DOCSLIB.ORG

Antibodies for Epigenetics and Gene Regulation Enabling Epigenetics Research

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Antibodies for Epigenetics and Gene Regulation Enabling Epigenetics Research antibodies for epigenetics and gene regulation Enabling Epigenetics Research 3 Chromatin Modifiers DNA Methylation Histones Transcription Regulation Highly Characterized Antibodies for Epigenetics and Gene Regulation At Active Motif, we are committed to providing the highest- polyclonal and AbFlex® recombinant antibodies are quality antibodies for studying epigenetics in the context validated for the applications you need – chromatin of histone and DNA modifications. Our antibodies are immunoprecipitation (ChIP), ChIP-Seq, Western blot, and manufactured in-house, and undergo rigorous development Immunofluorescence. and validation procedures to ensure their quality and To browse our complete list of antibodies and application performance. Our extensive, novel portfolio of monoclonal, data, please visit www.activemotif.com/abs. AbFlex® Recombinant Antibodies uniquely designed for multiple labeling methods AbFlex® antibodies are recombinant antibodies (rAbs) purification systems, and that have been generated using defined DNA sequences an avidin tag sequence to produce highly specific, reproducible antibodies. The for enzymatic biotin unique advantages of the AbFlex® antibody are its flexible conjugation using the biotin labeling and purification options. Each AbFlex® antibody ligase, BirA. contains a Sortase recognition motif (LPXTG) to covalently add fluorophores, enzymatic substrates (e.g., HRP), AbFlex is available for a peptides, DNA, drugs, or other labels to the antibody in range of Histone Markers, a directed and reproducible manner. Every antibody also DNA Methylation, and contains a 6xHis tag, which can be used with nickel-based Transcription Factors. Sortag-IT™ Labeling Kits for site-specific conjugation to AbFlex® rAbs Sortag-IT™ Labeling Kits are designed for site-specific labeling AbFlex antibody. Directly conjugate fluorophores, enzymes of Active Motif’s highly specific AbFlex® recombinant (HRP, AP), biotin, peptides, DNA, carbohydrates or other antibodies (rAb) via the Sortase tag recognition sequence labels to the terminal end of the heavy chain to ensure the (LPXTG) that is incorporated into the heavy chains of each antigen binding site remains available for target recognition. FIGURE: Sortase A belongs to a family of transpeptidases found in Gram-positive Simply add your AbFlex antibody with the poly-Glycine label, add Sortase A5 and bacteria that catalyze the attachment of poly-Glycine (G)n labels to the sortase incubate for approximately 1 hour. Purification columns are included to remove recognition sequence. The Sortag-IT Labeling Kits use Active Motif’s Sortase A5 excess label and Stop Solution is provided to inactivate the Sortase A5 enzyme. pentamutant from Staphylococcus aureus that is significantly more active Labeled antibodies are ready for downstream analysis. than wild-type Sortase to provide a faster, more efficient labeling reaction. APPLICATION KEY: ChIP = Chromatin Immunoprecipitation; DB = Dot Blot; ELISA = Enzyme-linked Immunosorbent Assay; EMSA = Electropho- retic Mobility Shift Assay FC = Flow Cytometry; ICC = Immunocytochemistry; IF = Immunofluorescence; IHC = Immunohistochemistry; IP = Immuno- precipitation; MeDIP = Methyl-DNA Immunoprecipitation; TR-FRET = Time-Resolved Fluorescence Resonance Energy Transfer; WB = Western Blotting 2 NORTH AMERICA 877 222 9543 EUROPE +32 (0)2 653 0001 www.activemotif.com Antibodies Description Applications Cat. No. Description Applications Cat. No. CHROMATIN MODIFIERS CHD2 (pAb) WB 39363 AbFlex® HDAC3 (rAb) WB 91199 CHD3 (mAb) ICC, IF, IP, WB 61469 AbFlex® JMJD2A (rAb) ELISA, WB 91143 Chd5 (mAb) ICC, IF, WB 61683 AbFlex® JMJD2B / KDM4B (rAb) IP, WB 91305 CoREST (pAb) WB 39955 AbFlex® KDM5A (rAb) ChIP-Seq, WB 91211 CTCF (pAb) ChIP, ChIP-Seq, EMSA, ICC, IF, IHC, WB 61311 AbFlex® Mi-2 beta (CHD4) (rAb) WB 91275 CUL4B (pAb) WB 61445 AbFlex® Mili / PiwiL2 (rAb) WB 91253 Dicer (mAb) WB 39817 AbFlex® N6-Methyladenosine (m6A) (rAb) DB, IP 91261 DMAP1 (pAb) IP, WB 61675 AbFlex® Nucleolin antibody (rAb) WB 91231 DOT1L (pAb) WB 39953 AbFlex® Rad21 antibody (rAb) IF, WB 91245 Drosha (pAb) IP, WB 39783 AbFlex® SMARCA1 / SNF2L1 (rAb) WB 91225 EED (mAb) ChIP, ChIP-Seq, IHC 61203 AbFlex® Suz12 (rAb) IP 91163 ELP3 (pAb) WB 39949 AATF / Che-1 (mAb) IF, WB 61789 EuHMT1 (pAb) WB 39777 Acf1 (pAb) ICC, IF, WB 39721 GCN5 (pAb) IP, WB 39831 ACTL6B (pAb) WB 61691 HDAC1 (mAb) ChIP, ICC, IF, IHC, IP, WB 39531 AEBP2 (pAb) WB 61539 HDAC2 (mAb) ChIP, ICC, IF, WB 39533 Ago1 (mAb) IP, WB 61071 HDAC3 (pAb) ChIP, WB 40968 Ago1/2/3 (mAb) ChIP, ICC, IF, IHC, IP, WB 39937 HDAC4 (pAb) ChIP, ChIP-Seq, WB 40969 Ago2 (mAb) ICC, IF, IP, WB 39853 HDAC5 (pAb) ChIP, IP, WB 40970 Ago3 (mAb) ChIP, ICC, IF, IP 39787 HDAC6 (pAb) ChIP, WB 40971 Ago4 (mAb) IP, WB 39855 HDAC9 (pAb) WB 39793 AIB1 / SRC-3 (pAb) ChIP, WB 39797 HDAC11 (pAb) WB 39208 AIB3 (pAb) IHC, WB 39835 HIPK1 (mAb) ICC, IF 39725 APOBEC2 (pAb) WB 39985 HIPK2 (mAb) ICC, IF, IHC, IP, WB 39677 ASH2L (pAb) ChIP, ChIP-Seq, WB 39099 HIRA (mAb) ICC, IF, WB 39557 Aurora B (pAb) ICC, IF, WB 39261 HMG-1 (pAb) WB 39551 BAP1 pAb) WB 61501 HMGA1 (pAb) ICC, IF, WB 39615 BAZ2A (pAb) WB 61707 HMGA2 / HMGI-C (pAb) IP, WB 61041 beta-Catenin (pAb) IP, WB 61487 HMGN1 (pAb) IP, WB 39833 BLIMP1 / PRDM1 (pAb) WB 61053 HP1 gamma phospho Ser93 (pAb) WB 39655 BMI-1 (mAb) ChIP, ChIP-Seq, IF, IHC, WB 39993 HP1β (pAb) WB 39295 Boris / CTCFL (pAb) ChIP, ChIP-Seq, WB 39851 HP1 α (mAb) ICC, IF, IP, WB 39979 BRD2 (pAb) ChIP, ChIP-Seq 61797 ING1 (mAb) ICC, IF, WB 61459 BRD3 (pAb) ChIP, ChIP-Seq, WB 61489 JARID1C / KDM5C (pAb) WB 39263 BRD4 (pAb) ChIP, ChIP-Seq, IHC, WB 39909 JMJD2A (mAb) WB 39815 BRD8 / SMAP2 (pAb) ChIP, ChIP-Seq, WB 61007 JMJD2B / KDM4B (pAb) ICC, IF, IP, WB 61221 BRD9 (pAb) ChIP, ChIP-Seq, IHC, IP, WB 61537 JMJD2D (pAb) WB 39247 CABIN1 (pAb) IP, WB 61597 JMJD2F (pAb) WB 39257 CAF-1 p150 (mAb) ICC, IF, IP, WB 39997 JMJD3 / KDM6B (mAb) WB 61387 CAF-1 p60 (mAb) ICC, IF, IP, WB 39995 JMJD6 (pAb) WB 61493 CARM1 (pAb) ChIP, IHC, IP, WB 39251 KAT5 (pAb) WB 61545 Cas9 (mAb) ChIP, ICC, IF, IP, WB 61577 KDM1B / LSD2 (pAb) WB 61457 CBX8 (pAb) WB 61237 KDM4C (pAb) WB 61687 CHD1 (mAb) ICC, IF, WB 39989 KMT2E (MLL5) (pAb) WB 61447 The lists above are a small subset of our over 700 antibodies, > 80% of which are available in a convenient