Ras-Associated, Small GTP-Binding Protein Mouse, Recombinant, E. Coli

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Rab3AGST-His Ras-associated, small GTP-binding protein mouse, recombinant, E. coli Cat. No. Amount Description: N-terminal tagged Rab3A is a small GTPase that belongs to the Ras PR-115 50 µg superfamily. Rab proteins play an important role in various aspects of membrane trafﬁc, including cargo selection, vesicle budding, vesicle motility, tethering, docking, and fusion. Rab3A, a member of For in vitro use only! the Rab small G protein family, is involved in the process of Ca2+- dependent neurotransmitter release. Rab3A activity is regulated by Shipping: shipped on dry ice a GDP/GTP exchange protein (Rab3 GEP), a Rab GDP dissociation inhibitor (Rab GDI), and a GTPaseactivating protein (Rab3 GAP). Storage Conditions: store at -80 °C The Rab3A recycling is coupled with synaptic vesicle trafﬁcking as follows: (i) GDP-Rab3A forms an inactive complex with Rab GDI and Additional Storage Conditions: avoid freeze/thaw cycles stays in the cytosol of nerve terminals. (ii) GDPRab3A released from Shelf Life: 12 months Rab GDI is converted to GTPRab3A by Rab3 GEP. (iii) GTP-Rab3A binds effector molecules, Rabphilin-3 and Rim, localized at synaptic Molecular Weight: 54 kDa vesicles and the active zone, respectively. These complexes facilitate Accession number: NM_009001 translocation and docking of the synaptic vesicles to the active zone. The GST-Tag facilitates the protein‘s application in typical GST Purity: > 90 % (SDS-PAGE) pull-down assays. Form: liquid (Supplied in 50 mM Tris-HCl pH 8.0, 100 mM NaCl, 10 mM Activity: MgCl2 and 2 mM beta-mercaptoethanol) 100 pmol of protein can bind > 80 pmol of GDP. Selected References: Stenmark et al. (2001) The Rab GTPase family. Genome Biol. 2:30071. Yamaguchi et al. (2002) A GDP/GTP exchange protein for the Rab3 small G protein family up-regulates a postdocking step of synaptic exocytosis in central synapses. Proc. Natl. Acad. Sci. USA. 99:14536. Jena Bioscience GmbH Löbstedter Str. 71 | 07749 Jena, Germany | Tel.:+49-3641-6285 000 Page 1 http://www.jenabioscience.com Version: 0001, Last update: Jul 23, 2021.

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Rab3a As a Modulator of Homeostatic Synaptic Plasticity
Wright State University CORE Scholar Browse all Theses and Dissertations Theses and Dissertations 2014 Rab3A as a Modulator of Homeostatic Synaptic Plasticity Andrew G. Koesters Wright State University Follow this and additional works at: https://corescholar.libraries.wright.edu/etd_all Part of the Biomedical Engineering and Bioengineering Commons Repository Citation Koesters, Andrew G., "Rab3A as a Modulator of Homeostatic Synaptic Plasticity" (2014). Browse all Theses and Dissertations. 1246. https://corescholar.libraries.wright.edu/etd_all/1246 This Dissertation is brought to you for free and open access by the Theses and Dissertations at CORE Scholar. It has been accepted for inclusion in Browse all Theses and Dissertations by an authorized administrator of CORE Scholar. For more information, please contact [email protected]. RAB3A AS A MODULATOR OF HOMEOSTATIC SYNAPTIC PLASTICITY A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy By ANDREW G. KOESTERS B.A., Miami University, 2004 2014 Wright State University WRIGHT STATE UNIVERSITY GRADUATE SCHOOL August 22, 2014 I HEREBY RECOMMEND THAT THE DISSERTATION PREPARED UNDER MY SUPERVISION BY Andrew G. Koesters ENTITLED Rab3A as a Modulator of Homeostatic Synaptic Plasticity BE ACCEPTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF Doctor of Philosophy. Kathrin Engisch, Ph.D. Dissertation Director Mill W. Miller, Ph.D. Director, Biomedical Sciences Ph.D. Program Committee on Final Examination Robert E. W. Fyffe, Ph.D. Vice President for Research Dean of the Graduate School Mark Rich, M.D./Ph.D. David Ladle, Ph.D. F. Javier Alvarez-Leefmans, M.D./Ph.D. Lynn Hartzler, Ph.D.
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Supporting Information
Supporting Information Hunter et al. 10.1073/pnas.1404639111 SI Methods and no additional magnesium. SML was added to a concentra- Protein Expression and Purification. A construct encoding codon- tion of 150 μM, and GTP and GDP were added to a concentra- optimized N-terminal His-tobacco etch virus (TEV)-G12C V-Ki- tion of 1.5 mM each in the respective samples. Samples were ras2 Kirsten rat sarcoma viral oncogene homolog (K-Ras) in the incubated at 37 °C for the indicated length of time. For each time pJExpressvector(DNA2.0)wassynthesized and used to transform point, 27 μL of sample was mixed with 3 μL of 7-diethylamino- BL21(DE3) cells. Cells were grown in Luria broth (LB) to OD 600 3-(4-maleimidophenyl)-4-methylcoumarin dissolved in DMSO 0.7 and induced with 250 mM isopropyl β-D-1-thiogalactopyrano- (100 μM final concentration) in a black 384-well plate and side (IPTG) for 16 h at 16 °C. Cells were pelleted and resuspended fluorescence was read at 384/470 nm. The assay was run in in lysis buffer [20 mM sodium phosphate (pH 8.0), 500 mM NaCl, triplicate, and normalized data were fit to a one-phase decay 10 mM imidazole, 1 mM 2-mercaptoethanol (BME), 5% (vol/vol) nonlinear regression curve in GraphPad Prism. glycerol] containing PMSF, benzamidine, and 1 mg/mL lysozyme. Lysates were flash-frozen and stored at −80 °C until use. Sequence Conservation Analysis. AminoacidsequencesofRas Protein was purified over an IMAC cartridge (BioRad) fol- family proteins were obtained from the National Center for lowing standard Ni-affinity protocols and desalted into 1× crys- Biotechnology Information Protein Data Bank (PDB) and tallization buffer [20 mM Hepes (pH 8.0), 150 mM NaCl, 5 mM aligned using the multiple alignment server, Clustal-Omega (v.1.2.0).
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