|Calculated MW||57023 Da|
|Homology||Rat - identical; human - 11/12 amino acid residues identical.|
|Other Names||Bestrophin-2, Vitelliform macular dystrophy 2-like protein 1, Best2, Vmd2l1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DPAQGYKDHTLD, corresponding to amino acid residues 259-270 of mouse Bestrophin-2 (Accession Q8BGM5). 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 dystrophy1,2. 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. However, the molecular identity and functional role of CaCC in the brain have not been well established6. Bestrophin-2 is prominently expressed in colon and testes. Recently, Bestrophin-2 has also been found to be expressed in olfactory sensory neurons (OSNs)7. Two different topologies for Bestrophin-1 have been proposed. The first structure proposes that six hydrophobic domains span the membrane8, while the second suggests that there are only four membrane-spanning domains9. The same structural controversy applies to Bestrophin-2. Bestrophin-1 and Bestrophin-2 (as well as Bestrophin-4 by heterologous expression) are activated by intracellular Ca2+ 10-12. Ca2+-dependent activation of Bestrophin-2 was also demonstrated in Xenopus13. Abgent is pleased to offer a highly specific antibody directed against an epitope located at the 3rd extracellular loop of mouse Bestrophin-2. Anti-Bestrophin-2 (extracellular) antibody (#AG1370) can be used in western blot and immunohistochemical applications, and has been designed to recognize Bestrophin-2 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. Pifferi, S. et al. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 12929. 8. Tsunenari, T. et al. (2003) J. Biol. Chem. 278, 41114. 9. Milenkovic, V.M. et al. (2007) J. Biol. Chem. 282, 1313. 10. Xia, 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. Qu, Z. et al. (2003) J. Biol. Chem. 278, 49563.
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