Peptidi

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

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

CJC-1295 is a synthetic peptide, which is an analogue of growth hormone-releasing hormone (GHRH). It is synthesized through recombinant DNA technology, which allows for precise control over its sequence and length. This particular peptide is designed to bind to GHRH receptors in the pituitary gland. By activating these receptors, CJC-1295 stimulates the release of growth hormone (GH) into the bloodstream.The primary function of CJC-1295 is to influence the endocrine system, particularly enhancing the release of endogenous growth hormone. It achieves this by increasing the amplitude and frequency of GH pulses without affecting the natural negative feedback mechanisms that regulate GH production. This mode of action distinguishes CJC-1295 from other growth hormone therapies, as it promotes a more physiological pattern of hormone secretion.CJC-1295 is used in various scientific contexts, primarily in research focusing on growth hormone deficiencies, muscle wasting conditions, and certain metabolic disorders. Its ability to increase GH release also makes it a subject of interest in studies related to aging, tissue repair, and regeneration. The longer half-life of CJC-1295 compared to natural GHRH peptides further enhances its applications in research, allowing for more sustained and controlled experimentation.

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

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