Open Oocyte Perfusion Chamber adapter
Open Oocyte Perfusion Chamber adapter
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
- The Thumb Domain Mediates Acid-sensing Ion Channel Desensitization Aram J. Krauson and Marcelo D. CarattinoJ. Biol. Chem. 2016; 291:11407-11419.
- The Lhs1/GRP170 Chaperones Facilitate the Endoplasmic Reticulum-associated Degradation of the Epithelial Sodium Channel Teresa M. Buck, Lindsay Plavchak, Ankita Roy, Bridget F. Donnelly, Ossama B. Kashlan, Thomas R. Kleyman, Arohan R. Subramanya, and Jeffrey L. BrodskyJ. Biol. Chem. 2013; 288(25): p. 18366-18380
- The epithelial Na+ channel γ subunit autoinhibitory tract suppresses channel activity by binding the γ subunit's finger–thumb domain interface Deidra M. Balchak, Rebecca N. Thompson and Ossama B. KashlanThe Journal of Biological Chemistry, 293, 16217-16225. October 19, 2018
- The Activation Gate and Gating Mechanism of the NMDA Receptor Huai-Ren Chang and Chung-Chin KuoJ. Neurosci. 2008; 28(7): p. 1546-1556
- Structural basis of neurosteroid anesthetic action on GABAA receptors Qiang Chen, Marta M. Wells, Palaniappa Arjunan, Tommy S. Tillman, Aina E. Cohen, Yan Xu & Pei TangNature Communications, Vol. 9, Article number: 3972, September 2018
- Specific connectivity between photoreceptors and horizontal cells in the zebrafish retina Lauw J. Klaassen, Wim de Graaff, Jorrit B. van Asselt, Jan Klooster, and Maarten KamermansJournal of Neurophysiology, Vol. 116, No. 6, 13 Dec 2016
- Small heat shock protein alpha A-crystallin regulates epithelial sodium channel expression Ossama 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. KleymanJ. Biol. Chem. published 30 July 2007, 10.1074/jbc.M703409200
- Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain 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 JuliusNature Vol. 534, pages 494–499 (23 June 2016)
- Rational Design of α-Conotoxin RegIIA Analogues Specifically Inhibiting the Human α3β2 Nicotinic Acetylcholine Receptor through Computational Scanning Qingliang Xu, Han-Shen Tae, Zihao Wang, Tao Jiang, David J. Adams, and Rilei YuACS Chem. Neurosci. July 2020
- Probing TARP Modulation of AMPA Receptor Conductance with Polyamine Toxins Alexander C. Jackson, Aaron D. Milstein, David Soto, Mark Farrant, Stuart G. Cull-Candy and Roger A. NicollJournal of Neuroscience 18 May 2011, 31 (20) 7511-7520
- Pharmacological modulators of nav1.1 voltage-gated sodium channels associated with mechanical pain Frank BosmansU.S. Provisional Patent Application No. 62/300,237, Feb. 26, 2016
- On the Interaction between Amiloride and Its Putative {alpha}-Subunit Epithelial Na+ Channel Binding Site Ossama B. Kashlan, Shaohu Sheng, and Thomas R. KleymanJ. Biol. Chem. 2005; 280(28): p. 26206-26215
- Na+ Inhibits the Epithelial Na+ Channel by Binding to a Site in an Extracellular Acidic Cleft Ossama B. Kashlan, Brandon M. Blobner, Zachary Zuzek, Michael Tolino, and Thomas R. KleymanJ. Biol. Chem. 2015; 290:568-576.
- Murine epithelial sodium (Na+) channel regulation by biliary factors Xue-Ping Wang, Seohyun Janice Im, Deidra M. Balchak, Nicolas Montalbetti, Marcelo D. Carattino, Evan C. Ray and Ossama B. KashlanJournal of Biological Chemistry, jbc.RA119.007394, May 2019
- Molecular basis of inhibition of acid sensing ion channel 1A by diminazene Aram J. Krauson, James G. Rooney, Marcelo D. CarattinoPlos One, May 21, 2018
- Ion conduction and selectivity in acid-sensing ion channel 1 Lei Yang and Lawrence G. PalmerJ. Gen. Physiol. 2014; 144:245-255.