sample size. For an up-to-date list of all available antibodies, please visit www.activemotif.com/abs. www.activemotif.com JAPAN +81 (0)3 5225 3638 CHINA +86 21 2092 6090 3 Antibodies Description Applications Cat. No. Description Applications Cat. No. CHROMATIN MODIFIERS, continued RbAp46/48 (pAb) ChIP, WB 39198 L3MBTL1 (pAb) ChIP, WB 39182 RBBP5 (pAb) ChIP, ChIP-Seq, WB 61405 L3MBTL2 (pAb) IP, WB 39569 REST (pAb) WB 61571 Lamin A, mature (mAb) ICC, IF, IP, WB 39961 RING1 (pAb) WB 61517 Lamin A/C (mAb) ICC, IF, WB 39287 Ring1B (mAb) ChIP, ChIP-Seq, ICC, IF, IP, WB 39663 Lamin B1 (pAb) WB 39095 Rsf1 (pAb) WB 39579 LAP2 alpha (mAb) WB 39267 RUVBL1 (pAb) WB 61711 LSD1 / KDM1A (pAb) ChIP, IP, WB 39186 SAP30 (pAb) ChIP, ChIP-Seq, WB 39731 LSH (pAb) WB 61595 SATB1 (pAb) WB 39839 Menin (pAb) ChIP, ChIP-Seq, WB 61005 SET8 / PR-SET7 antibody (pAb) WB 61009 MEP50 (pAb) WB 39190 SETD7 / SET7 antibody (pAb) WB 61451 Mi-2 (mAb) IF, IP, WB 61463 SFMBT1 antibody (pAb) ChIP, ChIP-Seq, IF, IP, WB 61759 Mi-2 beta (pAb) ICC, IF, IHC, WB 39289 SIN3A antibody (pAb) ChIP, WB 39865 Mili / PiwiL2 (mAb) ICC, IF, IP, WB 61143 SMARCA1 / SNF2L1 (mAb) IHC, WB 61465 MINA (pAb) WB 61713 SMARCA2 / BRM (mAb) ChIP, ICC, IF, WB 39805 MLL / HRX (pAb) ChIP, ChIP-Seq, ICC, IF, IP, WB 61295 SMARCA4 / BRG1 (mAb) ICC, IF, WB 39807 MMSET / WHSC1 (mAb) ICC, IF, WB 39879 SMARCA5 (mAb) ChIP, ICC, IF, IP, WB 39543 MOF / MYST1 (pAb) ICC, IF, WB 61245 SMARCAL1 / HARP (mAb) IP, WB 61115 MRG15 (pAb) WB 39361 SMARCB1 antibody (mAb) ICC, IF, WB 61649 MTA2 (pAb) WB 39359 SMARCC1 / BAF155 (pAb) ICC, IF, WB 61409 Nap1 (pAb) IF, WB 39577 SMARCC2 / BAF170 (pAb) ICC, IF, WB 61471 NAP1L1 (pAb) WB 39841 SMARCE1 (pAb) WB 61729 NCAPH2 (mAb) ICC, IF, WB 61681 SMC1-α (pAb) ChIP-Seq, IP, WB 61067 NCoA4 / ELE1 (pAb) WB 39895 SMC3 (pAb) WB 61131 Nucleophosmin (pAb) WB 39849 SMC4 (pAb) IP, WB 61129 O-GlcNAc (mAb) IP, WB 61453 SMRT / NCoR2 (pAb) WB 39845 OGT/O-GlcNAc transferase (pAb) ChIP, ChIP-Seq, WB 61355 Smyd3 (pAb) IHC, WB 61407 p300 (mAb) ChIP, ChIP-Seq, ICC, IF, IP, WB 61401 SNF5 (pAb) WB 39775 PARP-1 C-terminal (pAb) ChIP, ChIP-Seq, WB 39561 STAG1 (pAb) WB 61561 PARP-1 N-terminal (pAb) ChIP-Seq, IP, WB 61639 SUV39H1 (mAb) ChIP, ICC, IP, WB 39785 PARP-2 (pAb) ChIP, IF, IP, WB 39743 Suz12 (pAb) ChIP, ChIP-Seq, IF, WB 39357 PCL2 (mAb) WB 61153 TRF2 (pAb) IP, WB 39223 PELP1 (pAb) WB 61263 TRIM24 (pAb) IP, WB 61551 Phc1 (mAb) ICC, IF, IP, WB 39723 Ubn1 (pAb) WB 39869 Phc2 (mAb) ChIP, ICC, IF, IP, WB 39661 Uhrf1 (mAb) ICC, IF, IHC, IP, WB 61341 PHF20 (pAb) WB 61123 WDR5 (pAb) WB 61485 PHF6 (pAb) WB 61807 WRN (mAb) ICC, IF, IHC, WB 61169 PHF8 (pAb) WB 39711 PKC-B (pAb) WB 61733 Description Applications Cat. No. PKM2 (pAb) WB 61423 DNA METHYLATION PRMT2 (pAb) ICC, IF, WB 61491 AbFlex® 5-methylcytosine (rAb) DB, MeDIP 91187 PRMT5 (pAb) ChIP-Seq, WB 61001 AbFlex® N6-Methyladenosine (m6A) (rAb) DB, IP 91261 PRMT6 (pAb) WB 61003 AbFlex® TET1 (rAb) ChIP-Seq 91171 Rad21 (mAb) ICC, IF, WB 39383 3-Methylcytosine (3-mC) (pAb) DB, ICC, IF 61179 RAP1 / TERF2IP (pAb) IP, WB 61069 5-Carboxylcytosine (5-caC) (pAb) DB, ICC, IF, IHC, WB 61225 RB1 (pAb) IP, WB 61585 The lists above are a small subset of our over 700 antibodies, > 80% of which are available in a convenient sample size.
