Proteasome 26S Subunit, Non Atpase 7 (PSMD7)

Total Page：16

File Type：pdf, Size：1020Kb

RPG282Hu01 10µg Recombinant Proteasome 26S Subunit, Non ATPase 7 (PSMD7) Organism Species: Homo sapiens (Human) Instruction manual FOR IN VITRO USE AND RESEARCH USE ONLY NOT FOR USE IN CLINICAL DIAGNOSTIC PROCEDURES 10th Edition (Revised in Jan, 2014) [ PROPERTIES ] Residues: Met1~Lys324 Tags: Two N-terminal Tags, His-tag and T7-tag Accession: P51665 Host: E. coli Purity: >90% Endotoxin Level: <1.0EU per 1μg (determined by the LAL method). Formulation: Supplied as lyophilized form in 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5% trehalose, and preservative. Predicted isoelectric point: 6.7 Predicted Molecular Mass: 40.8kDa Applications: SDS-PAGE; WB; ELISA; IP. (May be suitable for use in other assays to be determined by the end user.) [ USAGE ] Reconstitute in sterile ddH2O. [ STORAGE AND STABILITY ] Storage: Avoid repeated freeze/thaw cycles. Store at 2-8oC for one month. Aliquot and store at -80oC for 12 months. Stability Test: The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37oC for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition. [ SEQUENCES ] The sequence of the target protein is listed below. MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR KEDKEKDKDK EKSDVKKEEK KEKK [ REFERENCES ] 1. Tsurumi C., et al. (1995) Biochem. Biophys. Res. Commun. 210:600-608. 2. Wang X., et al. (2007) Biochemistry 46:3553-3565. 3. Stelzl U., et al. (2005) Cell 122:957-968. 4. Thompson H.G., et al. (2004) Int. J. Cancer 111:338-347..

Copy Link

Recommended publications

Proteasome System of Protein Degradation and Processing
ISSN 0006-2979, Biochemistry (Moscow), 2009, Vol. 74, No. 13, pp. 1411-1442. © Pleiades Publishing, Ltd., 2009. Original Russian Text © A. V. Sorokin, E. R. Kim, L. P. Ovchinnikov, 2009, published in Uspekhi Biologicheskoi Khimii, 2009, Vol. 49, pp. 3-76. REVIEW Proteasome System of Protein Degradation and Processing A. V. Sorokin*, E. R. Kim, and L. P. Ovchinnikov Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: [email protected]; [email protected] Received February 5, 2009 Abstract—In eukaryotic cells, degradation of most intracellular proteins is realized by proteasomes. The substrates for pro- teolysis are selected by the fact that the gate to the proteolytic chamber of the proteasome is usually closed, and only pro- teins carrying a special “label” can get into it. A polyubiquitin chain plays the role of the “label”: degradation affects pro- teins conjugated with a ubiquitin (Ub) chain that consists at minimum of four molecules. Upon entering the proteasome channel, the polypeptide chain of the protein unfolds and stretches along it, being hydrolyzed to short peptides. Ubiquitin per se does not get into the proteasome, but, after destruction of the “labeled” molecule, it is released and labels another molecule. This process has been named “Ub-dependent protein degradation”. In this review we systematize current data on the Ub–proteasome system, describe in detail proteasome structure, the ubiquitination system, and the classical ATP/Ub- dependent mechanism of protein degradation, as well as try to focus readers’ attention on the existence of alternative mech- anisms of proteasomal degradation and processing of proteins.
