Plate Layout for Realtime Ready Human Apoptosis Panel, 96
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Epigenetic Reprogramming Sensitizes CML Stem Cells to Combined EZH2 and Tyrosine
Published OnlineFirst September 14, 2016; DOI: 10.1158/2159-8290.CD-16-0263 RESEARCH BRIEF Epigenetic Reprogramming Sensitizes CML Stem Cells to Combined EZH2 and Tyrosine Kinase Inhibition Mary T. Scott 1 , 2 , Koorosh Korfi 1 , 2 , Peter Saffrey 1 , Lisa E.M. Hopcroft 2 , Ross Kinstrie 1 , Francesca Pellicano 2 , Carla Guenther 1 , 2 , Paolo Gallipoli 2 , Michelle Cruz 1 , Karen Dunn 2 , Heather G. Jorgensen 2 , Jennifer E. Cassels 2 , Ashley Hamilton 2 , Andrew Crossan 1 , Amy Sinclair 2 , Tessa L. Holyoake 2 , and David Vetrie 1 ABSTRACT A major obstacle to curing chronic myeloid leukemia (CML) is residual disease main- tained by tyrosine kinase inhibitor (TKI)–persistent leukemic stem cells (LSC). These are BCR–ABL1 kinase independent, refractory to apoptosis, and serve as a reservoir to drive relapse or TKI resistance. We demonstrate that Polycomb Repressive Complex 2 is misregulated in chronic phase CML LSCs. This is associated with extensive reprogramming of H3K27me3 targets in LSCs, thus sensi- tizing them to apoptosis upon treatment with an EZH2-specifi c inhibitor (EZH2i). EZH2i does not impair normal hematopoietic stem cell survival. Strikingly, treatment of primary CML cells with either EZH2i or TKI alone caused signifi cant upregulation of H3K27me3 targets, and combined treatment further potentiated these effects and resulted in signifi cant loss of LSCs compared to TKI alone, in vitro , and in long-term bone marrow murine xenografts. Our fi ndings point to a promising epigenetic-based thera- peutic strategy to more effectively target LSCs in patients with CML receiving TKIs. SIGNIFICANCE: In CML, TKI-persistent LSCs remain an obstacle to cure, and approaches to eradicate them remain a signifi cant unmet clinical need. -
Gene Essentiality Landscape and Druggable Oncogenic Dependencies in Herpesviral Primary Effusion Lymphoma
ARTICLE DOI: 10.1038/s41467-018-05506-9 OPEN Gene essentiality landscape and druggable oncogenic dependencies in herpesviral primary effusion lymphoma Mark Manzano1, Ajinkya Patil1, Alexander Waldrop2, Sandeep S. Dave2, Amir Behdad3 & Eva Gottwein1 Primary effusion lymphoma (PEL) is caused by Kaposi’s sarcoma-associated herpesvirus. Our understanding of PEL is poor and therefore treatment strategies are lacking. To address this 1234567890():,; need, we conducted genome-wide CRISPR/Cas9 knockout screens in eight PEL cell lines. Integration with data from unrelated cancers identifies 210 genes as PEL-specific oncogenic dependencies. Genetic requirements of PEL cell lines are largely independent of Epstein-Barr virus co-infection. Genes of the NF-κB pathway are individually non-essential. Instead, we demonstrate requirements for IRF4 and MDM2. PEL cell lines depend on cellular cyclin D2 and c-FLIP despite expression of viral homologs. Moreover, PEL cell lines are addicted to high levels of MCL1 expression, which are also evident in PEL tumors. Strong dependencies on cyclin D2 and MCL1 render PEL cell lines highly sensitive to palbociclib and S63845. In summary, this work comprehensively identifies genetic dependencies in PEL cell lines and identifies novel strategies for therapeutic intervention. 1 Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. 2 Duke Cancer Institute and Center for Genomic and Computational Biology, Duke University, Durham, NC 27708, USA. 3 Department of Pathology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. Correspondence and requests for materials should be addressed to E.G. (email: [email protected]) NATURE COMMUNICATIONS | (2018) 9:3263 | DOI: 10.1038/s41467-018-05506-9 | www.nature.com/naturecommunications 1 ARTICLE NATURE COMMUNICATIONS | DOI: 10.1038/s41467-018-05506-9 he human oncogenic γ-herpesvirus Kaposi’s sarcoma- (IRF4), a critical oncogene in multiple myeloma33. -
RT² Profiler PCR Array (384-Well Format) Human Apoptosis 384HT
