I peptidi nella cura della pelle
I peptidi sono brevi catene di amminoacidi. Nelle liste INCI il loro nome contiene di solito «peptide», spesso legato a un acido grasso (per esempio palmitoyl).
674 ingredienti
SR-DOG POLYPEPTIDE-1
sr-Dog Polypeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Epidermal Growth Factor derived from dog. The protein contains a maximum of 1216 amino acids and consists of the proper sequence of the 20 standard amino acids.
SR-DOG POLYPEPTIDE-2
sr-Dog Polypeptide-2 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Vascular Endothelial Growth Factor A derived from dog. The parent protein contains a maximum of 214 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-DOG POLYPEPTIDE-3
sr-Dog Polypeptide-3 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Fibroblast Growth Factor 2 derived from dog. The parent protein contains a maximum of 187 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-DOG POLYPEPTIDE-4
sr-Dog Polypeptide-4 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Insulin-Like Growth Factor derived from dog. The parent protein contains a maximum of 153 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-ESCHERICHIA COLI METHIONYL COW POLYPEPTIDE-3 FERMENT LYSATE EXTRACT
sr-Escherichia Coli Methionyl Cow Polypeptide-3 Ferment Lysate Extract is the extract of the lysed cells obtained by the fermentation of E. coli which contains the fusion peptide consisting of sr-Cow Polypeptide-3 and Methionine.
SR-ESCHERICHIA COLI POLYPEPTIDE-1 TRIPEPTIDE-64 SR-SILKWORM POLYPEPTIDE-1 SH-POLYPEPTIDE-50 OLIGOPEPTIDE-144 HEXAPEPTIDE-40
sr-Escherichia Coli Polypeptide-1 Tripeptide-64 sr-Silkworm Polypeptide-1 sh-Polypeptide-50 Oligopeptide-144 Hexapeptide-40 is a single chain synthetic fusion peptide produced by fermentation in E. coli. The starting gene is synthesized by the fusion of the gene from sr-Escherichia Coli Polypeptide-1, sr-Silkworm Polypeptide-1, Tripeptide-64, sh-Polypeptide-50, Oligopeptide-144 and Hexapeptide-40. The fusion peptide contains 884 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 amino acids.
SR-HAGFISH POLYPEPTIDE-1
sr-Hagfish Polypeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Thread Biopolymer Filament Subunit Alpha derived from hagfish. The protein contains a maximum of 643 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-HORSE OLIGOPEPTIDE-1
sr-Horse Oligopeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Epidermal Growth Factor derived from horse. The protein contains a maximum of 89 amino acids and consists of the proper sequence of the 20 standard amino acids.
SR-HYDROZOAN POLYPEPTIDE-1
sr-Hydrozoan Polypeptide-1 is a single chain recombinant protein fragment produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Fibrillar Collagen derived from Podocoryna carnea (hydrozoan). The parent protein contains a maximum of 429 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-HYMENOBACTER POLYPEPTIDE-1
sr-Hymenobacter Polypeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Deoxyribodipyrimidine Photo-lyase derived from Hymenobacter sp. UV11. The parent protein contains 437 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-JELLYFISH POLYPEPTIDE-1
sr-Jellyfish Polypeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Green Fluorescent Protein derived from jellyfish. The protein contains a maximum of 238 amino acids and consists of the proper sequence of the 20 standard amino acids.
SR-JELLYFISH POLYPEPTIDE-1 SH-OLIGOPEPTIDE-1
sr-Jellyfish Polypeptide-1 sh-Oligopeptide-1 is a single chain synthetic fusion peptide, produced by fermentation in E. coli. The starting gene is synthesized by the fusion of the gene from sr-Jellyfish Polypeptide-1 and sh-Oligopeptide-1. The fusion peptide contains 291 amino acids and consists of the proper sequence of the 20 standard amino acids..
SR-MOUSE POLYPEPTIDE-1
sr-Mouse Polypeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Epidermal Growth Factor derived from mouse. The protein contains a maximum of 1217 amino acids and consists of the proper sequence of the 20 standard amino acids.
SR-MOUSE POLYPEPTIDE-5
sr-Mouse Polypeptide-5 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Immunoglobulin Heavy Chain Variable Region derived from mouse. The parent protein contains a maximum of 249 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-MOUSE POLYPEPTIDE-6
sr-Mouse Polypeptide-6 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Leukemia Inhibitory Factor derived from mouse. The parent protein contains a maximum of 203 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-MUSSEL DECAPEPTIDE-1
sr-Mussel Decapeptide-1 is a single chain peptide recombinantly produced by fermentation in E. coli. The starting gene is synthesized based on a 10 amino acid sequence from Adhesive Plaque Matrix Protein found in mussel, Mytilus galloprovincialiss. The parent protein contains a maximum of 473 amino acids which may contain disulfide bonds and/or glycosylation and consists of the proper sequence of the 20 standard amino acids.
SR-MUSSEL OLIGOPEPTIDE-1
sr-Mussel Oligopeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Polyphenolic Phosphoprotein MEFP-5 found in the mussel, Mytilus edulis. Polyphenolic Phosphoprotein MEFP-5 contains a maximum of 1245 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-MUSSEL OLIGOPEPTIDE-4
sr-Mussel Oligopeptide-4 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthesized to be identical to the gene which codes for Foot Protein-5 found in the mussel, Mytilus californianus. The parent protein contains a maximum of 96 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-MUSSEL POLYPEPTIDE-3
sr-Mussel Polypeptide-3 is a single chain recombinant mussel peptide, produced by fermentation in Pichia pastoris or E. coli. The starting gene is synthesized to be identical to the gene which codes for Foot Protein-6 derived from mussel. The parent protein contains a maximum of 122 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-MUSSEL POLYPEPTIDE-5
sr-Mussel Polypeptide-5 is a single chain recombinant mussel peptide, produced by fermentation in Pichia. The starting gene is synthesized to be identical to the gene which codes for Adhesive Plaque Matrix Protein derived from mussel. The parent protein contains a maximum of 565 amino acids which may contain disulfide bonds and/or glycosylation, and consists of the proper sequence of the 20 standard amino acids.
SR-OCTA SH-POLYPEPTIDE-69
sr-Octa sh-Polypeptide-69 is a single chain recombinant peptide, produced by fermentation in either E. coli or Pichia. The starting gene is synthesized by the fusion of eight repeats of sh-Polypeptide-69. The peptide contains 240 amino acids which may contain disulfide bonds and/or glycosylation and consists of the proper sequence of the 20 standard amino acids.
SR-OCTAPEPTIDE-1
sr-Octapeptide-1 is a single chain recombinant protein produced by fermentation in E. coli that consists of arginine, asparagine, aspartic acid, glycine, proline, tryptophan and tyrosine. The starting gene is synthetically produced, and consists of the 20 standard amino acids.
SR-OLIGOPEPTIDE-1
sr-Oligopeptide-1 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthetically produced, and the final peptide contains 91 amino acids consisting of the 20 standard amino acids.
SR-OLIGOPEPTIDE-193
sr-Oligopeptide-193 is a single chain recombinant protein produced by fermentation in E. coli. The starting gene is synthetically produced. The peptide contains 11 amino acids consisting of arginine, cysteine, glycine, leucine, lysine, proline and serine which may contain disulfide bonds and/or glycosylation.
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