Abgent

Last updated
Abgent, a WuXi AppTec company
Type Public
NYSE:  WX
Industry Biotech, Life Sciences, Manufacturing
Founded San Diego, California, United States (2001)
Headquarters
US
Area served
Worldwide
Products antibodies,
peptides,
custom antibody services,
custom peptide services,
custom protein services
Number of employees
200 (2014)
Parent WuXi AppTec
Website abgent.com

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]

Contents

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]

See also

Related Research Articles

MAFA is a type II membrane glycoprotein, first identified on the surface of rat mucosal-type mast cells of the RBL-2H3 line. More recently, human and mouse homologues of MAFA have been discovered yet also expressed by NK and T-cells. MAFA is closely linked with the type 1 Fcɛ receptors in not only mucosal mast cells of humans and mice but also in the serosal mast cells of these same organisms.

<span class="mw-page-title-main">SUMO protein</span> Family of proteins which attach to other proteins to modify them

In molecular biology, SUMOproteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. This process is called SUMOylation. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.

<span class="mw-page-title-main">Oncostatin M</span> Mammalian protein found in Homo sapiens

Oncostatin M, also known as OSM, is a protein that in humans is encoded by the OSM gene.

<span class="mw-page-title-main">Anthrax toxin</span> Tripartite protein complex secreted by virulent strains of Bacillus anthracis

Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis—the causative agent of anthrax. The toxin was first discovered by Harry Smith in 1954. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). These three protein components act together to impart their physiological effects. Assembled complexes containing the toxin components are endocytosed. In the endosome, the enzymatic components of the toxin translocate into the cytoplasm of a target cell. Once in the cytosol, the enzymatic components of the toxin disrupts various immune cell functions, namely cellular signaling and cell migration. The toxin may even induce cell lysis, as is observed for macrophage cells. Anthrax toxin allows the bacteria to evade the immune system, proliferate, and ultimately kill the host animal. Research on anthrax toxin also provides insight into the generation of macromolecular assemblies, and on protein translocation, pore formation, endocytosis, and other biochemical processes.

<span class="mw-page-title-main">Serine/threonine-specific protein kinase</span> Class of protein kinase enzymes

A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).

<span class="mw-page-title-main">SUMO enzymes</span>

SUMO enzymatic cascade catalyzes the dynamic posttranslational modification process of sumoylation. The Small Ubiquitin-related Modifier, SUMO-1, is a ubiquitin-like family member that is conjugated to its substrates through three discrete enzymatic steps : activation, involving the E1 enzyme (SAE1/SAE2); conjugation, involving the E2 enzyme (UBE2I); substrate modification, through the cooperation of the E2 and E3 protein ligases.

<span class="mw-page-title-main">UBE2I</span> Protein-coding gene in the species Homo sapiens

SUMO-conjugating enzyme UBC9 is an enzyme that in humans is encoded by the UBE2I gene. It is also sometimes referred to as "ubiquitin conjugating enzyme E2I" or "ubiquitin carrier protein 9", even though these names do not accurately describe its function.

<span class="mw-page-title-main">IGFBP7</span> Protein-coding gene in the species Homo sapiens

Insulin-like growth factor-binding protein 7 is a protein that in humans is encoded by the IGFBP7 gene. The major function of the protein is the regulation of availability of insulin-like growth factors (IGFs) in tissue as well as in modulating IGF binding to its receptors. IGFBP7 binds to IGF with low affinity compared to IGFBPs 1-6. It also stimulates cell adhesion. The protein is implicated in some cancers.

<span class="mw-page-title-main">SOGA2</span> Protein-coding gene in the species Homo sapiens

SOGA2, also known as Suppressor of glucose autophagy associated 2 or CCDC165, is a protein that in humans is encoded by the SOGA2 gene. SOGA2 has two human paralogs, SOGA1 and SOGA3. In humans, the gene coding sequence is 151,349 base pairs long, with an mRNA of 6092 base pairs, and a protein sequence of 1586 amino acids. The SOGA2 gene is conserved in gorilla, baboon, galago, rat, mouse, cat, and more. There is distant conservation seen in organisms such as zebra finches and anoles. SOGA2 is ubiquitously expressed in humans, with especially high expression in brain, colon, pituitary gland, small intestine, spinal cord, testis and fetal brain.