RT² Profiler PCR Array (384-Well Format) Human Apoptosis 384HT Cat. no. 330231 PAHS-3012ZE For pathway expression analysis Format For use with the following real-time cyclers RT² Profiler PCR Array, Applied Biosystems® models 7900HT (384-well block), Format E ViiA™ 7 (384-well block); Bio-Rad CFX384™ RT² Profiler PCR Array, Roche® LightCycler® 480 (384-well block) Format G Description The Human Apoptosis RT² Profiler PCR Array profiles the expression of 370 key genes involved in apoptosis, or programmed cell death. The array includes the TNF ligands and their receptors; members of the bcl-2 family, BIR (baculoviral IAP repeat) domain proteins, CARD domain (caspase recruitment domain) proteins, death domain proteins, TRAF (TNF receptor-associated factor) domain proteins and caspases. These 370 genes are also grouped by their functional contribution to apoptosis, either anti-apoptosis or induction of apoptosis. Using real-time PCR, you can easily and reliably analyze expression of a focused panel of genes related to apoptosis with this array. For further details, consult the RT² Profiler PCR Array Handbook. Sample & Assay Technologies Shipping and storage RT² Profiler PCR Arrays in formats E and G are shipped at ambient temperature, on dry ice, or blue ice packs depending on destination and accompanying products. For long term storage, keep plates at –20°C. Note: Ensure that you have the correct RT² Profiler PCR Array format for your real-time cycler (see table above). Note: Open the package and store the products appropriately immediately -
DFFA Monoclonal Antibody (M05), Degradation of the Chromosomal DNA Into Nucleosomal Clone 3A11 Units
DFFA monoclonal antibody (M05), degradation of the chromosomal DNA into nucleosomal clone 3A11 units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. Catalog Number: H00001676-M05 DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated Regulatory Status: For research use only (RUO) when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active Product Description: Mouse monoclonal antibody component of DFF. DFFB has been found to trigger both raised against a partial recombinant DFFA. DNA fragmentation and chromatin condensation during apoptosis. Two alternatively spliced transcript variants Clone Name: 3A11 encoding distinct isoforms have been found for this gene. [provided by RefSeq] Immunogen: DFFA (NP_004392.1, 231 a.a. ~ 331 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Sequence: TSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPK ALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLR SISASKASPPGDLQNPKRARQDPT Host: Mouse Reactivity: Human Applications: ELISA, PLA-Ce, S-ELISA, WB-Re, WB-Tr (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product page for detailed protocols Isotype: IgG2a Kappa Storage Buffer: In 1x PBS, pH 7.4 Storage Instruction: Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Entrez GeneID: 1676 Gene Symbol: DFFA Gene Alias: DFF-45, DFF1, ICAD Gene Summary: Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and Page 1/1 Powered by TCPDF (www.tcpdf.org). -
Cloning and Sequence Analysis of Canine Apoptosis-Associated Molecules
Zurich Open Repository and Archive University of Zurich Main Library Strickhofstrasse 39 CH-8057 Zurich www.zora.uzh.ch Year: 2007 Cloning and sequence analysis of canine apoptosis-associated molecules Schade, Benjamin Abstract: The aim of the study was to clone and sequence the coding sequences of a representative set of proteins, primarily from the intrinsic apoptotic pathway in dogs and to assess their conservation with hu- man and murine orthologues. cDNA for these proteins, including Bcl-2 family members (Bcl-XL, Bcl-w, Mcl-1, Bax, Bak, Bad, Noxa), caspases (Caspase-3, Caspase-8, Caspase-9), Inhibitors of Apoptosis Pro- teins (XIAP, cIAP-1, cIAP-2, Survivin), their mitochondrial inhibitors (Smac/ DIABLO, Omi/HtrA2) and p53, were generated by RT-PCR with RNA extracted from two canine non-neoplastic cell lines. Eleven sequences are novel for the dog. Interspecies comparison revealed strongest similarity between the sequences of human and canine intrinsic apoptosis pathway members. Differences with potential func- tional impact, however, were observed in both dogs and mice. In dogs, these changes involve the putative Inhibitor of Apoptosis Protein binding motif of canine Omi/HtrA2, some caspase substrate recognition motifs and some functionally relevant residues of p53. Canine XIAP yields a caspase-cleavage site reported as unique to humans. In conclusion, the generally high degree of similarity of canine apoptosis-associated proteins as compared to human counterparts is supportive of the use of dogs as a model for human dis- eases. Single interspecies sequence variations with potential functional relevance under physiologic and neoplastic conditions do exist, however, and will require further analysis. -
