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How should the ends of the peptide be handled? Keep it free or block it?

Peptides are used to simulate proteins. In order to mimic the performance of proteins, we need to synthesize polypeptides with similar structures and charges to proteins. When a peptide is "cut out" from a protein, the number of charges at both ends will be different from that of the gene body protein. We need to change the compositing strategy to make them consistent.

In general: If the sequence is from the C-terminus of the protein, shield the N-terminus by acetylation; if it is a sequence from the N-terminus of the protein, shield the C-terminus by amidation; if it is from the middle part of the protein, use acetylation and amidation to shield the Both ends are shielded.

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How is the purity of peptides calculated?

KS-V Peptide is obtained by calculating the purity of the peptide by measuring the ultraviolet absorption value of the peptide bond in the target at a specific absorption wavelength by reversed-phase high-performance liquid chromatography (RP-HPLC), and is separated and purified by gradient elution with water and acetonitrile . Among them, moisture and residual salt cannot be measured by UV detector, and there are other impurities in the test results, including incomplete sequence peptides (short peptides with one or more amino acid residues less than the target peptide), truncated sequences due to preventing Generation of incomplete sequence peptides (polypeptides produced by capping), incompletely deprotected peptides (polypeptides produced during synthesis or final cleavage).

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KS-V Peptide

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