[Show full text]
A Novel Proteasome Inhibitor NPI-0052 As an Anticancer Therapy
British Journal of Cancer (2006) 95, 961 – 965 & 2006 Cancer Research UK All rights reserved 0007 – 0920/06 $30.00 www.bjcancer.com Minireview A novel proteasome inhibitor NPI-0052 as an anticancer therapy 1 1 ,1 D Chauhan , T Hideshima and KC Anderson* 1Department of Medical Oncology, Harvard Medical School, Dana Farber Cancer Institute, The Jerome Lipper Multiple Myeloma Center, Boston, MA 02115, USA Proteasome inhibitor Bortezomib/Velcade has emerged as an effective anticancer therapy for the treatment of relapsed and/or refractory multiple myeloma (MM), but prolonged treatment can be associated with toxicity and development of drug resistance. In this review, we discuss the recent discovery of a novel proteasome inhibitor, NPI-0052, that is distinct from Bortezomib in its chemical structure, mechanisms of action, and effects on proteasomal activities; most importantly, it overcomes resistance to conventional and Bortezomib therapies. In vivo studies using human MM xenografts shows that NPI-0052 is well tolerated, prolongs survival, and reduces tumour recurrence. These preclinical studies provided the basis for Phase-I clinical trial of NPI-0052 in relapsed/ refractory MM patients. British Journal of Cancer (2006) 95, 961–965. doi:10.1038/sj.bjc.6603406 www.bjcancer.com & 2006 Cancer Research UK Keywords: protein degradation; proteasomes; multiple myeloma; novel therapy; apoptosis; drug resistance The systemic regulation of protein synthesis and protein degrada- inducible immunoproteasomes b-5i, b-1i, b-2i with different tion is essential
[Show full text]
PSMB8 Gene Proteasome Subunit Beta 8
PSMB8 gene proteasome subunit beta 8 Normal Function The PSMB8 gene provides instructions for making one part (subunit) of cell structures called immunoproteasomes. Immunoproteasomes are specialized versions of proteasomes, which are large complexes that recognize and break down (degrade) unneeded, excess, or abnormal proteins within cells. This activity is necessary for many essential cell functions. While proteasomes are found in many types of cells, immunoproteasomes are located primarily in immune system cells. These structures play an important role in regulating the immune system's response to foreign invaders, such as viruses and bacteria. One of the primary functions of immunoproteasomes is to help the immune system distinguish the body's own proteins from proteins made by foreign invaders, so the immune system can respond appropriately to infection. Immunoproteasomes may also have other functions in immune system cells and possibly in other types of cells. They appear to be involved in some of the same fundamental cell activities as regular proteasomes, such as regulating the amount of various proteins in cells (protein homeostasis), cell growth and division, the process by which cells mature to carry out specific functions (differentiation), chemical signaling within cells, and the activity of genes. Studies suggest that, through unknown mechanisms, the subunit produced from the PSMB8 gene in particular may be involved in the maturation of fat cells (adipocytes). Health Conditions Related to Genetic Changes Nakajo-Nishimura syndrome At least one mutation in the PSMB8 gene has been found to cause Nakajo-Nishimura syndrome, a condition that has been described only in the Japanese population. The identified mutation changes a single protein building block (amino acid) in the protein produced from the PSMB8 gene, replacing the amino acid glycine with the amino acid valine at protein position 201 (written as Gly201Val or G201V).
[Show full text]
Proteasome Biology: Chemistry and Bioengineering Insights
polymers Review Proteasome Biology: Chemistry and Bioengineering Insights Lucia Raˇcková * and Erika Csekes Centre of Experimental Medicine, Institute of Experimental Pharmacology and Toxicology, Slovak Academy of Sciences, Dúbravská cesta 9, 841 04 Bratislava, Slovakia; [email protected] * Correspondence: [email protected] or [email protected] Received: 28 September 2020; Accepted: 23 November 2020; Published: 4 December 2020 Abstract: Proteasomal degradation provides the crucial machinery for maintaining cellular proteostasis. The biological origins of modulation or impairment of the function of proteasomal complexes may include changes in gene expression of their subunits, ubiquitin mutation, or indirect mechanisms arising from the overall impairment of proteostasis. However, changes in the physico-chemical characteristics of the cellular environment might also meaningfully contribute to altered performance. This review summarizes the effects of physicochemical factors in the cell, such as pH, temperature fluctuations, and reactions with the products of oxidative metabolism, on the function of the proteasome. Furthermore, evidence of the direct interaction of proteasomal complexes with protein aggregates is compared against the knowledge obtained from immobilization biotechnologies. In this regard, factors such as the structures of the natural polymeric scaffolds in the cells, their content of reactive groups or the sequestration of metal ions, and processes at the interface, are discussed here with regard to their
[Show full text]
Structural Insights Into Substrate Recognition and Processing by the 20S Proteasome
biomolecules Review Structural Insights into Substrate Recognition and Processing by the 20S Proteasome Indrajit Sahu * and Michael H. Glickman * Faculty of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel * Correspondence: [email protected] (I.S.); [email protected] (M.H.G.); Tel.: +972-0586747499 (I.S.); +972-4-829-4552 (M.H.G.) Abstract: Four decades of proteasome research have yielded extensive information on ubiquitin- dependent proteolysis. The archetype of proteasomes is a 20S barrel-shaped complex that does not rely on ubiquitin as a degradation signal but can degrade substrates with a considerable unstructured stretch. Since roughly half of all proteasomes in most eukaryotic cells are free 20S complexes, ubiquitin-independent protein degradation may coexist with ubiquitin-dependent degradation by the highly regulated 26S proteasome. This article reviews recent advances in our understanding of the biochemical and structural features that underlie the proteolytic mechanism of 20S proteasomes. The two outer α-rings of 20S proteasomes provide a number of potential docking sites for loosely folded polypeptides. The binding of a substrate can induce asymmetric conformational changes, trigger gate opening, and initiate its own degradation through a protease-driven translocation mechanism. Consequently, the substrate translocates through two additional narrow apertures augmented by the β-catalytic active sites. The overall pulling force through the two annuli results in a protease-like unfolding of the substrate and subsequent proteolysis in the catalytic chamber. Although both proteasomes contain identical β-catalytic active sites, the differential translocation mechanisms yield distinct peptide products. Nonoverlapping substrate repertoires and product outcomes rationalize cohabitation of both proteasome complexes in cells.