Supplementary Materials For
Supplementary Materials for Elucidating cellular population dynamics by molecular density function perturbations 1 2,3, Thanneer Malai Perumal and Rudiyanto Gunawan * 1 Sage Bionetworks, Seattle, Washington, USA; [email protected] 2 Institute for Chemical and Bioengineering, ETH Zurich, Zurich, Switzerland; [email protected] 3 Swiss Institute of Bioinformatics, Lausanne, Switzerland * Correspondence: [email protected]; Tel.: +41-44-633-2134 Supplementary Material S1. Probability Distance Metrics Signed Engineering Metric: ∞ 2 ∆ (f A (t, x )||f B (t, x )) = sign(∆μ ) ∫ (x f A (t, x ) − x f B (t, x )) dx (S. 1) E Xi i Xi i Xi i Xi i i Xi i i −∞ Signed Jeffrey Divergence: ∞ f A (t,x ) A B A B Xi i ∆ (f (t, x )||f (t, x )) = sgn(∆μ ) ∫ (f (t, x ) − f (t, x ))ln ( B ) )dx (S. 2) JD Xi i Xi i Xi Xi i Xi i f (t,x ) i −∞ Xi i Signed Kullback-Leibler Distance: ∞ f B (t,x ) A B B Xi i ∆ (f (t, x )||f (t, x )) = sgn(∆μ ) ∫ f (t, x )ln ( A ) dx (S. 3) KLD Xi i Xi i Xi Xi i f (t,x ) i −∞ Xi i Signed Jensen-Shannon Divergence: f + (t,x )+f − (t,x ) Xi i Xi i ∆ f (t, x ) = sgn(∆μ ) (S. 4) JSD Xi i Xi 2 Signed Kolmogorov-Smirnov Metric: ∆ (f A (t, x )||f B (t, x )) = sgn(∆μ )sup|F A (t, x ) − F B (t, x )| (S. 5) KS Xi i Xi i Xi Xi i Xi i Supplementary Material S2. -
Cytokine Nomenclature
RayBiotech, Inc. The protein array pioneer company Cytokine Nomenclature Cytokine Name Official Full Name Genbank Related Names Symbol 4-1BB TNFRSF Tumor necrosis factor NP_001552 CD137, ILA, 4-1BB ligand receptor 9 receptor superfamily .2. member 9 6Ckine CCL21 6-Cysteine Chemokine NM_002989 Small-inducible cytokine A21, Beta chemokine exodus-2, Secondary lymphoid-tissue chemokine, SLC, SCYA21 ACE ACE Angiotensin-converting NP_000780 CD143, DCP, DCP1 enzyme .1. NP_690043 .1. ACE-2 ACE2 Angiotensin-converting NP_068576 ACE-related carboxypeptidase, enzyme 2 .1 Angiotensin-converting enzyme homolog ACTH ACTH Adrenocorticotropic NP_000930 POMC, Pro-opiomelanocortin, hormone .1. Corticotropin-lipotropin, NPP, NP_001030 Melanotropin gamma, Gamma- 333.1 MSH, Potential peptide, Corticotropin, Melanotropin alpha, Alpha-MSH, Corticotropin-like intermediary peptide, CLIP, Lipotropin beta, Beta-LPH, Lipotropin gamma, Gamma-LPH, Melanotropin beta, Beta-MSH, Beta-endorphin, Met-enkephalin ACTHR ACTHR Adrenocorticotropic NP_000520 Melanocortin receptor 2, MC2-R hormone receptor .1 Activin A INHBA Activin A NM_002192 Activin beta-A chain, Erythroid differentiation protein, EDF, INHBA Activin B INHBB Activin B NM_002193 Inhibin beta B chain, Activin beta-B chain Activin C INHBC Activin C NM005538 Inhibin, beta C Activin RIA ACVR1 Activin receptor type-1 NM_001105 Activin receptor type I, ACTR-I, Serine/threonine-protein kinase receptor R1, SKR1, Activin receptor-like kinase 2, ALK-2, TGF-B superfamily receptor type I, TSR-I, ACVRLK2 Activin RIB ACVR1B -
Katalog 2015 Cover Paul Lin *Hinweis Förderung.Indd
Product List 2015 WE LIVE SERVICE Certificates quartett owns two productions sites that are certified according to EN ISO 9001:2008 Quality management systems - Requirements EN ISO 13485:2012 + AC:2012 Medical devices - Quality management systems - Requirements for regulatory purposes GMP Conformity Our quality management guarantees products of highest quality! 