Abgent

Abgent is a global biotechnology company based in San Diego, California, US with offices in Maidenhead, UK and Suzhou, China and distributors around the world. Abgent develops antibodies and related agents to study proteins involved in cellular function and disease. Abgent's antibodies target key areas of research including autophagy, neuroscience, cancer, stem cells and more. Abgent was acquired in 2011 by WuXi AppTec, a global pharmaceutical, biopharmaceutical, and medical device outsourcing company with operations in China and the United States.[1]

Abgent, a WuXi AppTec company
Public
Traded asNYSE: WX
IndustryBiotech, Life Sciences, Manufacturing
FoundedSan Diego, California, United States (2001)
Headquarters
US
Area served
Worldwide
Productsantibodies,
peptides,
custom antibody services,
custom peptide services,
custom protein services
Number of employees
200 (2014)
Websiteabgent.com

Peer review

Abgent was listed as a selected supplier in Nature Magazine,[2] Antibody Technology, Drug Discovery Features and The Scientist's cell signaling feature. More than 1,100 peer-reviewed publications[3] in scientific journals have cited Abgent antibody, protein, and peptide products and custom services.

Core business

As one of the world's largest manufacturers of antibodies for biological research and drug discovery, Abgent develops, produces, and sells antibodies for use in academic, biotechnological, and pharmaceutical industries. Core products are complemented by custom antibody services and custom protein services for drug discovery targets.

Tools

SUMOplot Analysis Program

SUMOplot is a tool used to predict sumoylation sites, an important post-translational modification of proteins. SUMO-modified proteins contain the tetrapeptide motif B-K-x-D/E where B is a hydrophobic residue, K is the lysine conjugated to SUMO, x is any amino acid (aa), D or E is an acidic residue. Substrate specificity appears to be derived directly from Ubc9 and the respective substrate motif. SUMOplot predicts the probability for the SUMO consensus sequence (SUMO-CS) to be engaged in SUMO attachment. The SUMOplot score system is based on two criteria: first, direct amino acid match to the SUMO-CS observed and shown to bind Ubc9, and second, substitution of the consensus amino acid residues with amino acid residues exhibiting similar hydrophobicity. SUMOplot has been used in the past to predict Ubc9 dependent sites.[4][5][6][7][8][9][10][11][12]

Autophagy Receptor Motif Plotter

The autophagy pathway is mediated by selective receptors. They recognize and sort diverse cargo substrates (e.g., proteins, organelles, pathogens) for delivery to the autophagic machinery. Known autophagy receptors are characterized by short linear sequence motifs (autophagy receptor motifs, or ARMs) responsible for the interaction with the Atg8/LC3 family. Many ARM-containing proteins (ARM-CPs) are also involved in autophagosome formation and maturation and a few of them in regulating signaling pathways. Autophagy Receptor Motif Plotter assists in the identification of novel ARM-CPs. Users input a given an amino acid sequence into the web-enabled tool, and the program identifies internal sequences matching a pattern within the 3 classes of the extended ARM motif (x6-W/F/Yxxx-x2). The program then computes and lists the top four scores for each motif class (W-, F-, Y-). The full sequence of the ARM-CP is displayed, where ARMs are colored by their score and ranked score-values are presented in tabular form.[13][14][15]

gollark: Encryption, I mean.
gollark: No, that's totally different and unrelated.
gollark: What?
gollark: IIRC you can't really make your own enzymes easily or edit them much, because they have weird folding stuff going on, and are hyperoptimized by billions of years (well, for some of them, just hundreds or tens of millions in others) of evolution for their particular tasks.
gollark: Not specifically for that, but practice exam questions?

See also

References
  1. WuXi PharmaTech Acquires Abgent, a Leading Producer of Biological Research Reagents. Oct 14, 2011.
  2. Technology Feature - Table of Suppliers. (2004) Nature 428(6979) p232
  3. HireWire Abgent Publication Search Results
  4. Gramatikoff K. et al. In Frontiers of Biotechnology and Pharmaceuticals, Science Press USA Inc 2004; 4: 181 - 210
  5. Vyacheslav Yurchenko, Zhu Xue, and Moshe J. Sadofsky. SUMO Modification of Human XRCC4 Regulates Its Localization and Function in DNA Double-Strand Break Repair Mol. Cell. Biol., Mar 2006; 26: 1786 - 1794
  6. Meiluen Yang, Chia-Tse Hsu, Chun-Yuan Ting, Leroy F. Liu, and Jaulang Hwang. Assembly of a Polymeric Chain of SUMO1 on Human Topoisomerase I in Vitro J. Biol. Chem., Mar 2006; 281: 8264 - 8274
  7. Yutaka Morita, Chie Kanei-Ishii, Teruaki Nomura, and Shunsuke Ishii. TRAF7 Sequesters c-Myb to the Cytoplasm by Stimulating Its Sumoylation. Mol. Biol. Cell, Nov 2005; 16: 5433 - 5444
  8. Zhongshu Tang, Oussama El Far, Heinrich Betz, and Astrid Scheschonka. Pias1 Interaction and Sumoylation of Metabotropic Glutamate Receptor 8. J. Biol. Chem., Nov 2005; 280: 38153 - 38159
  9. Brigit E. Riley, Huda Y. Zoghbi, and Harry T. Orr. SUMOylation of the Polyglutamine Repeat Protein, Ataxin-1, Is Dependent on a Functional Nuclear Localization Signal. J. Biol. Chem., Jun 2005; 280: 21942 - 21948
  10. Timothy A. Hinsley, Pamela Cunliffe, Hannah J. Tipney, Andrew Brass, and May Tassabehji. Comparison of TFII-I gene family members deleted in Williams-Beuren syndrome. Protein Sci., Oct 2004; 13: 2588 - 2599
  11. Frederik Van Dyck, Els L. D. Delvaux, Wim J. M. Van de Ven, and Marcela V. Chavez. Repression of the Transactivating Capacity of the Oncoprotein PLAG1 by SUMOylation. J. Biol. Chem., Aug 2004; 279: 36121 - 36131.
  12. Tianwei Li, Evgenij Evdokimov, Rong-Fong Shen, Chien-Chung Chao, Ephrem Tekle, Tao Wang, Earl R. Stadtman, David C. H. Yang, and P. Boon Chock. Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis. PNAS, Jun 2004; 101: 8551 - 8556
  13. Noda et al (2010) FEBS Letters 584: 1379-85 PMID 20083108
  14. Birgisdottir et al (2013) J Cell Sci 126: 3237-47 PMID 23908376
  15. Rogov et al (2014) Molecular Cell 53: 167-78 PMID 24462201
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