GOLGA2/GM130 Monoclonal ANTIBODY Catalog Number:66662-1-Ig

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GOLGA2/GM130 Monoclonal ANTIBODY Catalog Number:66662-1-Ig

For Research Use Only GOLGA2/GM130 Monoclonal ANTIBODY www.ptglab.com Catalog Number:66662-1-Ig Catalog Number: GenBank Accession Number: Purification Method: Basic Information 66662-1-Ig BC014188 Protein G purification Size: GeneID (NCBI): CloneNo.: 150UL , Concentration: 1000 μg/ml by 2801 2A4F11 Bradford method using BSA as the Full Name: Recommended Dilutions: standard; golgi autoantigen, golgin subfamily WB 1:5000-1:50000 Source: a, 2 Mouse Calculated MW: Isotype: 111 kDa IgG1 Observed MW: Immunogen Catalog Number: 130 kDa AG1848 Applications Tested Applications: Positive Controls: WB, ELISA WB : LNCaP cells, HEK-293 cells, HepG2 cells, Jurkat Species Specificity: cells, HSC-T6 cells, HeLa cells, K-562 cells, PC-12 cells Human, Rat GOLGA2, also known as GM130, is a 130 kDa cis-Golgi matrix protein which is one component of the detergent and Background Information salt resistant Golgi matrix. It is a peripheral membrane protein highly bound to Golgi membrane and localized mainly at the cytoplasmic face of cis-Golgi membrane. Together with its interacting partner proteins, including p115, giantin, GRASP65, and Rab GTPase, GOLGA2/GM130 is involved in the regulation of ER-to-Golgi transport and also in the maintenance of the Golgi structure. Emerging evidence suggest that the GOLGA2/GM130 has potential roles in the control of glycosylation, cell cycle progression, and higher order cell functions such as cell polarization and directed cell migration. (PMID: 20197635) Storage: Storage Store at -20°C. Stable for one year after shipment. Storage Buffer: PBS with 0.1% sodium azide and 50% glycerol pH 7.3. Aliquoting is unnecessary for -20ºC storage For technical support and original validation data for this product please contact: This product is exclusively available under Proteintech T: 1 (888) 4PTGLAB (1-888-478-4522) (toll free E: [email protected] Group brand and is not available to purchase from any in USA), or 1(312) 455-8498 (outside USA) W: ptglab.com other manufacturer. Selected Validation Data Various lysates were subjected to SDS PAGE followed by western blot with 66662-1-Ig (GOLGA2/GM130 antibody) at dilution of 1:10000 incubated at room temperature for 1.5 hours..