Load more

Recommended publications
  • Table of Contents (PDF)
    July 26, 2011 u vol. 108 u no. 30 u 12187–12560 Cover image: Pictured is a Tasmanian devil (Sarcophilus harrisii), a carnivorous marsupial whose numbers are dwindling due to an infectious facial cancer called Devil Facial Tumor Disease. Webb Miller et al. sequenced the genome of devils from northwest and south- east Tasmania, spanning the range of this threatened species on the Australian island. The authors report that the sequences reveal a worrisome dearth of genetic diversity among devils, suggesting the need for genetically characterized stocks to help breed hardier devils that might be better equipped to fight diseases. See the article by Miller et al. on pages 12348–12353. Image courtesy of Stephan C. Schuster. From the Cover 12348 Decoding the Tasmanian devil genome 12283 Illuminating chromosomal architecture 12295 Symmetry of cultured cells 12319 Caloric restriction and infertility 12366 Genetic diversity among ants Contents COMMENTARIES 12189 Methyl fingerprinting of the nucleosome reveals the molecular mechanism of high-mobility group THIS WEEK IN PNAS nucleosomal-2 (HMGN2) association Catherine A. Musselman and Tatiana G. Kutateladze See companion article on page 12283 12187 In This Issue 12191 Examining the establishment of cellular axes using intrinsic chirality LETTERS (ONLINE ONLY) Jason C. McSheene and Rebecca D. Burdine See companion article on page 12295 E341 Difference between restoring and predicting 3D 12193 Secrets of palm oil biosynthesis revealed structures of the loops in G-protein–coupled Toni Voelker receptors by molecular modeling See companion article on page 12527 Gregory V. Nikiforovich, Christina M. Taylor, Garland R. Marshall, and Thomas J. Baranski E342 Reply to Nikiforovich et al.: Restoration of the loop regions of G-protein–coupled receptors Dahlia A.
    [Show full text]
  • Cross-Talk Between HER2 and MED1 Regulates Tamoxifen Resistance of Human Breast Cancer Cells
    Published OnlineFirst September 10, 2012; DOI: 10.1158/0008-5472.CAN-12-1305 Cancer Tumor and Stem Cell Biology Research Cross-talk between HER2 and MED1 Regulates Tamoxifen Resistance of Human Breast Cancer Cells Jiajun Cui1, Katherine Germer1, Tianying Wu2, Jiang Wang3, Jia Luo5, Shao-chun Wang1, Qianben Wang4, and Xiaoting Zhang1 Abstract Despite the fact that most breast cancer patients have estrogen receptor (ER) a-positive tumors, up to 50% of the patients are or soon develop resistance to endocrine therapy. It is recognized that HER2 activation is one of the major mechanisms contributing to endocrine resistance. In this study, we report that the ER coactivator MED1 is a novel cross-talk point for the HER2 and ERa pathways. Tissue microarray analysis of human breast cancers revealed that MED1 expression positively correlates most strongly with HER2 status of the tumors. MED1 was highly phosphorylated, in a HER2-dependent manner, at the site known to be critical for its activation. Importantly, RNAi-mediated attenuation of MED1 sensitized HER2-overexpressing cells to tamoxifen treatment. MED1 and its phosphorylated form, but not the corepressors N-CoR and SMRT, were recruited to the ERa target gene promoter by tamoxifen in HER2-overexpressing cells. Significantly, MED1 attenuation or mutation of MED1 phosphorylation sites was sufficient to restore the promoter recruitment of N-CoR and SMRT. Notably, we found that MED1 is required for the expression of not only traditional E2-ERa target genes but also the newly described EGF-ERa target genes. Our results additionally indicated that MED1 is recruited to the HER2 gene and required for its expression.