2 Foreword to the quartett product list 2015 quartett Immunodiagnostika, Biotechnologie + Kosmetik Vertriebs GmbH welcomes you as one of our new business partners as well as all of our previous loyal clients. You are now member of quartett´s worldwide customers. First of all we would like to introduce ourselves to you. Founded as a family-run company in 1986, quartett ensures for more than a quarter of a century consistent quality of products. Service and support of our valued customers are our daily businesses. And we will continue! In the end 80´s quartett offered radioimmunoassay and enzyme immunoassay kits from different manufacturers in the USA. In the beginning 90´s the company changed its strategy from offering products for routine diagnostic to the increasing field of research and development. Setting up a production plant in 1997 and a second one in 2011 supported this decision. The company specialized its product profile in the field of manufacturing synthetic peptides for antibody production, peptides such as protease inhibitors, biochemical reagents and products for histology, cytology and immunohistology. All products are exclusively manufactured in Germany without outsourcing any production step. Nowadays, we expand into all other diagnostic and research fields and supply our customers in universities, government institutes, pharmaceutical and biotechnological companies, hospitals, and private doctor offices. -
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. -
DFFB (NM 004402) Human Tagged ORF Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC208266 DFFB (NM_004402) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: DFFB (NM_004402) Human Tagged ORF Clone Tag: Myc-DDK Symbol: DFFB Synonyms: CAD; CPAN; DFF-40; DFF2; DFF40 Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin ORF Nucleotide >RC208266 ORF sequence Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGCTCCAGAAGCCCAAGAGCGTGAAGCTGCGGGCCCTGCGCAGCCCGAGGAAGTTCGGCGTGGCTGGCC GGAGCTGCCAGGAGGTGCTGCGCAAGGGCTGTCTCCGCTTCCAGCTCCCTGAGCGCGGTTCCCGGCTGTG CCTGTACGAGGATGGCACGGAGCTGACGGAAGATTACTTCCCCAGTGTTCCCGACAACGCCGAGCTGGTG CTGCTCACCTTGGGCCAGGCCTGGCAGGGCTATGTGAGCGACATCAGGCGCTTCCTCAGTGCATTTCACG AGCCACAGGTGGGGCTCATCCAGGCCGCCCAGCAGCTGCTGTGTGATGAGCAGGCCCCACAGAGGCAGAG GCTGCTGGCTGACCTCCTGCACAACGTCAGCCAGAACATCGCGGCCGAGACCCGGGCTGAGGACCCGCCG TGGTTTGAAGGCTTGGAGTCCCGATTTCAGAGCAAGTCTGGCTATCTGAGATACAGCTGTGAGAGCCGGA TCCGGAGTTACCTGAGGGAGGTGAGCTCCTACCCCTCCACAGTGGGTGCGGAGGCTCAGGAGGAATTCCT GCGGGTCCTCGGCTCCATGTGCCAGAGGCTCCGGTCCATGCAGTACAATGGCAGCTACTTCGACAGAGGA GCCAAGGGCGGCAGCCGCCTCTGCACACCGGAAGGCTGGTTCTCCTGCCAGGGTCCCTTTGACATGGACA GCTGCTTATCAAGACACTCCATCAACCCCTACAGTAACAGGGAGAGCAGGATCCTCTTCAGCACCTGGAA CCTGGATCACATAATAGAAAAGAAACGCACCATCATTCCTACACTGGTGGAAGCAATTAAGGAACAAGAT GGAAGAGAAGTGGACTGGGAGTATTTTTATGGCCTGCTTTTTACCTCAGAGAACCTAAAACTAGTGCACA -
C-Terminal Region (ARP58987 P050) Data Sheet
CASP3 antibody - C-terminal region (ARP58987_P050) Data Sheet Product Number ARP58987_P050 Product Name CASP3 antibody - C-terminal region (ARP58987_P050) Size 50ug Gene Symbol CASP3 Alias Symbols CPP32; CPP32B; SCA-1 Nucleotide Accession# NM_032991 Protein Size (# AA) 277 amino acids Molecular Weight 12kDa Product Format Lyophilized powder NCBI Gene Id 836 Host Rabbit Clonality Polyclonal Official Gene Full Name Caspase 3, apoptosis-related cysteine peptidase Gene Family CASP This is a rabbit polyclonal antibody against CASP3. It was validated on Western Blot by Aviva Systems Biology. At Aviva Systems Biology we manufacture rabbit polyclonal antibodies on a large scale (200-1000 Description products/month) of high throughput manner. Our antibodies are peptide based and protein family oriented. We usually provide antibodies covering each member of a whole protein family of your interest. We also use our best efforts to provide you antibodies recognize various epitopes of a target protein. For availability of antibody needed for your experiment, please inquire (). Peptide Sequence Synthetic peptide located within the following region: NLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFG CASP3 is a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, Description of Target large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. -
Receptor-Mediated Mitophagy Accepted21march2016
King’s Research Portal DOI: 10.1016/j.yjmcc.2016.03.010 Document Version Peer reviewed version Link to publication record in King's Research Portal Citation for published version (APA): Yamaguchi, O., Murakawa, T., Nishida, K., & Otsu, K. (2016). Receptor-mediated mitophagy. Journal of Molecular and Cellular Cardiology, 95, 50-56. [95]. https://doi.org/10.1016/j.yjmcc.2016.03.010 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.