Open Oocyte Perfusion Chamber adapter
Open Oocyte Perfusion Chamber adapter
Description
Oocyte Perfusion Chamber
Low working volume means fast exchange times.
Features:
- Small working volume (< 20µl)
- Fast solution exchange
- 80mm to 120mm diameters
Expression of recombinant receptors in oocytes has been a favorite choice for researchers to assess the pharmacology of recombinant receptors. Since the oocytes are 1-1.5 mm in diameter, however, fast solution exchange around the oocyte was difficult. After several years of electro-physiological research, we have designed a Xenopus oocyte perfusion chamber for use in automated and unattended experiments. Combined with an automated perfusion system, the oocyte chamber allows researchers to obtain dose-response data quickly and easily.
References – Oocyte Perfusion Chamber
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- The Lhs1/GRP170 Chaperones Facilitate the Endoplasmic Reticulum-associated Degradation of the Epithelial Sodium Channel J. Biol. Chem. 2013; 288(25): p. 18366-18380Teresa M. Buck, Lindsay Plavchak, Ankita Roy, Bridget F. Donnelly, Ossama B. Kashlan, Thomas R. Kleyman, Arohan R. Subramanya, and Jeffrey L. Brodsky
- The epithelial Na+ channel γ subunit autoinhibitory tract suppresses channel activity by binding the γ subunit's finger–thumb domain interface The Journal of Biological Chemistry, 293, 16217-16225. October 19, 2018Deidra M. Balchak, Rebecca N. Thompson and Ossama B. Kashlan
- The Activation Gate and Gating Mechanism of the NMDA Receptor J. Neurosci. 2008; 28(7): p. 1546-1556Huai-Ren Chang and Chung-Chin Kuo
- Structural basis of neurosteroid anesthetic action on GABAA receptors Nature Communications, Vol. 9, Article number: 3972, September 2018Qiang Chen, Marta M. Wells, Palaniappa Arjunan, Tommy S. Tillman, Aina E. Cohen, Yan Xu & Pei Tang
- Specific connectivity between photoreceptors and horizontal cells in the zebrafish retina Journal of Neurophysiology, Vol. 116, No. 6, 13 Dec 2016Lauw J. Klaassen, Wim de Graaff, Jorrit B. van Asselt, Jan Klooster, and Maarten Kamermans
- Small heat shock protein alpha A-crystallin regulates epithelial sodium channel expression J. Biol. Chem. published 30 July 2007, 10.1074/jbc.M703409200Ossama B. Kashlan, Gunhild M. Mueller, Mohammed Z. Qamar, Paul A. Poland, Annette Ahner, Ronald C. Rubenstein, Rebecca P. Hughey, Jeffrey L. Brodsky, and Thomas R. Kleyman
- Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain Nature Vol. 534, pages 494–499 (23 June 2016)Jeremiah D. Osteen, Volker Herzig, John Gilchrist, Joshua J. Emrick, Chuchu Zhang, Xidao Wang, Joel Castro, Sonia Garcia-Caraballo, Luke Grundy, Grigori Y. Rychkov, Andy D. Weyer, Zoltan Dekan, Eivind A. B. Undheim, Paul Alewood, Cheryl L. Stucky, Stuart M. Brierley, Allan I. Basbaum, Frank Bosmans, Glenn F. King, and David Julius
- Rational Design of α-Conotoxin RegIIA Analogues Specifically Inhibiting the Human α3β2 Nicotinic Acetylcholine Receptor through Computational Scanning ACS Chem. Neurosci. July 2020Qingliang Xu, Han-Shen Tae, Zihao Wang, Tao Jiang, David J. Adams, and Rilei Yu
- Probing TARP Modulation of AMPA Receptor Conductance with Polyamine Toxins Journal of Neuroscience 18 May 2011, 31 (20) 7511-7520Alexander C. Jackson, Aaron D. Milstein, David Soto, Mark Farrant, Stuart G. Cull-Candy and Roger A. Nicoll
- Pharmacological modulators of nav1.1 voltage-gated sodium channels associated with mechanical pain U.S. Provisional Patent Application No. 62/300,237, Feb. 26, 2016Frank Bosmans
- On the Interaction between Amiloride and Its Putative {alpha}-Subunit Epithelial Na+ Channel Binding Site J. Biol. Chem. 2005; 280(28): p. 26206-26215Ossama B. Kashlan, Shaohu Sheng, and Thomas R. Kleyman
- Na+ Inhibits the Epithelial Na+ Channel by Binding to a Site in an Extracellular Acidic Cleft J. Biol. Chem. 2015; 290:568-576.Ossama B. Kashlan, Brandon M. Blobner, Zachary Zuzek, Michael Tolino, and Thomas R. Kleyman
- Murine epithelial sodium (Na+) channel regulation by biliary factors Journal of Biological Chemistry, jbc.RA119.007394, May 2019Xue-Ping Wang, Seohyun Janice Im, Deidra M. Balchak, Nicolas Montalbetti, Marcelo D. Carattino, Evan C. Ray and Ossama B. Kashlan
