Abgent is a San Diego biotechnology company that develops tools to profile post-translational modifications related to cellular function and disease. Abgent's antibodies cover targeting protein kinases (kinome), phosphatases, methyl and acetyl transferases, ubiquitin and SUMO, glycosylases and other protein modification enzymes. Flag Seal Nickname: Americas Finest City Location Location of San Diego within San Diego County Coordinates , Government County San Diego Mayor City Attorney         City Council District One District Two District Three District Four District Five District Six District Seven District Eight Jerry Sanders (R) Michael Aguirre Scott Peters Kevin... The structure of insulin Biotechnology is technology based on biology, especially when used in agriculture, food science, and medicine. ... Posttranslational modification is the chemical modification of a protein after its translation. ... Wikipedia does not yet have an article with this exact name. ... In biochemistry, a kinase is a type of enzyme that transfers phosphate groups from, for example, ATP to a specified substrate or target; the process is termed phosphorylation. Typically, the target is activated or energized by being phosphorylated. ... In molecular biology, the kinome is the ensemble of kinases that are expressed in a particular cell or present in the genome of an organism. ... A phosphatase is an enzyme that hydrolyses phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxy group. ... Wikipedia does not yet have an article with this exact name. ... Ubiquitin is a very conserved small regulatory protein that is ubiquitous in eukaryotes. ... For other uses, see Sumo (disambiguation). ... Neuraminidase ribbon diagram An enzyme (in Greek en = in and zyme = blend) is a protein, or protein complex, that catalyzes a chemical reaction and also controls the 3D orientation of the catalyzed substrates. ...

Peer review

Abgent's was listed as a selected supplier in Nature Magazine^[1], Antibody Technology, Drug Discovery Features and The Scientist's cell signaling feature Full list of citations^[2]. A cover of Nature Nature is one of the oldest and most reputable general-purpose scientific journals, first published on November 4, 1869. ... Each antibody binds to a specific antigen; an interaction similar to a lock and key. ... In medicine, biotechnology and pharmacology, drug discovery is the process by which drugs are discovered and/or designed. ... Cell signaling is part of a complex system of communication that governs basic cellular activities and coordinates cell actions. ...

Core business

Conversion of pseudo-Pro (ψPro) residues.

Abgent specilizes in FMOC solid-phase synthesis of peptides using pseudoproline to improve the quality of synthetic peptides^[3]. Pseudoproline dipeptides have been shown to increase the success rate for synthesizing both long and difficult peptides.^{[citation needed]} Pseudoproline dipeptides can be introduced in the same manner as other amino acid derivatives. The routine use of pseudoproline (oxazolidine) dipeptides in the FMOC solid phase pepdide sysnthesis (SPPS) of serine- and threonine-containing peptides has been shown to improve the quality and yield of crude products and helps avoid unnecessary repeat synthesis of failed sequences^[4]. Pseudoproline dipeptides have also been shown to be effective in the synthesis of intractable peptides, long peptides/small proteins, and cyclic peptides, enabling in many cases the production of peptides that are otherwise difficult to produce. The dipeptides are used by substituting a serine or threonine residue together with the preceding amino acid residue in the peptide sequence with the appropriate pseudoproline dipeptide. The native sequence is regenerated on cleavage and deprotection^[5][6][7]. In organic chemistry, peptide synthesis is the creation of peptides, which are organic compounds in which multiple amino acids bind via peptide bonds which are also known as amide bonds. ... In chemistry, solid-phase synthesis is a method in which molecules are bound on a bead and synthesized step-by-step in a reactant solution; compared with normal synthesis in a liquid state, it is easier to remove excess reactant or byproduct from the product. ... Peptides (from the Greek πεπτος, digestible), are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ... This article is about the class of chemicals. ... In mathematics, the derivative of a function is one of the two central concepts of calculus. ... Oxazolidines consist of one or more five-membered heterocyclic rings containing oxygen and nitrogen. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ... In organic chemistry, peptide synthesis is the creation of peptides, which are organic compounds in which multiple amino acids bind via peptide bonds which are also known as amide bonds. ... Serine (IPA ), organic compound, one of the 20 amino acids commonly found in animal proteins. ... Threonine is one of the 20 natural amino acids. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ... Serine (IPA ), organic compound, one of the 20 amino acids commonly found in animal proteins. ... Threonine is one of the 20 natural amino acids. ... This article is about the class of chemicals. ... Peptides (from the Greek πεπτος, digestible), are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. ... A dipeptide is a molecule consisting of two amino acids joined by a single peptide bond. ...

SUMOplot

SUMOplot software.

Most 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: 1) direct amino acid match to the SUMO-CS observed and shown to bind Ubc9, and 2) 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^{[8][9][10][11][12][13][14][15][16]}. In chemistry, hydrophobic or lipophilic species, or hydrophobes, tend to be electrically neutral and nonpolar, and thus prefer other neutral and nonpolar solvents or molecular environments. ... Lysine is one of the 20 amino acids normally found in proteins. ... Look up substrate in Wiktionary, the free dictionary. ... Look up substrate in Wiktionary, the free dictionary. ... This article is about the class of chemicals. ... In chemistry, hydrophobic or lipophilic species, or hydrophobes, tend to be electrically neutral and nonpolar, and thus prefer other neutral and nonpolar solvents or molecular environments. ...

References

1. ^ Technology Feature - Table of Suppliers. (2004) Nature 428(6979) p232
2. ^ Abgent's Full list of articles produced
3. ^ P. White, et al. (2004) J. Pept. Sci. 10, 18
4. ^ Balbach J, Schmid FX. (2000). Proline isomerization and its catalysis in protein folding. In Mechanisms of Protein Folding 2nd ed. Editor RH Pain. Oxford University Press.
5. ^ T. Haack & M. Mutter (1992) Tetrahedron Lett. 33, 1589
6. ^ W.R.Sampson, et al. (1999) J. Pept. Sci. 5, 403
7. ^ P. White, et al. (2003) Biopolymers, 71, 338.P156
8. ^ Gramatikoff K. et al. In Frontiers of Biotechnology and Pharmaceuticals, Science Press USA Inc 2004; 4: 181 - 210
9. ^ 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
10. ^ 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
11. ^ 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
12. ^ 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
13. ^ 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
14. ^ 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
15. ^ 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.
16. ^ 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

See also

• SUMO protein
• SUMO pathway
• SUMO network
• Autophagy network
• Ubiquitin
• Pseudoproline
• Aurora inhibitors
• Kinome
• Diet and cancer
• PRMT4 pathway

Small Ubiquitin-related Modifier or SUMO proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. ... The Autophagy network extracted from the recent 500 PubMed entries. ... Ubiquitin is a very conserved small regulatory protein that is ubiquitous in eukaryotes. ... In molecular biology, the kinome is the ensemble of kinases that are expressed in a particular cell or present in the genome of an organism. ... The methionine metabolism pathway. ... PRMT4 pathway Protein arginine N-methyltransferase-4 (PRMT4/CARM1)[1][2][3] methylation of arginine residues within proteins plays a critical key role in transcriptional regulation (see the PRMT4 pathway on the left). ...

External links

• This article contains material from the Science Primer published by the NCBI, which, as a U.S. government publication, is in the public domain.