|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||74447 Da|
|Homology||Human, mouse, rat - 14/15 amino acid residues identical.|
|Other Names||Pannexin-2, PANX2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)EEPIY(S)YTPHNFTRD, corresponding to amino acid residues 76-90 of human Pannexin 2 (Accession Q96RD6). 1st extracellular loop.|
|Peptide Confirmation||Confirmed by mass-spectrography and 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, 0.05% 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.
Gap junctions are usually found in clusters and enable intercellular communication by allowing the passage of small molecules between cells1. They play important roles in different biological processes. These include differentiation, cell cycle synchronization, cellular development, neuronal activity and the immune response2-4. Proteins involved in gap junction formation are composed of four transmembrane domains, 2 extracellular loops and one intracellular loop and intracellular N- and C-termini5,6. Several consensus cysteine residues are in the extracellular loop and are essential and necessary for intercellular docking of gap junction hemichannels in the opposing cell membrane5-7. Pannexins (Pannexin 1, Pannexin 2 and Pannexin 3) belong to the superfamily of gap junction proteins. Pannexin 1 (PANX1) is ubiquitously expressed, Pannexin 2 (PANX2) is specifically expressed in the human brain and widespread in rodents and Pannexin 3 (PANX3) is also detected in the brain8. The gating properties of Pannexins were studied in Xenopus oocytes and results demonstrate that only PANX1 is able to form homomeric hemichannels, and is also able to form heteromeric hemichannels with PANX2 but not with PANX39,10. Not surprising, PANX1 gating properties depend whether it forms homomeric or heteromeric hemichannels. A number of different stimuli are known to open these channels and include mechanical stress, extracellular ATP, increases in intracellular Ca2+ and inflammation9. Possible roles for Pannexins include paracrine signaling in vascular endothelial cells and taste cell signaling9. Abgent is pleased to offer a highly specific antibody directed against an epitope of human Pannexin 2. Anti-Pannexin 2 (extracellular) antibody (#AG1316) can be used in western blot analysis and immunocytochemistry applications and was designed to recognize PANX2 from rat, mouse and human samples.
References 1. Chew, S.S.L. et al. (2010) Exp. Neurol. 225, 250. 2. Nakagawa, S. et al. (2010) Curr. Opin. Struct. Biol. 20, 423. 3. Trexter, E.B. et al. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 5836. 4. Hu, X. et al. (2006) Biophys. J. 90, 140. 5. Shestopalov, V.I. and Panchin, Y. (2008) Cell. Mol. Life Sci. 65, 376. 6. Unger, V.M. et al. (1999) Science 283, 1176. 7. Falk, MM. (2000) Eur. J. Cell. Biol. 79, 564. 8. Panchin, Y.V. (2005) J. Exp. Biol. 208, 1415. 9. Litvin, O. et al. (2006) J. Cell. Mol. Med. 10, 613. 10. Bruzzone, R. et al. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 13664.
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