[Show full text]
The Proteasome: a Protein-Degrading Organelle?
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector DAVID M. RUBIN AND DANIEL FINLEY PROTEOLYSIS The proteasome: a protein-degrading organelle? The crystal structure of the proteasome suggests that degradation of ubiquitin-protein conjugates is achieved by unfolding the protein substrate and translocating it through a channel into a peptidase-containing chamber. The specificity pockets of intestinal proteases such as Proteasome active sites trypsin have long guided thinking about selectivity in Proteasome subunits are arranged into four heptameric proteolysis. Using the polypeptide ubiquitin to tag pro- rings, which are stacked together to form a hollow teins for degradation has, by contrast, seemed a rather cylinder (Fig. 1). In the proteasome from Thermoplasma baroque approach to the problem of substrate discrimina- acidophilum, an archaebacterium, the subunits are of two tion. We now know that ubiquitination accounts for the types, at and 3, located in the outer and inner rings, turnover of cyclins, cyclin-dependent kinase inhibitors, respectively (Fig. 1) [3]. The eukaryotic forms of these p53, c-Jun and other oncoproteins [1,2]. However, it has subunits are surprisingly similar to those of T acidophilum, remained unclear why, of the many known proteolytic although in eukaryotes the a and 13 genes are differenti- mechanisms, only this one has evolved a tagging step. ated into families. In the yeast Saccharomyces cerevisiae, for Recent studies of the 26S protease, a 2 megadalton com- example, there are seven at subunit genes and seven 3 plex that degrades ubiquitinated proteins, have pointed subunit genes.
[Show full text]
PSMB8) Mutation Causes the Autoinﬂammatory Disorder, Nakajo-Nishimura Syndrome
Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinﬂammatory disorder, Nakajo-Nishimura syndrome Kazuhiko Arimaa,1, Akira Kinoshitab,1, Hiroyuki Mishimab,1, Nobuo Kanazawac,1, Takeumi Kanekod, Tsunehiro Mizushimae, Kunihiro Ichinosea, Hideki Nakamuraa, Akira Tsujinof, Atsushi Kawakamia, Masahiro Matsunakac, Shimpei Kasagig, Seiji Kawanog, Shunichi Kumagaig, Koichiro Ohmurah, Tsuneyo Mimorih, Makito Hiranoi, Satoshi Uenoi, Keiko Tanakaj, Masami Tanakak, Itaru Toyoshimal, Hirotoshi Suginom, Akio Yamakawan, Keiji Tanakao, Norio Niikawap, Fukumi Furukawac, Shigeo Muratad, Katsumi Eguchia, Hiroaki Idaa,q,2, and Koh-ichiro Yoshiurab,2 aUnit of Translational Medicine, Department of Immunology and Rheumatology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8501, Japan; bDepartment of Human Genetics, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8523, Japan; cDepartment of Dermatology, Wakayama Medical University, Wakayama 641-0012, Japan; dLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan; eDepartment of Life Science, Picobiology Institute, Graduate School of Life Science, University of Hyogo, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan; fUnit of Translational Medicine, Department of Neuroscience and Neurology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8501; gDepartment of Clinical Pathology and Immunology, Kobe University
[Show full text]
Protein Degradation Fact Sheet
Understanding Cellular Protein Degradation Proteins are fundamental to cellular function Proteins are large, complex molecules that have a range of significant roles in the body and are necessary for the structure, function and regulation of tissues and organs.1 Cells maintain the proper balance of proteins by regulating several fundamental processes including protein synthesis and degradation, or the creation and removal of proteins.2 Protein homeostasis is critical for cell health Protein degradation is part of a cell’s protein homeostasis regulatory network that ensures unnecessary proteins are removed from the cellular environment when they are no longer needed or are damaged or faulty in some way.2,3 An efficiently functioning proteome, or all the possible proteins in an organism, is fundamental to all cellular processes and critical to the health of the cell and lifespan of the organism. Protein Degradation in Practice The ubiquitin-proteasome system (UPS) is one of 2 primary means of protein degradation in cells (the other is lysosomal proteolysis). The UPS tags intracellular proteins for degradation with a