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Barlow et al. BMC Biology (2018) 16:27 https://doi.org/10.1186/s12915-018-0492-9 RESEARCHARTICLE Open Access A sophisticated, differentiated Golgi in the ancestor of eukaryotes Lael D. Barlow1, Eva Nývltová2,3, Maria Aguilar1, Jan Tachezy2 and Joel B. Dacks1,4* Abstract Background: The Golgi apparatus is a central meeting point for the endocytic and exocytic systems in eukaryotic cells, and the organelle’s dysfunction results in human disease. Its characteristic morphology of multiple differentiated compartments organized into stacked flattened cisternae is one of the most recognizable features of modern eukaryotic cells, and yet how this is maintained is not well understood. The Golgi is also an ancient aspect of eukaryotes, but the extent and nature of its complexity in the ancestor of eukaryotes is unclear. Various proteins have roles in organizing the Golgi, chief among them being the golgins. Results: We address Golgi evolution by analyzing genome sequences from organisms which have lost stacked cisternae as a feature of their Golgi and those that have not. Using genomics and immunomicroscopy, we first identify Golgi in the anaerobic amoeba Mastigamoeba balamuthi. We then searched 87 genomes spanning eukaryotic diversity for presence of the most prominent proteins implicated in Golgi structure, focusing on golgins. We show some candidates as animal specific and others as ancestral to eukaryotes. Conclusions: None of the proteins examined show a phyletic distribution that correlates with the morphology of stacked cisternae, suggesting the possibility of stacking as an emergent property. Strikingly, however, the combination of golgins conserved among diverse eukaryotes allows for the most detailed reconstruction of the organelle to date, showing a sophisticated Golgi with differentiated compartments and trafficking pathways in the common eukaryotic ancestor.
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Golgi Matrix Proteins Interact with P24 Cargo Receptors and Aid Their Efficient Retention in the Golgi Apparatus
Published December 10, 2001 JCBReport Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus Francis A. Barr, Christian Preisinger, Robert Kopajtich, and Roman Körner Department of Cell Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany he Golgi apparatus is a highly complex organelle in vivo. GRASPs interact directly with the cytoplasmic comprised of a stack of cisternal membranes on the domains of specific p24 cargo receptors depending on T secretory pathway from the ER to the cell surface. their oligomeric state, and mutation of the GRASP binding This structure is maintained by an exoskeleton or Golgi site in the cytoplasmic tail of one of these, p24a, results in it matrix constructed from a family of coiled-coil proteins, being transported to the cell surface. These results suggest the golgins, and other peripheral membrane components that one function of the Golgi matrix is to aid efficient such as GRASP55 and GRASP65. Here we find that TMP21, retention or sequestration of p24 cargo receptors and other Downloaded from p24a, and gp25L, members of the p24 cargo receptor family, membrane proteins in the Golgi apparatus. are present in complexes with GRASP55 and GRASP65 Introduction on April 13, 2017 The Golgi apparatus is an organelle on the secretory pathway required to target it to the Golgi (Barr et al., 1998). GM130 required for the processing of complex sugar structures on in turn is a receptor for p115, required for tethering vesicles many proteins and lipids, and for the sorting of these proteins to their target membrane (Barroso et al., 1995; Nakamura et and lipids to their correct subcellular destinations (Farquhar al., 1997).
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Crystal Structures of the Single PDZ Domains from GRASP65 and Their Interaction with the Golgin GM130
ORIGINAL SCIENTIFIC PAPER Croat. Chem. Acta 2018, 91(2), 255–264 Published online: July 11, 2018 DOI: 10.5562/cca3341 Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130 Claudia M. Jurk,1 Yvette Roske,1 Udo Heinemann1,2,* 1 Macromolecular Structure and Interaction Laboratory, Max-Delbrück-Center for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany 2 Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany * Corresponding author’s e-mail address: [email protected] RECEIVED: April 12, 2018 REVISED: June 19, 2018 ACCEPTED: June 19, 2018 THIS PAPER IS DEDICATED TO DR. BISERKA K -P ON THE OCCASION OF HER 80TH BIRTHDAY OJIĆ RODIĆ Abstract: Among the major components of the Golgi apparatus are the GRASP family proteins, including GRASP65 on the cis-Golgi side. With its GRASP domain, GRASP65 is involved in Golgi stacking and ribbon formation. Interaction of GRASP65 with the Golgi marker protein GM130 is important for the docking of vesicles to the Golgi membrane. We present here structures of the two individual PDZ domains comprising the GRASP domain in human GRASP65. We use isothermal titration calorimetry to probe the interaction between GRASP65 and GM130. Additionally, we present evidence for the limited sequence conservation of the PDZ fold by describing the PDZ domain structure of the GRASP65 homolog Grh1 from Saccharomyces cerevisiae. Keywords: PDZ domain structure, Golgi stacking, GRASP family, Golgins, Golgi apparatus,
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Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice Chunyi Liua,b,1, Mei Meia,1, Qiuling Lia,1, Peristera Robotic, Qianqian Panga,b, Zhengzhou Yinga,b, Fei Gaod, Martin Lowec,2, and Shilai Baoa,b,2 aState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China; bSchool of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China; cFaculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, United Kingdom; and dState Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China Edited by Jennifer Lippincott-Schwartz, Howard Hughes Medical Institute, Ashburn, VA, and approved November 28, 2016 (received for review May 27, 2016) The Golgi apparatus lies at the heart of the secretory pathway remains unclear (20). Several studies have shown that polarized where it is required for secretory trafficking and cargo modifica- membrane delivery via the Golgi apparatus is important for tion. Disruption of Golgi architecture and function has been widely neuronal morphogenesis during brain development (8–10, 21), but observed in neurodegenerative disease, but whether Golgi dys- whether impairment of this process can cause neuronal death with function is causal with regard to the neurodegenerative process, consequent neurological impairment in vivo is currently unknown. or is simply a manifestation of neuronal death, remains unclear. Members of the golgin family of coiled-coil proteins are re- Here we report that targeted loss of the golgin GM130 leads to quired for maintenance of Golgi organization and are important a profound neurological phenotype in mice.
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GOLGA2/GM130 Polyclonal Antibody Catalog Number:11308-1-AP 42 Publications
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