32-2748: PSMB1 Recombinant Protein Description Product Info

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32-2748: PSMB1 Recombinant Protein Description Product Info

9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 32-2748: PSMB1 Recombinant Protein Alternative HC5,PSC5,PMSB1,FLJ25321,KIAA1838,PSMB1,Proteasome subunit beta type-1,Proteasome component Name : C5,Macropain subunit C5,Multicatalytic endopeptidase complex subunit C5,Proteasome gamma chain. Description Source : Escherichia Coli. PSMB1 Human Recombinant fused to 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids (30-241) and having a molecular mass of 27.7 kDa. The PSMB1 is purified by proprietary chromatographic techniques. PSMB1 is part of the proteasome B-type family, also identified as the T1B family, that is a 20S core beta subunit. PSMB1 is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species.The main function of PSMB1 is its degradation activity of unnecessary or damaged proteins by proteolysis. PSMB1 is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with arg, phe, tyr, leu, and glu adjacent to the leaving group at neutral or slightly basic ph. the proteasome has an atp-dependent proteolytic activity. Product Info Amount : 10 µg Purification : Greater than 95.0% as determined by SDS-PAGE. Content : The PSMB1 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol. PSMB1 Recombinant Human although stable at 4°C for 30 days, should be stored desiccated Storage condition : below -20°C for periods greater than 30 days. Please avoid freeze-thaw cycles. Amino Acid : MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMFS PYVFNGGTIL AIAGEDFAIV ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLSLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVSLRKD. For Research Use Only. Not for use in diagnostic/therapeutics procedures..

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View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by King's Research Portal King’s Research Portal DOI: 10.1016/j.biotechadv.2017.05.004 Document Version Publisher's PDF, also known as Version of record Link to publication record in King's Research Portal Citation for published version (APA): Neville, J. J., Orlando, J., Mann, K., McCloskey, B., & Antoniou, M. N. (2017). Ubiquitous Chromatin-opening Elements (UCOEs): Applications in biomanufacturing and gene therapy. BIOTECHNOLOGY ADVANCES, 557- 564. DOI: 10.1016/j.biotechadv.2017.05.004 Citing this paper Please note that where the full-text provided on King's Research Portal is the Author Accepted Manuscript or Post-Print version this may differ from the final Published version. If citing, it is advised that you check and use the publisher's definitive version for pagination, volume/issue, and date of publication details. And where the final published version is provided on the Research Portal, if citing you are again advised to check the publisher's website for any subsequent corrections. General rights Copyright and moral rights for the publications made accessible in the Research Portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognize and abide by the legal requirements associated with these rights. •Users may download and print one copy of any publication from the Research Portal for the purpose of private study or research. •You may not further distribute the material or use it for any profit-making activity or commercial gain •You may freely distribute the URL identifying the publication in the Research Portal Take down policy If you believe that this document breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim.
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A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
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Supplementary Table 2
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