    [Show full text]
  • Key Roles for MED1 Lxxll Motifs in Pubertal Mammary Gland Development and Luminal-Cell Differentiation
    Key roles for MED1 LxxLL motifs in pubertal mammary gland development and luminal-cell differentiation Pingping Jianga,b,1, Qiuping Hua,1, Mitsuhiro Itoc,1,3, Sara Meyera, Susan Waltza, Sohaib Khana, Robert G. Roederc,2, and Xiaoting Zhanga,2 aDepartment of Cancer and Cell Biology, College of Medicine, University of Cincinnati, 3125 Eden Avenue, OH 45267; bCollege of Life Sciences, Zhejiang University, 388 Yuhangtang Road, Hangzhou 310058, China; and cLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065 Contributed by Robert G. Roeder, February 16, 2010 (sent for review January 18, 2010) Mediator recently has emerged as a central player in the direct (7–9). In general, individual Mediator subunits interact transduction of signals from transcription factors to the general specifically with their corresponding transcription factors and de- transcriptional machinery. In the case of nuclear receptors, in vitro letions of these Mediator subunits often affect expression primar- studies have shown that the transcriptional coactivator function of ily of target genes and pathways controlled by their corresponding the Mediator involves direct ligand-dependent interactions of the transcription factor(s) (9). In the case of nuclear receptors, the MED1 subunit, through its two classical LxxLL motifs, with the re- Mediator interactions are ligand- and AF-2-dependent and ceptor AF2 domain. However, despite the strong in vitro evidence, mediated through the LxxLL motifs in the MED1 (a.k.a. there currently is little information regarding in vivo functions of TRAP220/PBP/DRIP205) subunit (10–13). Importantly, in rela- the LxxLL motifs either in MED1 or in other coactivators.
    [Show full text]
  • Integrase Interactor 1 (INI-1) Deficient Renal Cell Carcinoma
    Open Access Case Report DOI: 10.7759/cureus.13082 Integrase Interactor 1 (INI-1) Deficient Renal Cell Carcinoma Manpreet Singh 1 , Harkirat Singh 1 , Benjamin Hambro 1 , Jasleen Kaur 1 , Ravi Rao 2 1. Internal Medicine, St Agnes Medical Center, Fresno, USA 2. Hematology and Oncology, St Agnes Medical Center, Fresno, USA Corresponding author: Manpreet Singh, [email protected] Abstract Members of the SWItch/sucrose nonfermentable (SWI-SNF) family, including SWI/SNF related, matrix- associated, actin-dependent regulator of chromatin, subfamily A, member 4 (SMARCA4), SWI/SNF related, matrix‐associated, actin‐dependent regulator of chromatin, subfamily B member 1 (SMARCB1)/integrase interactor 1 (INI-1) are known tumor suppressor genes. Interactions between SMARCB1/INI-1 and key protein components in various cellular pathways are related to tumor progression and proliferation. SMARCB1/INI-1 protein was undetectable in rhabdoid tumor cells, whereas non-tumorous cells express the SMARCB1/INI-1 genes. Germline and sporadic mutations of several genes encoding for proteins in this complex are known to cause a spectrum of cancers, usually with sarcomatoid features which include a very aggressive renal medullary carcinoma. We report a case of a 29-year-old male who presented with SMARCA4 deficient renal tumor with a very aggressive clinical behavior which ultimately led to his death. Categories: Nephrology, Oncology Keywords: renal medullary carcinoma, ini-1, renal cell carcinoma, swi/snf, smarcb1, integrase interactor 1 Introduction Renal medullary carcinoma is a rare and very aggressive malignancy affecting young adults with rare cases in patients with sickle cell disease or trait [1]. The tumor arises predominantly in the renal medulla and exhibits a variety of growth patterns including reticular, solid, tubular, trabecular, cribriform, sarcomatoid, and micropapillary [1].
