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Genesis Biotech Inc.
 Chemical Modification
 
Chemical Modification
Genesis Biotech Inc. provides a wide variety of choices for modifications ,it can Match 
your specific needs. That includes N-terminal Acylation, C-terminal Amidation,Biotion, 
Cylization, Disulfide Bridge, Phosphorylation, Fatty acid etc.In addition, Peptide 
modifications is an essential task in biological sciences, this modification makes the 
resulting peptide more stable towards enzymatic degradation resulting from exopeptidases. 

1.Phosphorylation 
Phosphopeptides can assist in the investigation of the influences of phosphorylation on peptides and protein structure and in the understanding of regulatory processes mediated by protein kinases. Utilizing our optimized Fmoc and Boc methodologies, Utilizing our optimized Fmoc and Boc methodologies, Genesis Biotech Inc. has successfully synthesized numerous serine-,threonine-,and
tyrosine- phosphopeptides. For peptides containing one or more of these hydroxy-amino acids,selective phosphorylation can be achieved by orthogonal protection or by Fmoc-protected phosphorylated amino acids. Use of such peptides can determine how a cell responds to extracellular signals and how they produce intracellular responses. The specificity of the post-translational phosphorylation is critical in this kind of research. In addition, phospho-specific antibodies made from phospho peptides are used to detect changes in the phosphorylation of specific proteins at a specific site.
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2.Amidation and Acetylation 
If the peptide is from an internal sequence of a protein, terminal amidation (C-terminus) 
or acetylation (N-terminus) will remove its charge and help it imitate its natural 
structure (amide, CONH2). In addition, this modification makes the resulting peptide more 
stable towards enzymatic degradation resulting from exopeptidases. 

3.Biotin and FITC 
Fluorescein isothiocyanate (FITC) is an activated precursor used for fluorescein labeling. 
For efficient N-terminal labeling, a seven-atom aminohexanoyl spacer 
(NH2-CH2-CH2-CH2-CH2-CH2-COOH) is inserted between the fluorophore (fluoroscein) and the 
N-terminus of the peptide. For C-terminal labeling of biotin, a Lys residue is added to 
the C-terminus of the peptide. Biotin is then attached to the lysine side chain via amide
bond. The positive charge of the lysine is then removed. 

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