|Calculated MW||63684 Da|
|Homology||Rat - 10/12 amino acid residues identical; human - 9/12 amino acid residues identical.|
|Other Names||Bestrophin-1, Vitelliform macular dystrophy protein 2 homolog, Best1, Bmd1, Vmd2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)NPNKDYPGHEMD, corresponding to amino acid residues 259-270 of mouse Bestrophin-1 (Accession O88870).ֲ ֲ 3rd extracellular loop.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
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. Abgent is pleased to offer a highly specific antibody directed against an epitope located at the 3rd extracellular loop of mouse Bestrophin-1. Anti-Bestrophin-1 (extracellular) antibody (#AG1371) can be used in western blot and immunohistochemical and indirect flow cytometry applications, and has been designed to recognize Bestrophin-1 channel from mouse, rat and human samples.
References 1. Men, G. et al. (2004) Am. J. Ophtalmol. 137, 963. 2. Petrukhin, K. et al. (1998) Nat. Genet. 19, 241. 3. Hartzell, C.H. et al. (2008) Physiol. Rev. 88, 639. 4. Kramer, F. et al. (2004) Cytogen. Genome Res. 105, 107. 5. Stohr, H et al. (2002) Eur. J. Hum. Genet. 10, 281. 6. Park, H. et al. (2009) J. Neurosci. 29, 13063. 7. Marmostein, A.D. et al. (2009) Prog Retin Eye Res. 28, 206. 8. Tsunenari, T. et al. (2003) J. Biol. Chem. 278, 41114. 9. Milenkovic, V.M. et al. (2007) J. Biol. Chem. 282, 1313. 10. Xiao, Q. et al. (2008) J. Gen. Physiol. 132, 681. 11. Chien, L.T. et al. (2006) J. Gen. Physiol. 128, 247. 12. Tsunenari, T. et al. (2006) J. Gen. Physiol. 127, 749. 13. Woo, D.H. et al. (2012) Cell 151, 25.
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