Peptídeos

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Myelin oligodendrocyte glycoprotein (MOG) is a myelin protein found in the central nervous system. MOG is a ligand for CD200, which is an inhibitory receptor expressed by astrocytes. It has been shown that MOG can induce the proliferation and differentiation of primary cultures of rat astrocytes in vitro. MOG induces the production of reactive oxygen species in mitochondria and increases the expression of acid-binding protein, which are both important factors in the demyelination process. MOG has also been implicated as a potential factor in the development of multiple sclerosis. Further research into this protein may lead to new treatments or cures for disorders such as encephalomyelitis, nervous system diseases, or even cancer.

Extraordinary strength of the streptavidin-biotin interaction allows for efficient capturing of even highly dilute targets; however, it makes recovery of proteins from affinity resins challenging. Conventional methods to elute biotinylated proteins from immobilized avidin include the following: (i) denaturation of streptavidin by boiling the resin in a denaturing buffer that may include high concentrations of chaotropic salts, (ii) trypsin digestion of proteins while they are bound to the resin, or (iii) elution of proteins with excess free biotin. These protocols can co-elute contaminant proteins by releasing nonspecifically bound proteins and/or naturally biotinylated proteins concurrently with labeled proteins. In addition, some of these methods can cause elution of high levels of resin-based peptides along with the proteins of interest, resulting in further sample contamination.
Disulfide Biotin Azide probe eliminates a major limitation of the streptavidin-biotin affinity purification. This reagent contains a biotin moiety linked to an azide moiety through a spacer arm containing a cleavable disulfide linker. Captured biomolecules can be efficiently released under mild conditions (50 mM dithiothreitol, 10 mM 2-mercaptoethanol or 1% sodium borohydride) and the small molecular fragment (188.25 Da) left on the labeled protein following cleavage. These features make the cleavable probe especially attractive for use in biomolecular labeling and proteomic studies.

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity