungsmittel
- Without preservative
-
Lagerung
- -20 °C
-
Informationen zur Lagerung
- The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C
-
-
- Bestrophin 1 (BEST1)
-
Andere Bezeichnung
- BEST1
-
Hintergrund
-
Synonyms: BEST1, Vitelliform macular dystrophy protein 2, VMD2, BMD1
Description: 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 (γ-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)1,2. 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 vision3. To date Bestrophin 1-4 have been identified, although Bestrophin-3 and Bestrophin-4 have been observed only at the RNA level3. In addition, splice variants of some of these Ca2+-activated Cl- channels (CaCCs) have also been detected2,4,5. 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 situ6. Bestrophin-1 is also detected in retina, brain, spinal cord and testes7.Two different topologies for Bestrophin-1 have been proposed. The first, the preferred structure, proposes that six hydrophobic domains span the membrane8, while the second suggests that there are only four membrane-spanning domains9. 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+ 10, providing additional evidence that Bestrophin-1 is activated by direct binding of Ca2+ to the channel11,12.Bestrophin-1 has been found to release glutamate from astrocytes and is located at microdomains near synapses13.
-
Gen-ID
- 24115
-
UniProt
- O88870
Target
-