small protein called ubiquitin by the E3 ligase enzyme complex. Ubiquitin-tagged proteins are then sent to the proteasome and degraded.3 Protein Ubiquitin Proteasome Cereblon E3 Ligase Enzyme Complex Destroyed Protein The accumulation of proteins in a cell may lead to detrimental effects When a cell is unable to degrade abnormal and/or unnecessary proteins, these proteins can accumulate within the cellular environment. The accumulation of proteins within a cell is implicated in the pathogenesis of many diseases, including several malignancies and neurodegenerative disorders.2,3 Targeting a cell’s protein degradation system Many current approaches to treating cancer focus on inhibiting specific pathways or proteins.
[Show full text]
Expanding Role of Ubiquitin in Translational Control
International Journal of Molecular Sciences Review Expanding Role of Ubiquitin in Translational Control 1, 1, 2 1, Shannon E. Dougherty y, Austin O. Maduka y , Toshifumi Inada and Gustavo M. Silva * 1 Department of Biology, Duke University, Durham, NC 27708-0338, USA; [email protected] (S.E.D.); [email protected] (A.O.M.) 2 Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan; [email protected] * Correspondence: [email protected]; Tel.: +1-919-684-8442 These authors contributed equally to this work. y Received: 11 January 2020; Accepted: 5 February 2020; Published: 9 February 2020 Abstract: The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regulation is controlled by a variety of RNA binding proteins, translation and associated factors, numerous enzymes, and by post-translational modifications (PTM). Ubiquitination, a prominent PTM discovered as the signal for protein degradation, has newly emerged as a modulator of protein synthesis by controlling several processes in translation. Advances in proteomics and cryo-electron microscopy have identified ubiquitin modifications of several ribosomal proteins and provided numerous insights on how this modification affects ribosome structure and function. The variety of pathways and functions of translation controlled by ubiquitin are determined by the various enzymes involved in ubiquitin conjugation and removal, by the ubiquitin chain type used, by the target sites of ubiquitination, and by the physiologic signals triggering its accumulation. Current research is now elucidating multiple ubiquitin-mediated mechanisms of translational control, including ribosome biogenesis, ribosome degradation, ribosome-associated protein quality control (RQC), and redox control of translation by ubiquitin (RTU).
[Show full text]
Converting Enzyme (TACE&Sol;ADAM17)
Leukemia (2010) 24, 51–57 & 2010 Macmillan Publishers Limited All rights reserved 0887-6924/10 $32.00 www.nature.com/leu ORIGINAL ARTICLE TNF-a-converting enzyme (TACE/ADAM17)-dependent loss of CD30 induced by proteasome inhibition through reactive oxygen species AM Vahdat1, KS Reiners1, VL Simhadri1, DA Eichenauer1,BBo¨ll1, A Chalaris2, VR Simhadri1, K Wiegmann3, H-W Krell4, S Rose-John2, A Engert1, EP von Strandmann1 and HP Hansen1 1Laboratory of Immunotherapy, Department I of Internal Medicine, University Clinic Cologne, Cologne, Germany; 2Department of Biochemistry, University of Kiel, Kiel, Germany; 3Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Cologne, Germany and 4Roche Diagnostics Pharma Research, Penzberg, Germany Combinations with proteasome inhibitors are currently being inhibitors of nuclear factor-kB (I-kB species).7 We previously investigated to improve the therapy of hematological malig- tested the combination of bortezomib and the fully human anti- nancies. We previously found that proteasome inhibition by CD30 antibody (Ab), MDX-060, in the anti-CD30 Ab-responsive bortezomib failed to sensitize anti-CD30 antibody (Ab)-based 8 lymphoma cell killing. In this study, we demonstrate in L540 HL cell line L540, both in vitro and in a SCID mouse model. Hodgkin’s lymphoma cells that proteasome inhibition not only Although preincubation with MDX-060 enhanced the cytotoxic communicates apoptosis but also more rapidly causes a loss of potency of bortezomib, simultaneous or preincubation with CD30 antigen from cell membrane and a simultaneous release bortezomib failed to improve Ab therapy. Currently, there is no of soluble CD30, a targeting competitor. This shedding was explanation for this defect.