    [Show full text]
  • Comparison of Immunohistochemistry with Immunoassay (ELISA
    British Journal of Cancer (1999) 79(9/10), 1534–1541 © 1999 Cancer Research Campaign Article no. bjoc.1998.0245 Comparison of immunohistochemistry with immunoassay (ELISA) for the detection of components of the plasminogen activation system in human tumour tissue CM Ferrier1, HH de Witte2, H Straatman3, DH van Tienoven2, WL van Geloof1, FJR Rietveld1, CGJ Sweep2, DJ Ruiter1 and GNP van Muijen1 Departments of 1Pathology, 2Chemical Endocrinology and 3Epidemiology, University Hospital Nijmegen, PO Box 9101, 6500 HB Nijmegen, The Netherlands Summary Enzyme-linked immunosorbent assay (ELISA) methods and immunohistochemistry (IHC) are techniques that provide information on protein expression in tissue samples. Both methods have been used to investigate the impact of the plasminogen activation (PA) system in cancer. In the present paper we first compared the expression levels of uPA, tPA, PAI-1 and uPAR in a compound group consisting of 33 cancer lesions of various origin (breast, lung, colon, cervix and melanoma) as quantitated by ELISA and semi-quantitated by IHC. Secondly, the same kind of comparison was performed on a group of 23 melanoma lesions and a group of 28 breast carcinoma lesions. The two techniques were applied to adjacent parts of the same frozen tissue sample, enabling the comparison of results obtained on material of almost identical composition. Spearman correlation coefficients between IHC results and ELISA results for uPA, tPA, PAI-1 and uPAR varied between 0.41 and 0.78, and were higher for the compound group and the breast cancer group than for the melanoma group. Although a higher IHC score category was always associated with an increased median ELISA value, there was an overlap of ELISA values from different scoring classes.
    [Show full text]
  • Immunoassay - Elisa
    IMMUNOASSAY - ELISA PHUBETH YA-UMPHAN National Institute of Health, Department of Medical Sciences 0bjective After this presentation, participants will be able to Explain how an ELISA test determines if a person has certain antigens or antibodies . Explain the process of conducting an ELISA test. Explain interactions that take place at the molecular level (inside the microtiter well) during an ELISA test. Outline - Principal of immunoassay - Classification of immunoassay Type of ELISA - ELISA ELISA Reagents General - Applications Principal of ELISA ELISA workflow What is immunoassay? Immunoassays are bioanalytical methods that use the specificity of an antigen-antibody reaction to detect and quantify target molecules in biological samples. Specific antigen-antibody recognition Principal of immunoassay • Immunoassays rely on the inherent ability of an antibody to bind to the specific structure of a molecule. • In addition to the binding of an antibody to its antigen, the other key feature of all immunoassays is a means to produce a measurable signal in response to the binding. Classification of Immunoassays Immunoassays can be classified in various ways. Unlabeled Labeled Competitive Homogeneous Noncompetitive Competitive Heterogeneous Noncompetitive https://www.sciencedirect.com/science/article/pii/S0075753508705618 Classification of Immunoassays • Unlabeled - Immunoprecipitation • Labeled Precipitation of large cross-linked Ag-Ab complexes can be visible to the naked eyes. - Fluoroimmnoassay (FIA) - Radioimmunoassay (RIA) - Enzyme Immunoassays (EIA) - Chemiluminescenceimmunoassay(CLIA) - Colloidal Gold Immunochromatographic Assay (ICA) https://www.creative-diagnostics.com/Immunoassay.htm Classification of Immunoassays • Homogeneous immunoassays Immunoassays that do not require separation of the bound Ag-Ab complex. (Does not require wash steps to separate reactants.) Example: Home pregnancy test. • Heterogeneous immunoassays Immunoassays that require separation of the bound Ag-Ab complex.