- Interaction of Synthetic Human SLURP-1 with the Nicotinic Acetylcholine Receptors 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. TsetlinNature Scientific Reports, Vol. 7, Article number: 16606 (2017)
- Insights into Distinct Modulation of α7 and α7β2 Nicotinic Acetylcholine Receptors by the Volatile Anesthetic Isoflurane David D. Mowrey, Qiang Liu, Vasyl Bondarenko, Qiang Chen, Edom Seyoum, Yan Xu, Jie Wu, and Pei TangJ. Biol. Chem. 2013; 288:35793-35800.
- Inhibitory Tract Traps the Epithelial Na+ Channel in a Low Activity Conformation Ossama B. Kashlan, Brandon M. Blobner, Zachary Zuzek, Marcelo D. Carattino, Thomas R. KleymanJ. Biol. Chem. 2012 287: 20720-20726.
- Gating Transitions in the Palm Domain of ASIC1a Margaret C. Della Vecchia, Anna C. Rued, Marcelo D. CarattinoJ. Biol. Chem. 2013 288: 5487-5495.
- Functional Tolerance to Cysteine Mutations in Human α7 Nicotinic Acetylcholine Receptors Tommy S. Tillman, Zachary Choi, Yan Xu Pei TangACS Chem. Neurosci. January 2020
- Functional Human α7 Nicotinic Acetylcholine Receptor (nAChR) Generated from Escherichia coli Tommy S. Tillman, Frances J. D. Alvarez, Nathan J. Reinert, Chuang Liu, Dawei Wang, Yan Xu, Kunhong Xiao, Peijun Zhang and Pei TangThe Journal of Biological Chemistry, 291, 18276-18282. August 26, 2016
- Extracellular Proton-Modulated Pore-Blocking Effect of the Anticonvulsant Felbamate on NMDA Channels Huai-Ren Chang and Chung-Chin KuoBiophys. J. published 18 May 2007, 10.1529/biophysj.106.103176
- Engineered receptor and their use Yan Xu, Pei Tang, Tommy S. TillmanUniversity of Pittsburgh (Patent), January 2020
- ELIC-α7 Nicotinic Acetylcholine Receptor (α7nAChR) Chimeras Reveal a Prominent Role of the Extracellular-Transmembrane Domain Interface in Allosteric Modulation Tommy S. Tillman, Edom Seyoum, David D. Mowrey, Yan Xu, and Pei TangJ. Biol. Chem. 2014; 289:13851-13857.
- Distinct structural elements in the first membrane-spanning segment of the epithelial sodium channel Ossama B. Kashlan, Ahmad B. Maarouf, Cassandra Kussius, Robert M. Denshaw, Kenneth M. Blumenthal, and Thomas R. KleymanJ. Biol. Chem. published 14 August 2006, 10.1074/jbc.M604615200
- Determinants of selective ion permeation in the epithelial Na+ channel Lei Yang, Lawrence G. PalmerJournal of General Physiology. DOI: 10.1085/jgp.201812164, Published August 22, 2018
- Contribution of Residues in Second Transmembrane Domain of ASIC1a Protein to Ion Selectivity Marcelo D. Carattino and Margaret C. Della VecchiaJ. Biol. Chem. 2012 287: 12927-12934.
- Conserved cysteines in the finger domain of the epithelial Na+ channel α and γ subunits are proximal to the dynamic finger–thumb domain interface Brandon M. Blobner, Xue-Ping Wang and Ossama B. KashlanThe Journal of Biological Chemistry, 293, 4928-4939. March 30, 2018
- Antidromic-rectifying gap junctions amplify chemical transmission at functionally mixed electrical-chemical synapses Ping Liu, Bojun Chen, Roger Mailler & Zhao-Wen WangNature Communications Vol. 8, Article number: 14818 (2017)
- Allosteric Inhibition of the Epithelial Na+ Channel through Peptide Binding at Peripheral Finger and Thumb Domains Ossama B. Kashlan, Cary R. Boyd, Christos Argyropoulos, Sora Okumura,Rebecca P. Hughey, Michael Grabe, Thomas R. KleymanJ. Biol. Chem. 2010 285: 35216-35223.
- A new familial form of a late-onset, persistent hyperinsulinemic hypoglycemia of infancy caused by a novel mutation in KCNJ11 Yen-Yu Yang, Roger K. Long, Christine T. Ferrara, Stephen E. Gitelman, Michael S. German & Shi-Bing YangJournal Channels, Vol. 11, Issue 6, 2017
Additional information
| Weight | .1 lbs |
|---|---|
| Diameter | 80 mm, 90 mm, 100 mm, 108 mm, 110 mm, 120 mm |