[Show full text]
Immunoproteasome Deficiency Is a Feature of Non-Small Cell Lung
Immunoproteasome deficiency is a feature of non-small PNAS PLUS cell lung cancer with a mesenchymal phenotype and is associated with a poor outcome Satyendra C. Tripathia, Haley L. Petersb, Ayumu Taguchic, Hiroyuki Katayamaa, Hong Wanga, Amin Momina, Mohit Kumar Jollyd, Muge Celiktasa, Jaime Rodriguez-Canalesc, Hui Liuc, Carmen Behrensc, Ignacio I. Wistubac, Eshel Ben-Jacobd,1, Herbert Levined,2, Jeffrey J. Molldremb, Samir M. Hanasha, and Edwin J. Ostrine,2 aDepartment of Clinical Cancer Prevention, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; bDepartment of Stem Cell Transplantation and Cellular Therapy, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; cDepartment of Translational Molecular Pathology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; dCenter for Theoretical Biological Physics, Rice University, Houston, TX; and eDepartment of Pulmonary Medicine, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030 Contributed by Herbert Levine, January 26, 2016 (sent for review November 5, 2015; reviewed by Eleftherios Diamandis, Beatrice S. Knudsen, and Jean Paul Thiery) The immunoproteasome plays a key role in generation of HLA proteasome specific subunits (Fig. 1 A and B). No significant peptides for T cell-mediated immunity. Integrative genomic and differences were observed for proteasome subunits between proteomic analysis of non-small cell lung carcinoma (NSCLC) cell these two groups. We also observed a significantly reduced ex- lines revealed significantly reduced expression of immunoprotea- pression of the immunoproteasome regulators IRF1 and STAT1 in some components and their regulators associated with epithelial the immunoproteasome low versus high cell lines (Fig. 1C).
[Show full text]
Proteasome Inhibition Activates the Transport and the Ectodomain Shedding of TNF-Α Receptors in Human Endothelial Cells
Research Article 1061 Proteasome inhibition activates the transport and the ectodomain shedding of TNF-α receptors in human endothelial cells Franck Peiretti, Matthias Canault, Denis Bernot, Bernadette Bonardo, Paule Deprez-Beauclair, Irène Juhan-Vague and Gilles Nalbone INSERM UMR626, IFR125 IPHM, Faculté de Médecine, 27 Bd Jean Moulin, Marseilles 13385 Cedex 5, France Author for correspondence (e-mail: [email protected]) Accepted 30 December 2004 Journal of Cell Science 118, 1061-1070 Published by The Company of Biologists 2005 doi:10.1242/jcs.01696 Summary Binding of tumor necrosis factor-α (TNF-α) to its (TACE) because it is reduced by synthetic metalloprotease transmembrane receptors (TNFRs) mediates inhibitors, recombinant TIMP-3 and by a dominant proinflammatory, apoptotic and survival responses in negative form of TACE. In the presence of TACE inhibitor, several cell types including vascular endothelial cells. proteasome inhibition increases the cell surface expression Because ectodomain shedding of cell surface molecules can of TNFRs and enhances the sensitivity of these cells to the be modified by proteasome activity, we studied in human proapoptotic effect of recombinant TNF-α. endothelial cells whether the TNF-α–TNFRs axis can be In conclusion, our data provide evidence that proteasome regulated by the cleavage of their transmembrane forms inhibitors increase TACE-dependent TNFR-shedding in in a proteasome-dependent manner. We show that endothelial cells, supporting the use of these molecules in proteasome inhibition increases the release of TNF-α and inflammatory disorders. In association with TACE TNFRs from human endothelial cells and decreases their inhibitor, proteasome inhibitors increase the amount of cellular and cell surface expression.
[Show full text]