Peptides

Catalogue peptide; min. 95% purity

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

Endogenous heptapetide which causes vasodilation and has anti-hypertensive properties.

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Peptide H-ASCLYGQLPK-OH is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice.

FluM1 (58-66) is a short part of the matrix protein of Influenza A virus which is the most abundant component of this enveloped virus localized under the viral lipid envelope. The GILGFVFTL epitope is highly conserved in Influenza A virus strains at a rate of 93% for 69 strains tested. Human Influenza epitopes may bind MHC molecules and then may be recognized by CD8+ cytotoxic T cells. Applications of FluM1 (58-66): FluM1 (58-66) is used to stimulate CTL responses in peripheral blood mononuclear cells (PBMCs). Then, ELISPOT assay is used to quantify peptide epitope specificity and IFN-γ releasing effector cells. FluM1 (58-66) has shown CTL responses qualified of immunodominant with restriction by HLA-A*02:01. It has also been detected CTL responses when FluM1 (58-66) is restricted by all HLA-C. Therefore, FluM1 (58-66) may help to understand the reaction of immune system against Influenza virus of each populations having different HLA type. FluM1 (58-66) has indeed prompted research to develop T-cell vaccine strategies capable of inducing specific CTL responses in patients upon immunization with Influenza M1 antigenic epitope. MVA-NP+M1 vaccine use GILGFVFTL epitope and is tested in clinical trial. Potential cross-reactivity with HIV-1 p17 Gag (77-85): Moreover, FluM1 (58-66) share similarities with HIV-1 p17 Gag (77-85) which can potentially show a cross-reactivity between these epitopes. It has been demonstrated a cross-reactivity and results suggest that immunity following infection by Influenza virus causes specific immune response to HIV-1 p17 Gag (77-85).

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