metabolomics service

Metabolomics service is the study of metabolism, specifically the science of identifying and quantifying the biochemical byproducts of metabolism, called cellular metabolites. This is achievedby using analytical technologies such as NMR and mass spectrometry combined with sophisticated statistical methods to interpret the generated data. Compared with genomics, transcriptomics and proteomics, metabolomics provide a direct and global snapshot of all the metabolites, and tell the researchers what have happened, making it more and more popular in disease research, toxicology,environmental analysis, agriculture, biofuel development and nutrition.

The routine procedure of metabolomic research can be divided into untargeted and targeted. The formeraims for a quick and reliable identification of small molecule metabolites for a particular physiological state in response to internal or external perturbations; and the latter provides an accurate quantitation of metabolites the researcher are interested in, able to screen and validate biomarkers for medical research.

Creative Proteomics is a professional and component CRO with experienced bioanalysts and technicians, which can provide reliable and customer-tailored service, with rapid analytical procedures to speed up your research, and detailed and easy-to-read report for your publications.

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Researchers from Lawrence Livermore National Laboratory (LLNL) assisted a team from the University of Melbourne (link is external) in discovering how methylmercury enters the Antarctic sea and bioaccumulates in the marine food web.

LLNL scientists Michael Thelen and Adam Zemla performed protein sequence analysis and structural modeling to predict key proteins involved in mercury methylation.

Thelen explained: "We examined the sequence data obtained from DNA samples collected in sea ice and other Southern ocean environments. A candidate sequence for a mercury methylation enzyme was found in a bacterial strain of the genus Nitrospina. Then Adam used computational tools he developed at the Lab to predict the structure and show in an elegant model how the active site of the enzyme would react with mercury."

Mercury (Hg) created from volcanoes and human activity such as burning fossil fuels circulates in the atmosphere then deposits onto sea ice. The marine nitrite-oxidizing bacterium Nitrospina, may convert Hg to methylmercury (MeHg), which is released into the Southern Ocean, where it enters the marine food web. Scientists are concerned that MeHg stored in the fatty tissues of fish would contain more mercury than humans can handle and could be a public health concern in the future.

"Further research could physically confirm the proteins responsible for Hg methylation in Nitrospina, and perhaps could help us find a way to inhibit or to reverse the reaction to reduce methylmercury poisoning," Thelen said.

Samples were collected from snow, sea ice, brine and surface sea water across five pack-ice stations during the second Sea Ice Physics and Ecosystem eXperiment (link is external) (SIPEX). Those taken from various depths of sea water under seasonal ice cover showed Hg concentrations significantly higher than those taken from open water. These ice-covered sea water Hg concentrations increased southward. The study proposes that ocean bacteria may convert Hg to MeHg, and supports this with the identification of bacterial enzymes required for this reaction.

The research from Lawrence Livermore National Laboratory, University of Melbourne, and U.S. Geological Survey (link is external) appears in the Aug. 1 online edition of Nature Microbiology (link is external).

The work is funded by the Department of Energy's Office of Science.


Related service: protein methylation

Our motivation for developing zebrafish specific rabbit monoclonal antibodies

Although zebrafish has been a very powerful model in biomedical research, less than 3% of zebrafish proteins have available antibodies, not to mention monoclonal antibodies. Yurogen Biosystems LLC would like to bring our proprietary single cell based SMabTM platform and develop rabbit monoclonal antibodies (RmAbs) to zebrafish proteins to remove this reagent hurdle that hinders many research projects in fast-growing zebrafish field. With the help from zebrafish community, we will rigorously validate our recombinant RmAbs to ensure they will work reproducibly for specific applications such as western blotting or whole mount immunofluorescence staining. In addition, we can deliver the gene sequences of RmAbs to enhance reproducibility and ease antibody engineering for special applications such as generating transgenic zebrafish with specific RmAbs to knock down protein function in a controllable manner. We envision that RmAbs will be important and powerful addition to expand the current zebrafish research resources.