    [Show full text]
  • Datasheet PB1029 Anti-AEBP2 Antibody
    Product datasheet Anti-AEBP2 Antibody Catalog Number: PB1029 BOSTER BIOLOGICAL TECHNOLOGY Special NO.1, International Enterprise Center, 2nd Guanshan Road, Wuhan, China Web: www.boster.com.cn Phone: +86 27 67845390 Fax: +86 27 67845390 Email: [email protected] Basic Information Product Name Anti-AEBP2 Antibody Gene Name AEBP2 Source Rabbit IgG Species Reactivity human,mouse,rat Tested Application WB,IHC-P,ICC/IF,FCM Contents 500ug/ml antibody with PBS ，0.02% NaN3 , 1mg BSA and 50% glycerol. Immunogen E.coli-derived human AEBP2 recombinant protein (Position: K424-Q517). Human AEBP2 shares 98.8% amino acid (aa) sequence identity with mouse AEBP2. Purification Immunogen affinity purified. Observed MW 54KD Dilution Ratios Western blot: 1:500-2000 Immunohistochemistry(Paraffin-embedded Section): 1:50-400 Immunocytochemistry/Immunofluorescence (ICC/IF): 1:50-400 Flow cytometry (FCM): 1-3μg/1x106 cells Storage 12 months from date of receipt，-20℃ as supplied.6 months 2 to 8℃ after reconstitution. Avoid repeated freezing and thawing Background Information Adipocyte Enhancer-Binding Protein is a zinc finger protein that in humans is encoded by the evolutionarily well-conserved gene AEBP2. This gene is mapped to 12p12.3. AEBP2 is a DNA-binding transcriptional repressor. It may regulate the migration and development of the neural crest cells through the PRC2-mediated epigenetic mechanism and is most likely a targeting protein for the mammalian PRC2 complex. Reference Anti-AEBP2 Antibody被引用在0文献中。 暂无引用 FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC AND CLINICAL USE. 1 Product datasheet Anti-AEBP2 Antibody Catalog Number: PB1029 BOSTER BIOLOGICAL TECHNOLOGY Special NO.1, International Enterprise Center, 2nd Guanshan Road, Wuhan, China Web: www.boster.com.cn Phone: +86 27 67845390 Fax: +86 27 67845390 Email: [email protected] Selected Validation Data Figure 1.
    [Show full text]
  • Bioinformatics Applications Through Visualization of Variations on Protein
    1 Bioinformatics applications through visualization of variations on protein structures, comparative functional genomics, and comparative modeling for protein structure studies A dissertation presented by Alper Uzun to The Department of Biology In partial fulfillment of the requirements for the degree of Doctor of Philosophy in the field of Biology Northeastern University Boston, Massachusetts July 2009 2 ©2009 Alper Uzun ALL RIGHTS RESERVED 3 Bioinformatics applications through visualization of variations on protein structures, comparative functional genomics, and comparative modeling for protein structure studies by Alper Uzun ABSTRACT OF DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biology in the Graduate School of Arts and Sciences of Northeastern University, July, 2009 4 Abstract The three-dimensional structure of a protein provides important information for understanding and answering many biological questions in molecular detail. The rapidly growing number of sequenced genes and related genomic information is intensively accumulating in the biological databases. It is significantly important to combine biological data and developing bioinformatics tools while information of protein sequences, structures and DNA sequences are exponentially growing. On the other hand, especially the number of known protein sequences is much larger than the number of experimentally solved protein structures. However the experimental methods cannot always be applied or protein structures
    [Show full text]
  • ` Probing the Epigenome Andrea Huston1, Cheryl H Arrowsmith1,2
    ` Probing the Epigenome Andrea Huston1, Cheryl H Arrowsmith1,2, Stefan Knapp3,4,*, Matthieu Schapira1,5,* 1. Structural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada 2. Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto , Toronto, ON M5G 1L7, Canada 3. Nuffield Department of Clinical Medicine, Target Discovery Institute, and Structural Genomic Consortium, University of Oxford, Headington, Oxford OX3 7DQ, United Kingdom 4. Institute for Pharmaceutical Chemistry, Johann Wolfgang Goethe University, D-60438 Frankfurt am Main, Germany 5. Department of Pharmacology and Toxicology, University of Toronto, Toronto, ON M5S 1A8, Canada * Correspondence: [email protected], [email protected] Epigenetic chemical probes are having a strong impact on biological discovery and target validation. Systematic coverage of emerging epigenetic target classes with these potent, selective, cell-active chemical tools will profoundly influence our understanding of the human biology and pathology of chromatin-templated mechanisms. ` Chemical probes are research-enablers Advances in genomics and proteomics methodologies in recent years have made it possible to associate thousands of genes and proteins with specific diseases, biological processes, molecular networks and pathways. However, data from these large scale initiatives alone has not translated widely into new studies on these disease-associated proteins, and the biomedical research community still tends to focus on proteins that were already known before the sequencing of the human genome1. The human kinome for instance, a target class of direct relevance to cancer and other disease areas, is a telling example: based on the number of research articles indexed in pubmed in 2011, 75% of the research activity focused on only 10% of the 518 human kinases – largely the same kinases that were the focus of research before sequencing of the human genome - while 60% of the kinome, some 300 enzymes, was virtually ignored by the community2.
