Half-life Assay by SNAP-tag
For Research Use Only. Not for Clinical Use.
The stability and turnover of proteins in vivo is a carefully controlled parameter that affects numerous biological functions and degradation rate of extrinsic protein, which affects the potency of therapeutic proteins to a large extent. SNAP-tag fusion provides a widely suitable and stable combination strategy to enable the target proteins to be modified by other functional groups, which further reflect the in vivo half-life of protein drugs. Creative Biolabs is a leading service provider that focuses on therapeutic protein development. With years of experience in this area, we can provide inexpensive and rapid half-life assay service by SNAP-tag to support your protein drugs development.
Introduction of Half-life Assay by SNAP-tag
A powerful approach to characterize the properties of a protein of interest is based on its expression as a fusion protein with an appropriate tag. Fluorescent proteins have been the most widely exploited tags for studies of localization and function of their fusion partners. However, every probe is tailored for a specific protein and application, which required huge investment. SNAP-tag is commonly used to most proteins and convenient to bind target molecules with fluorescent tags.
SNAP-tag is a mutant of human O6-alkylguanine-DNA alkyltransferase (AGT) that permits specific labeling with O6-benzylguanine (BG) derivatives carrying fluorescent probes irreversibly. It has been proven not to affect the function of proteins fusion and used in the pulse-chase labeling previously. The metabolism and side effects of SNAP-tag based half-life assay method have been extensively studied and it is widely accepted due to low toxic, high safety, and strong specificity.
Fig.1 Structure and principle of SNAP-tag protein. (Keppler, 2003)
Applications of Half-life Assay by SNAP-tag
Fig.2 In vivo labeling of tumor-bearing mice with different doses of BG derivatives. (Bojkowska, 2011)
As a widely used protein labeling method, many studies supported that SNAP-tag mediated protein modification showed no major side effect in vivo administration. These properties make SNAP-tag an attractive approach for measuring in vivo protein half-life and distribution in living animals.
By using SNAP-tag attached proteins, some researchers obtained in vivo imaging of fusion proteins in living mice, which showed that the labeling is specific and efficient in most mouse organs. Moreover, with the fluorescent groups labeling on the target proteins, the in vivo protein half-life was determined avoiding mass mice sacrifice. These results guaranteed the effectiveness and universality of SNAP-tag based half-life assay.
Highlights of Half-life Assay by SNAP-tag
- Low toxicity allowing high in vivo probe concentrations
- high specificity and strong binding
- Maintain the function of proteins
- Commonly suitable to most proteins
Half-life assay by SNAP-tag provides a convenient and rapid method to measure proteins pharmaceutical properties as well as visual tracking of protein distribution in vivo. If you are interested in our half-life assay services by SNAP-tag, please feel free to contact us.
References
- Keppler, A.; et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nature biotechnology. 2003, 21(1), 86-89.
- Bojkowska, K.; et al. Measuring in vivo protein half-life. Chemistry & biology. 2011, 18(6), 805-815.
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For Research Use Only. Not for Clinical Use.