- Molecular basis of inhibition of acid sensing ion channel 1A by diminazene Plos One, May 21, 2018Aram J. Krauson, James G. Rooney, Marcelo D. Carattino
- Ion conduction and selectivity in acid-sensing ion channel 1 J. Gen. Physiol. 2014; 144:245-255.Lei Yang and Lawrence G. Palmer
- Interaction of Synthetic Human SLURP-1 with the Nicotinic Acetylcholine Receptors Nature Scientific Reports, Vol. 7, Article number: 16606 (2017)Thomas Durek, Irina V. Shelukhina, Han-Shen Tae, Panumart Thongyoo, Ekaterina N. Spirova, Denis S. Kudryavtsev, Igor E. Kasheverov, Grazyna Faure, Pierre-Jean Corringer, David J. Craik, David J. Adams & Victor I. Tsetlin
- Insights into Distinct Modulation of α7 and α7β2 Nicotinic Acetylcholine Receptors by the Volatile Anesthetic Isoflurane J. Biol. Chem. 2013; 288:35793-35800.David D. Mowrey, Qiang Liu, Vasyl Bondarenko, Qiang Chen, Edom Seyoum, Yan Xu, Jie Wu, and Pei Tang
- Inhibitory Tract Traps the Epithelial Na+ Channel in a Low Activity Conformation J. Biol. Chem. 2012 287: 20720-20726.Ossama B. Kashlan, Brandon M. Blobner, Zachary Zuzek, Marcelo D. Carattino, Thomas R. Kleyman
- Gating Transitions in the Palm Domain of ASIC1a J. Biol. Chem. 2013 288: 5487-5495.Margaret C. Della Vecchia, Anna C. Rued, Marcelo D. Carattino
- Functional Tolerance to Cysteine Mutations in Human α7 Nicotinic Acetylcholine Receptors ACS Chem. Neurosci. January 2020Tommy S. Tillman, Zachary Choi, Yan Xu Pei Tang
- Functional Human α7 Nicotinic Acetylcholine Receptor (nAChR) Generated from Escherichia coli The Journal of Biological Chemistry, 291, 18276-18282. August 26, 2016Tommy S. Tillman, Frances J. D. Alvarez, Nathan J. Reinert, Chuang Liu, Dawei Wang, Yan Xu, Kunhong Xiao, Peijun Zhang and Pei Tang
- Extracellular Proton-Modulated Pore-Blocking Effect of the Anticonvulsant Felbamate on NMDA Channels Biophys. J. published 18 May 2007, 10.1529/biophysj.106.103176Huai-Ren Chang and Chung-Chin Kuo
- Engineered receptor and their use University of Pittsburgh (Patent), January 2020Yan Xu, Pei Tang, Tommy S. Tillman
- ELIC-α7 Nicotinic Acetylcholine Receptor (α7nAChR) Chimeras Reveal a Prominent Role of the Extracellular-Transmembrane Domain Interface in Allosteric Modulation J. Biol. Chem. 2014; 289:13851-13857.Tommy S. Tillman, Edom Seyoum, David D. Mowrey, Yan Xu, and Pei Tang
- Distinct structural elements in the first membrane-spanning segment of the epithelial sodium channel J. Biol. Chem. published 14 August 2006, 10.1074/jbc.M604615200Ossama B. Kashlan, Ahmad B. Maarouf, Cassandra Kussius, Robert M. Denshaw, Kenneth M. Blumenthal, and Thomas R. Kleyman
- Determinants of selective ion permeation in the epithelial Na+ channel Journal of General Physiology. DOI: 10.1085/jgp.201812164, Published August 22, 2018Lei Yang, Lawrence G. Palmer
- Contribution of Residues in Second Transmembrane Domain of ASIC1a Protein to Ion Selectivity J. Biol. Chem. 2012 287: 12927-12934.Marcelo D. Carattino and Margaret C. Della Vecchia
- Conserved cysteines in the finger domain of the epithelial Na+ channel α and γ subunits are proximal to the dynamic finger–thumb domain interface The Journal of Biological Chemistry, 293, 4928-4939. March 30, 2018Brandon M. Blobner, Xue-Ping Wang and Ossama B. Kashlan
- Antidromic-rectifying gap junctions amplify chemical transmission at functionally mixed electrical-chemical synapses Nature Communications Vol. 8, Article number: 14818 (2017)Ping Liu, Bojun Chen, Roger Mailler & Zhao-Wen Wang
- Allosteric Inhibition of the Epithelial Na+ Channel through Peptide Binding at Peripheral Finger and Thumb Domains J. Biol. Chem. 2010 285: 35216-35223.Ossama B. Kashlan, Cary R. Boyd, Christos Argyropoulos, Sora Okumura,Rebecca P. Hughey, Michael Grabe, Thomas R. Kleyman
- A new familial form of a late-onset, persistent hyperinsulinemic hypoglycemia of infancy caused by a novel mutation in KCNJ11 Journal Channels, Vol. 11, Issue 6, 2017Yen-Yu Yang, Roger K. Long, Christine T. Ferrara, Stephen E. Gitelman, Michael S. German & Shi-Bing Yang
Additional information
Weight | .1 lbs |
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Diameter | 80 mm, 90 mm, 100 mm, 108 mm, 110 mm, 120 mm |