    [Show full text]
  • Table S1 the Four Gene Sets Derived from Gene Expression Profiles of Escs and Differentiated Cells
    Table S1 The four gene sets derived from gene expression profiles of ESCs and differentiated cells Uniform High Uniform Low ES Up ES Down EntrezID GeneSymbol EntrezID GeneSymbol EntrezID GeneSymbol EntrezID GeneSymbol 269261 Rpl12 11354 Abpa 68239 Krt42 15132 Hbb-bh1 67891 Rpl4 11537 Cfd 26380 Esrrb 15126 Hba-x 55949 Eef1b2 11698 Ambn 73703 Dppa2 15111 Hand2 18148 Npm1 11730 Ang3 67374 Jam2 65255 Asb4 67427 Rps20 11731 Ang2 22702 Zfp42 17292 Mesp1 15481 Hspa8 11807 Apoa2 58865 Tdh 19737 Rgs5 100041686 LOC100041686 11814 Apoc3 26388 Ifi202b 225518 Prdm6 11983 Atpif1 11945 Atp4b 11614 Nr0b1 20378 Frzb 19241 Tmsb4x 12007 Azgp1 76815 Calcoco2 12767 Cxcr4 20116 Rps8 12044 Bcl2a1a 219132 D14Ertd668e 103889 Hoxb2 20103 Rps5 12047 Bcl2a1d 381411 Gm1967 17701 Msx1 14694 Gnb2l1 12049 Bcl2l10 20899 Stra8 23796 Aplnr 19941 Rpl26 12096 Bglap1 78625 1700061G19Rik 12627 Cfc1 12070 Ngfrap1 12097 Bglap2 21816 Tgm1 12622 Cer1 19989 Rpl7 12267 C3ar1 67405 Nts 21385 Tbx2 19896 Rpl10a 12279 C9 435337 EG435337 56720 Tdo2 20044 Rps14 12391 Cav3 545913 Zscan4d 16869 Lhx1 19175 Psmb6 12409 Cbr2 244448 Triml1 22253 Unc5c 22627 Ywhae 12477 Ctla4 69134 2200001I15Rik 14174 Fgf3 19951 Rpl32 12523 Cd84 66065 Hsd17b14 16542 Kdr 66152 1110020P15Rik 12524 Cd86 81879 Tcfcp2l1 15122 Hba-a1 66489 Rpl35 12640 Cga 17907 Mylpf 15414 Hoxb6 15519 Hsp90aa1 12642 Ch25h 26424 Nr5a2 210530 Leprel1 66483 Rpl36al 12655 Chi3l3 83560 Tex14 12338 Capn6 27370 Rps26 12796 Camp 17450 Morc1 20671 Sox17 66576 Uqcrh 12869 Cox8b 79455 Pdcl2 20613 Snai1 22154 Tubb5 12959 Cryba4 231821 Centa1 17897
    [Show full text]
  • 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.
    [Show full text]
  • 4-6 Weeks Old Female C57BL/6 Mice Obtained from Jackson Labs Were Used for Cell Isolation
    Methods Mice: 4-6 weeks old female C57BL/6 mice obtained from Jackson labs were used for cell isolation. Female Foxp3-IRES-GFP reporter mice (1), backcrossed to B6/C57 background for 10 generations, were used for the isolation of naïve CD4 and naïve CD8 cells for the RNAseq experiments. The mice were housed in pathogen-free animal facility in the La Jolla Institute for Allergy and Immunology and were used according to protocols approved by the Institutional Animal Care and use Committee. Preparation of cells: Subsets of thymocytes were isolated by cell sorting as previously described (2), after cell surface staining using CD4 (GK1.5), CD8 (53-6.7), CD3ε (145- 2C11), CD24 (M1/69) (all from Biolegend). DP cells: CD4+CD8 int/hi; CD4 SP cells: CD4CD3 hi, CD24 int/lo; CD8 SP cells: CD8 int/hi CD4 CD3 hi, CD24 int/lo (Fig S2). Peripheral subsets were isolated after pooling spleen and lymph nodes. T cells were enriched by negative isolation using Dynabeads (Dynabeads untouched mouse T cells, 11413D, Invitrogen). After surface staining for CD4 (GK1.5), CD8 (53-6.7), CD62L (MEL-14), CD25 (PC61) and CD44 (IM7), naïve CD4+CD62L hiCD25-CD44lo and naïve CD8+CD62L hiCD25-CD44lo were obtained by sorting (BD FACS Aria). Additionally, for the RNAseq experiments, CD4 and CD8 naïve cells were isolated by sorting T cells from the Foxp3- IRES-GFP mice: CD4+CD62LhiCD25–CD44lo GFP(FOXP3)– and CD8+CD62LhiCD25– CD44lo GFP(FOXP3)– (antibodies were from Biolegend). In some cases, naïve CD4 cells were cultured in vitro under Th1 or Th2 polarizing conditions (3, 4).
    [Show full text]