A nuclear export signal (NES) is a short target peptide containing 4 hydrophobic residues in a protein that targets it for export from the cell nucleus to the cytoplasm through the nuclear pore complex using nuclear transport. It has the opposite effect of a nuclear localization signal, which targets a protein located in the cytoplasm for import to the nucleus. The NES is recognized and bound by exportins.

<span class="mw-page-title-main">Protein aggregation</span> Accumulation of clumps of misfolded or disordered proteins

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease.

<span class="mw-page-title-main">UBA2</span> Protein-coding gene in the species Homo sapiens

Ubiquitin-like 1-activating enzyme E1B (UBLE1B) also known as SUMO-activating enzyme subunit 2 (SAE2) is an enzyme that in humans is encoded by the UBA2 gene.

<span class="mw-page-title-main">CCDC144A</span> Protein-coding gene in the species Homo sapiens

Coiled-coil domain-containing protein 144A is a protein that in humans is encoded by the CCDC144A gene. An alias of this gene is called KIAA0565. There are four members of the CCDC family: CCDC 144A, 144B, 144C and putative CCDC 144 N-terminal like proteins.

<span class="mw-page-title-main">Collagen, type XXIII, alpha 1</span> Mammalian protein found in Homo sapiens

Collagen α-1 (XXIII) chain is a protein encoded by COL23A1 gene, which is located on chromosome 5q35 in humans, and on chromosome 11B1+2 in mice. The location of this gene was discovered by genomic sequence analysis.

<span class="mw-page-title-main">SHLD1</span> Protein-coding gene in the species Homo sapiens

SHLD1 or shieldin complex subunit 1 is a gene on chromosome 20. The C20orf196 gene encodes an mRNA that is 1,763 base pairs long, and a protein that is 205 amino acids long.

<span class="mw-page-title-main">ZCCHC18</span> Protein-coding gene in the species Homo sapiens

Zinc finger CCHC-type containing 18 (ZCCHC18) is a protein that in humans is encoded by ZCCHC18 gene. It is also known as Smad-interacting zinc finger protein 2 (SIZN2), para-neoplastic Ma antigen family member 7b (PNMA7B), and LOC644353. Other names such as zinc finger, CCHC domain containing 12 pseudogene 1, P0CG32, ZCC18_HUMAN had been used to describe this protein.

<span class="mw-page-title-main">TEX9</span> Protein-coding gene in the species Homo sapiens

Testis-expressed protein 9 is a protein that in humans is encoded the TEX9 gene. TEX9 that encodes a 391-long amino acid protein containing two coiled-coil regions. The gene is conserved in many species and encodes orthologous proteins in eukarya, archaea, and one species of bacteria. The function of TEX9 is not yet fully understood, but it is suggested to have ATP-binding capabilities.

Putative uncharacterized protein C6orf52 (C6orf52) is a protein in humans that is encoded by the gene "C6orf52" and has six known isoforms. C6orf52 was identified in 2002 by The National Institutes of Health Mammalian Gene Collection (MGC) Program. C6orf52 has one known paralog, tRNA selenocysteine 1-associated protein 1 (TRNAU1AP).

<span class="mw-page-title-main">TMEM267</span> Protein

TMEM267 is a protein that in humans is encoded by the TMEM267 gene. It is a possible oncogene which encodes a transmembrane protein. The function of TMEM267 most likely involves transportation of molecules from the cytosol, as the presence of motifs and domains involved in transportation were conserved in orthologs. TMEM267 has orthologs in many species and is expressed at highest levels in the thyroid.

Transmembrane protein 39B (TMEM39B) is a protein that in humans is encoded by the gene TMEM39B. TMEM39B is a multi-pass membrane protein with eight transmembrane domains. The protein localizes to the plasma membrane and vesicles. The precise function of TMEM39B is not yet well-understood by the scientific community, but differential expression is associated with survival of B cell lymphoma, and knockdown of TMEM39B is associated with decreased autophagy in cells infected with the Sindbis virus. Furthermore, the TMEM39B protein been found to interact with the SARS-CoV-2 ORF9C protein. TMEM39B is expressed at moderate levels in most tissues, with higher expression in the testis, placenta, white blood cells, adrenal gland, thymus, and fetal brain.

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