Péptidos

Z-Ala-Arg-Arg-AMC hydrochloride salt is a synthetic amino acid that inhibits aminopeptidase activity. It is used to study the enzyme's role in the degradation of muscle proteins, and as a pharmaceutical drug for treating inflammatory bowel disease. The target enzyme is inhibited by binding to its active site, thereby preventing the breakdown of peptides. Z-Ala-Arg-Arg-AMC hydrochloride salt can be used as an inhibitor in the laboratory because it prevents denaturation of protein samples during analysis using electrophoresis or chromatography. This product also has been shown to have inhibitory effects on ileal aminopeptidases and prostate aminopeptidases, which may be due to its ability to bind to these enzymes and block their active sites.

Catalogue peptide; min. 95% purity

Catalogue peptide; min. 95% purity

This activated peptide-cleavable linker has an extended functionality linked to the Gly in the peptide sequence. This is quite useful in conjugation in enzymatically cleavable environments inside target cells for controlled release of the drug or payload.

Peptide H-SIYRYYGL-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.

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

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

Boc-Lys(Tfa)-AMC is a small molecule that inhibits the acetylation of histone H3 and has anticancer activity. Acetylation increases the rate of transcription and replication, whereas Boc-Lys(Tfa)-AMC inhibits this process by preventing acetylation. This drug also binds to δ-opioid receptors in cancer cells, triggering a redox signal that leads to inhibition of cancer cell proliferation. The mechanism of this drug's anticancer activity is unknown, but it may be due to its ability to inhibit enzyme activities or disulfide bond formation in vivo.

Please enquire for more information about H-Ala-Abu-OH including the price, delivery time and more detailed product information at the technical inquiry form on this page

Catalogue peptide; min. 95% purity