Advantages of rabbit monoclonal antibodies

Unlike mice and other rodents, rabbit has a better immune system which can generate antibodies with greater diversity, higher affinity, broader epitope recognition, and better stability [1]. Therefore, RmAbs have many advantages which set them apart from traditional mouse antibodies. Taking advantage of our robust SMabTM platform, we can quickly and efficiently generate high quality rabbit monoclonal antibodies for a variety of antigens.

High Affinity Typically, RmAbs have 10 – 100 times higher affinity than mouse monoclonal antibodies. On average, the KD values of RmAbs are range from 10-12 M up to 10-14 M [3].

Superior Specificity The development of primary and secondary antibody repertoires in rabbits possesses unique characteristics, such as gut-associated lymphoid tissues (GALT) B cell development and multiple selection procedures. These unique characteristics may account for the improved quality of the antibodies produced in rabbit [4,5]. The high specificity of RmAbs has clear edges in assays: improved assay sensitivity, improve accuracy with decreased false positive rate, and lower background noises. These features make RmAbs ideal choices for stringent assays including IHC in clinics [6].

Broad Epitope Recognition including Haptens Due to its reduced immunodominance, rabbit antigen presenting cells can present broader range of epitopes than their mouse counterparts. Many less abundant proteins or epitopes can be well presented and recognized by rabbits. Rabbits are therefore able to generate high affinity antibodies against difficult epitopes, such as protein modifications, enzyme cleavage sites, or conformational epitopes. Partially due to the expression of all three subclasses of CD1 proteins, the non-peptidic epitope presenting in rabbits is more efficient. As a result, rabbit can handle haptens better than mice and is widely adopted as preferable host to generate better antibodies to haptens, including small molecule drugs, steroid hormones, lipids, and glycolipids.

Great Stability and Long Shelf-life Rabbit IgG has extra disulfide bonds in the variable region of the heavy chain and an extra disulfide bond between Vκ and Cκ. These extra disulfide bonds may result in the great stability and long shelf-life of rabbit antibodies.


About Yurogen

Yurogen Biosystems LLC is found in 2015, located in the Greater Boston area. Yurogen strives to become a leading provider of premium monoclonal antibodies and antibody-based products for our customers in both research community and industries. Yurogen has developed an innovative single cell based SMabTM platform that can efficiently screen monoclonal antibodies from a variety of host animal in a cost-efficient manner without sacrificing antibody quality. Since 2015, Yurogen has quickly established and is actively marketing our own product lines of RmAbs. In addition to our own product lines, we offer full scope of antibody CRO services including antigen design and production, and antibody screening, engineering, and production.



1. Schiaffella E, Sehgal D, Anderson A, Mage R. Gene conversion and hypermutation during diversification of VH sequences in developing splenic germinal centers of immunized rabbits. J Immunol. 1999;162:3984-95.

2. Pan R, Chen Y, Vaine M, Hu G, Wang S, Lu S, Kong XP. Structural analysis of a novel rabbit monoclonal antibody R53 targeting an epitope in HIV-1 gp120 C4 region critical for receptor and co-receptor binding. Emerg Microbes Infect. 2015 Jul;4(7)

3. Gendusa R, Scalia C, Buscone S, Cattoretti G. Elution of High-affinity (>10-9 KD) Antibodies from Tissue Sections: Clues to the Molecular Mechanism and Use in Sequential Immunostaining. J Histochem Cytochem. 2014;62:519-531

4. Rossi S, Laurino L, Furlanetto A, Chinellato S, Orvieto E, Canal F, et al. Rabbit monoclonal antibodies: a comparative study between a novel category of immunoreagents and the corresponding mouse monoclonal antibodies. Am J Clin Pathol. 2005;124:295-302

5. Rocha R, Nunes C, Rocha G, Oliveira F, Sanches F, Gobbi H. Rabbit monoclonal antibodies show higher sensitivity than mouse monoclonals for estrogen and progesterone receptor evaluation in breast cancer by immunohistochemistry. Pathol Res Pract. 2008;204:655-62

6. Vilches-Moure J, Ramos-Vara J. Comparison of rabbit monoclonal and mouse monoclonal antibodies in immunohistochemistry in canine tissues. J Vet Diagn Invest. 2005;17:346-50