Protein Sulfation Service
Services

Protein Sulfation Service

Sulfation is a post-translational modification (PTM) of which tyrosine sulfation is probably one of the most common protein PTMs. Protein sulfation affects many biological processes, including cell signaling, detoxification, hormone regulation, molecular recognition, viral entry into host cells, etc. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein sulfation service to accelerate your project.

Protein sulfation is a very common PTM, facilitated by the addition of oxygen or nitrogen sulfate groups, respectively, and typically occurs on secreted and transmembrane-bound proteins and glycoproteins. It is estimated that up to 1% of all tyrosine residues present in proteins may be sulfated in a given organism. Protein tyrosine sulfation (PTS) is also an enzymatic modification in which the sulfo group from a 3'-phosphoadenosine-5' phosphosulfate (PAPS) donor is passed through tyrosine protein sulfotransferase (TPST) transferred to the hydroxyl group of tyrosine residues. Many of the tyrosine sulfated proteins are involved in protein-protein interactions. Studies have shown that tyrosine sulfation is a key factor in many diseases, including autoimmune responses, HIV infection, lung disease, multiple sclerosis, and cellular enzyme regulation. However, so far, little information is available on the sulfation of recombinant therapeutic proteins (RTPs) and monoclonal antibodies (mAbs).

Protein tyrosine sulfation (PTS) and its biological path. Fig 1. Protein tyrosine sulfation (PTS) and its biological path.(Yang YS, et al., 2015)

Services

The importance of post-translational protein tyrosine sulfation (PTS) of membrane and secreted proteins is widely recognized in biology for its role and potential as a target for drug development. However, only a small fraction of sulfated proteins are currently known, and understanding the mechanism of protein sulfation is challenging. Creative BioMart has successfully used a variety of techniques to reliably study protein sulfation to fully understand the sulfation state of proteins. In addition, we are working on developing computational software tools for predicting tyrosine sulfation sites in protein sequences.

TPST is the enzyme responsible for biological PTS, which is present in a variety of organisms. Only limited tools are currently available for the study of PTS. Therefore, our scientists explored the function of PTS in inducing protein-protein interactions and subsequent biochemical and physiological responses by studying the natural substrates of TPST. We provide the following services for protein sulfation, including but not limited to:

  • Preparation and purification of TPST: we have employed several types of affinity chromatography to facilitate TPST purification, purifying TPST in a homogeneous form.
  • TPST cloning, sequence, and structural analysis: predicting and validating TPST enzyme properties by gene sequence analysis.
  • Detecting protein sulfation: target known sulfated proteins. We use a variety of cutting-edge techniques for detecting various sulfated sites, monitoring molecular weight changes before and after PTM, and characterizing the identification and screening of TPST and its protein substrates.

Approaches for Analyzing Protein Sulfation

  • Radioisotope labeling.
  • Edman sequencing.
  • Amino acid tag.
  • Fluorescence method.
  • Two-dimensional gel electrophoresis.
  • Peptide mapping.
  • Mass spectrometry.
  • Bioinformatics tools.

Our mission is to provide global customers with the most comprehensive and professional customized protein sulfation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.

References

  1. Yang YS, Wang CC, Chen BH, et al.. (2015) Tyrosine sulfation as a protein post-translational modification. Molecules. 20(2): 2138-64.
  2. Kehoe JW, Bertozzi CR. (2000) Tyrosine sulfation: a modulator of extracellular protein-protein interactions. Chem Biol. 7(3): R57-61.
For research use only, not intended for any clinical use.